PMID- 12953803
UI  - 22834262
OWN - NLM
STAT- in-process
DA  - 20030904
IS  - 0925-5710
VI  - 78
IP  - 2
DP  - 2003 Aug
TI  - Survival and proliferation factors of normal and malignant plasma cells.
PG  - 106-13
AB  - Since the first identification of interleukin (IL)-6 as a myeloma cell
      growth factor by Dr. Kawano's and Dr. Klein's groups 14 years ago,
      numerous studies have emphasized its major roles in the emergence of
      malignant plasma cells in vivo and in the generation of normal plasma
      cells. Four transcription factors control B-cell differentiation into
      plasma cells. The B-cell transcription factor pax-5 is mainly responsible
      for a B-cell phenotype, and bcl-6 represses the plasma cell transcription
      factor blimp-1 and plasma cell differentiation. bcl-6 expression is
      triggered by CD40 and IL-4 activation. A lack of CD40 and IL-4 activation
      yields a down-regulation of bcl-6 expression, and IL-6 stimulation yields
      an up-regulation of blimp-1, mainly through STAT3 activation. Blimp-1
      further down-regulates bcl-6 and pax-5 expression and makes plasma cell
      differentiation possible. IL-6 as well as IL-10 up-regulate XBP-1. XBP-1
      is another transcription factor that is involved in plasma cell
      differentiation and whose gene expression is shut down by pax-5. The
      plasma cell transcription factors blimp-1 and XBP-1 are up-regulated, and
      the B-cell transcription factors bcl-6 and pax-5 are down-regulated, in
      malignant cells compared to B-cells. Apart from the recent identification
      of these 4 transcription factors, the factors involved in normal plasma
      cell generation are mostly unknown. Regarding malignant plasma cells, 3
      categories of growth factors have been identified: (1) the IL-6 family
      cytokines, IL-10, and interferon alpha that activate the Janus
      kinase-signal transducer and activator of transcription (JAK/STAT) and
      mitogen-activated protein (MAP) kinase pathways; (2) growth factors
      activating the phosphatidylinositol (PI)-3 kinase/AKT and MAP kinase
      pathways, unlike the JAK/STAT pathway (insulin-like growth factor 1,
      hepatocyte growth factor, and members of the epidermal growth factor
      family able to bind syndecan-1 proteoglycan); and (3) B-cell-activating
      factor (BAFF) or proliferation-inducing ligand (APRIL) that activate the
      nuclear factor KB and PI-3 kinase/AKT pathways. BAFF and APRIL bind to
      BAFF receptor and TACI and are major B-cell survival factors. Recent data
      indicate that these various growth factors may cooperate to provide
      optimum signaling because they are localized together and with cytoplasmic
      transduction elements in caveolinlinked membrane caveolae. The
      identification of these myeloma cell growth factors and of the associated
      transduction pathways should provide novel therapeutic targets in multiple
      myeloma.
AD  - INSERM U475 and Unit for Cellular and Gene Therapy, CHU Montpellier,
      Montpellier, France. klein@montp.inserm.fr
FAU - Klein, Bernard
AU  - Klein B
FAU - Tarte, Karin
AU  - Tarte K
FAU - Jourdan, Michel
AU  - Jourdan M
FAU - Mathouk, Karene
AU  - Mathouk K
FAU - Moreaux, Jerome
AU  - Moreaux J
FAU - Jourdan, Eric
AU  - Jourdan E
FAU - Legouffe, Eric
AU  - Legouffe E
FAU - De Vos, John
AU  - De Vos J
FAU - Rossi, Jean Francois
AU  - Rossi JF
LA  - eng
PT  - Journal Article
PL  - Ireland
TA  - Int J Hematol
JID - 9111627
SB  - IM
EDAT- 2003/09/05 05:00
MHDA- 2003/09/05 05:00
PST - ppublish
SO  - Int J Hematol 2003 Aug;78(2):106-13.

UI  - 0
PMID- 12947106
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030829
IS  - 1083-351X
DP  - 2003 Aug 28
TI  - Normal human keratinocytes bind to alpha 3LG4/5 domain of unprocessed
      laminin-5 through the receptor syndecan-1Fz.
AB  - Basal keratinocytes of the epidermis adhere to their underlying basement
      membrane through a specific interaction with laminin-5, which is composed
      by the association of alpha3, beta3 and gamma2 chains. Laminin-5 has the
      ability to induce either stable cell adhesion or migration depending on
      specific processing of different part of the molecule. One event results
      in the cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5)
      of the alpha3 chain. In this study, we have recombinantly expre ssed the
      human alpha3LG4/5 fragment in mammalian cells and we show that this
      fragment induces adhesion of normal human keratinocytes and
      fibrosarcoma-derived HT1080 cells in a heparan and chondroitin
      sulfate-dependent manner. Immunoprecipitation ex periments with
      Na(2)[(35)S]O(4)-labelled keratinocyte and HT1080 cell lysates, as well as
      immunoblotting experiments, revealed that the major proteoglycan receptor
      for the alpha3LG4/5 fragment is syndecan-1. Syndecan-4 from keratinocytes
      also bound to alpha3LG4/5. Furthermore, we could show for the first time
      that unprocessed laminin-5 specifically binds syndecan-1 while processed
      laminin-5 does not. These results demonstrate that the LG4/5 modules
      within unprocessed laminin-5 permit its cell binding activity through
      heparan and chondroitin sulfate chains of syndecan-1 and reinforce
      previous data suggesting specific properties for the precursor molecule.
AD  - Institut de Biologie et Chimie des Proteines, CNRS, UMR-5086, IFR 128
      Biosciences Lyon-Gerland, Lyon 69 367.
AU  - Okamoto O
AU  - Bachy S
AU  - Odenthal U
AU  - Bernaud J
AU  - Rigal D
AU  - Lortat-Jacob H
AU  - Smyth N
AU  - Rousselle P
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - J Biol Chem
JID - 2985121R
EDAT- 2003/08/30 05:00
MHDA- 2003/08/30 05:00
AID - 10.1074/jbc.M300726200 [doi]
AID - M300726200 [pii]
PST - aheadofprint
SO  - J Biol Chem 2003 Aug 28;.

PMID- 12935821
UI  - 22818441
OWN - NLM
STAT- in-process
DA  - 20030825
IS  - 0945-053X
VI  - 22
IP  - 4
DP  - 2003 Jun
TI  - An extracellular matrix-specific microarray allowed the identification of
      target genes downstream of discoidin domain receptors.
PG  - 373-81
AB  - The two discoidin domain receptors, DDR1 and DDR2, are tyrosine kinases
      that are activated by collagen and are essential regulators of cell-matrix
      communication. However, the target genes downstream of activated DDRs and
      their physiological significance are largely unknown. Here, we describe a
      novel method to dissect signaling pathways induced by extracellular matrix
      (ECM) receptors. Using the doxycycline-inducible repression system
      (tet-off), we generated human fibrosarcoma and mouse fibroblast cell lines
      over-expressing DDR1 or DDR2. These cell lines were employed for gene
      expression analysis using microarrays specific for human and mouse genes
      coding for ECM proteins or ECM-interacting factors. We found that
      approximately 10% of the genes studied were up- or down-regulated more
      than twofold in response to signals generated by over-expressing DDRs. A
      common event downstream of DDR1 and DDR2 in human and mouse cells was the
      up-regulation of P-selectin glycoprotein ligand. Key target genes
      repressed upon DDR activation were agrin, syndecan-1 and alpha3 integrin.
      ECM-specific microarrays were found a valuable tool to dissect gene
      expression changes induced by collagen-receptor signaling pathways.
AD  - Department of Laboratory Medicine and Pathobiology, University of Toronto,
      Ont., M5S 1A8, Toronto, Canada
FAU - Faraci, Elena
AU  - Faraci E
FAU - Eck, Maresa
AU  - Eck M
FAU - Gerstmayer, Bernhard
AU  - Gerstmayer B
FAU - Bosio, Andreas
AU  - Bosio A
FAU - Vogel, Wolfgang F
AU  - Vogel WF
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Matrix Biol
JID - 9432592
SB  - IM
EDAT- 2003/08/26 05:00
MHDA- 2003/08/26 05:00
AID - S0945053X03000532 [pii]
PST - ppublish
SO  - Matrix Biol 2003 Jun;22(4):373-81.

PMID- 12929127
UI  - 22809562
OWN - NLM
STAT- in-process
DA  - 20030820
IS  - 0360-4012
VI  - 73
IP  - 5
DP  - 2003 Sep 1
TI  - Matrix metalloproteinase-dependent shedding of syndecan-3, a transmembrane
      heparan sulfate proteoglycan, in Schwann cells.
PG  - 593-602
AB  - Schwann cells transiently express the transmembrane heparan sulfate
      proteoglycan syndecan-3 during the late embryonic and early postnatal
      periods of peripheral nerve development. Neonatal rat Schwann cells
      released soluble syndecan-3 into the culture medium by a process that was
      blocked by inhibition of endogenous matrix metalloproteinase activity.
      When Schwann cells were plated on a substratum that binds syndecan-3, the
      released proteoglycan bound to the substratum adjacent to the cell border.
      Membrane-anchored syndecan-3 was concentrated in actin-containing
      filopodia that projected from the lateral edges of the Schwann cell
      membrane. Membrane shedding was specific for syndecan-3 and was not
      observed for the related proteoglycan syndecan-1. Analysis of Schwann
      cells transfected with wild-type and chimeric syndecan-1 and syndecan-3
      cDNAs revealed that membrane shedding was a property of the syndecan-3
      ectodomain. Inhibition of syndecan-3 release significantly enhanced
      Schwann cell adhesion and process extension on dishes coated with the
      non-collagenous N-terminal domain of alpha4(V) collagen, which binds
      syndecan-3 and mediates heparan sulfate-dependent Schwann cell adhesion.
      Matrix metalloproteinase-dependent syndecan-3 shedding was also observed
      in newborn rat peripheral nerve tissue. Syndecan-3 shedding in peripheral
      nerve tissue was age specific, and was not observed during later stages of
      postnatal nerve development. These results demonstrate that Schwann cell
      syndecan-3 is subject to matrix metalloproteinase-dependent membrane
      processing, which modulates the biological function of this proteoglycan.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania.
FAU - Asundi, Vinod K
AU  - Asundi VK
FAU - Erdman, Robert
AU  - Erdman R
FAU - Stahl, Richard C
AU  - Stahl RC
FAU - Carey, David J
AU  - Carey DJ
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Neurosci Res
JID - 7600111
SB  - IM
EDAT- 2003/08/21 05:00
MHDA- 2003/08/21 05:00
AID - 10.1002/jnr.10699 [doi]
PST - ppublish
SO  - J Neurosci Res 2003 Sep 1;73(5):593-602.

PMID- 12926067
UI  - 22807563
OWN - NLM
STAT- in-process
DA  - 20030820
IS  - 0250-7005
VI  - 23
IP  - 4
DP  - 2003 Jul-Aug
TI  - Large matrix proteoglycans, versican and perlecan, are expressed and
      secreted by human leukemic monocytes.
PG  - 3303-9
AB  - THP-1 is a monocytic cell line originally derived from a patient with
      acute monocytic leukemia. Interactions of THP-1 cells with other cells and
      their microenvironment are largely determined by proteoglycans (PGs), the
      identity of which has not been determined. Previous studies on
      glycosaminoglycan expression by THP-1 cells and peripheral blood
      mononuclear cells from healthy individuals showed that both cell types
      secrete mainly chondroitin sulfate PGs to the culture medium, whereas
      heparan sulfate PGs are mainly retarded at the cell membrane. However,
      limited data on the type of PGs synthesized by THP-1 is available. In this
      study, the identification of PG types synthesised by THP-1 cells, which
      are not differentiated to macrophages, was examined. Analysis at the mRNA
      level by RT-PCR showed the expression of six cell membrane-associated PGs:
      syndecan-1, -2 and -4, glypican-1, thrombomodulin and CD44. Cell
      extraction, ion-exchange chromatography and dot blot analysis of the
      isolated PG populations with monoclonal antibodies showed the presence of
      syndecan-1 and thrombomodulin; the other two syndecans were not detected
      in any of the isolated populations. The synthesis of matrix PGs was also
      studied. THP-1 monocytes were positive for the mRNA encoding for versican
      and perlecan, but not for those encoding for decorin, biglycan, betaglycan
      and fibromodulin. The mRNA encoding for two versican splice variants V0
      (351 bp) and V1 (386 bp), but not for V2, were identified. Biochemical
      analysis showed the presence of perlecan and of two populations of
      versican in culture medium with protein cores of average molecular sizes
      similar to those of V0 and V1. The production of these large matrix PGs by
      THP-1 monocytes is reported for the first time and may be of importance in
      monocyte malignant transformation and differentiation.
AD  - Department of Chemistry, Section of Organic Chemistry, Biochemistry &
      Natural Products, University of Patras, 26500 Patras, Greece.
FAU - Makatsori, Evdokia
AU  - Makatsori E
FAU - Lamari, Fotini N
AU  - Lamari FN
FAU - Theocharis, Achilleas D
AU  - Theocharis AD
FAU - Anagnostides, Stavros
AU  - Anagnostides S
FAU - Hjerpe, Anders
AU  - Hjerpe A
FAU - Tsegenidis, Theodore
AU  - Tsegenidis T
FAU - Karamanos, Nikos K
AU  - Karamanos NK
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JID - 8102988
SB  - IM
EDAT- 2003/08/21 05:00
MHDA- 2003/08/21 05:00
PST - ppublish
SO  - Anticancer Res 2003 Jul-Aug;23(4):3303-9.

PMID- 12920224
UI  - 22801386
OWN - NLM
STAT- in-process
DA  - 20030815
IS  - 0893-3952
VI  - 16
IP  - 8
DP  - 2003 Aug
TI  - Induced expression of syndecan-1 in the stroma of head and neck squamous
      cell carcinoma.
PG  - 796-801
AB  - Syndecan-1 (CD138), a cell-surface heparan sulfate proteoglycan, is
      involved in cell-cell, cell-matrix interaction and growth factor binding.
      Loss of expression of syndecan-1 in tumor cells leads to decreased
      intercellular cohesion, increased potential for tumor invasiveness, and
      metastatic spread. Furthermore, induction of syndecan-1 expression in the
      tumor stroma has been postulated to promote tumor angiogenesis via its
      binding to growth factors such as basic fibroblast growth factor. Although
      syndecan-1 expression within tumor cells has been investigated in head and
      neck squamous cell carcinoma, stromal expression has not been studied in
      detail. We analyzed 38 cases of head and neck squamous cell carcinoma by
      immunohistochemical staining for syndecan-1 expression within the stroma.
      The expression of syndecan-1 within tumor cells of various histologic
      grades of differentiation, squamous cell carcinoma in situ cells, and
      benign squamous epithelium was also determined. Variable levels of
      diminished syndecan-1 expression were noted within the dysplastic cells of
      9 of 16 (60%) squamous cell carcinoma in situ lesions and in all 38 (100%)
      invasive squamous cell carcinoma. In general, higher levels of syndecan-1
      expression were observed in the well-differentiated tumors, in contrast to
      significant reduction of expression seen in poorly differentiated tumors.
      Syndecan-1 expression was observed within the stroma (in fibroblasts)
      surrounding infiltrating carcinoma cells in 28 of 38 (74%) cases. The
      intensity of syndecan-1 staining within the stroma showed generally an
      inverse correlation with the degree of tumor cell differentiation.
      Syndecan-1 expression was not detected in the stroma beneath normal
      squamous epithelium or adjacent to areas of squamous cell carcinoma in
      situ. We conclude that induced expression of syndecan-1 in the stroma
      surrounding tumor cells of invasive head and neck squamous cell carcinoma
      is a frequent event. The increased stromal syndecan-1 expression, coupled
      with its loss from the surface of carcinoma cells, may contribute to tumor
      cell invasion and the development of metastases.
AD  - Department of Pathology, University of Arkansas for Medical Sciences and
      Central Arkansas Veterans Healthcare System, Little Rock, Arkansas 72205,
      USA. mukunyadziperkins@uams.edu
FAU - Mukunyadzi, Perkins
AU  - Mukunyadzi P
FAU - Liu, Kela
AU  - Liu K
FAU - Hanna, Ehab Y
AU  - Hanna EY
FAU - Suen, James Y
AU  - Suen JY
FAU - Fan, Chun-Yang
AU  - Fan CY
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Mod Pathol
JID - 8806605
SB  - IM
EDAT- 2003/08/16 05:00
MHDA- 2003/08/16 05:00
PST - ppublish
SO  - Mod Pathol 2003 Aug;16(8):796-801.

PMID- 12917256
UI  - 22798842
OWN - NLM
STAT- in-process
DA  - 20030814
IS  - 0953-8178
VI  - 15
IP  - 9
DP  - 2003 Sep
TI  - Increased plasma cell frequency and accumulation of abnormal
      syndecan-1plus T-cells in Igmu-deficient/lpr mice.
PG  - 1045-52
AB  - The expression of muH chain is an important checkpoint in B cell
      development. In mice deficient for IgM transmembrane tail exons (muMT
      mice) B cell development is blocked at the pro-B stage. However, we showed
      that Fas-deficient muMT mice (muMT/lpr) develop a very small population of
      isotype-switched B cells and produce high titers of self-reactive serum
      antibodies. In addition, muMT/lpr mice develop severe lymphoproliferation
      and both pathologic processes occur at young ages. This may suggest that
      lack of Fas-Fas ligand signaling exacerbates murine lupus in B cell
      lymphopenic mice. To test this we analyzed antibody and plasma cell
      formation, and accumulation of abnormal T cells in muMT/lpr mice. Our
      results show that the muMT/lpr mouse is particularly permissive for the
      development and accumulation of antibody-producing cells, thereby
      explaining the high titers of serum antibodies in these mice. In addition,
      we found that accumulating cells in spleen and lymph nodes of muMT/lpr
      mice are alphabeta T cells expressing the abnormal B220+/CD3+ surface
      markers, a phenotype also described for other Fas-deficient mouse models.
      Strikingly, we found that accumulating cells in muMT/lpr mice express the
      membrane proteoglycan syndecan-1, a known plasma cell marker. Development
      of these cells is blocked in mice deficient for TCRbeta and TCRdelta. We
      also found that both antibody production and lymphoproliferation in
      muMT/lpr mice are Th1 regulated. Our results, therefore, suggest that in
      the muMT/lpr mouse model a small population of isotype-switched B cells is
      sufficient for the initiation and propagation of Th1-regulated murine
      lupus.
AD  - Department of Immunology, Bruce Rappaport Faculty of Medicine,
      Technion-Israel Institute of Technology, Haifa 31096, Israel.
FAU - Seagal, Jane
AU  - Seagal J
FAU - Leider, Nira
AU  - Leider N
FAU - Wildbaum, Gizi
AU  - Wildbaum G
FAU - Karin, Nathan
AU  - Karin N
FAU - Melamed, Doron
AU  - Melamed D
LA  - eng
PT  - Journal Article
PL  - England
TA  - Int Immunol
JID - 8916182
SB  - IM
EDAT- 2003/08/15 05:00
MHDA- 2003/08/15 05:00
PST - ppublish
SO  - Int Immunol 2003 Sep;15(9):1045-52.

UI  - 0
PMID- 12904296
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030807
IS  - 1083-351X
DP  - 2003 Aug 6
TI  - Cleavage of syndecan-1 by membrane-type matrix metalloproteinase-1
      stimulates cell migration.
AB  - The transmembrane heparan sulfate proteoglycan syndecan-1 was identified
      from a human placenta cDNA library by the expression cloning method as a
      gene product which interacts with membrane-type matrix metalloproteinase-1
      (MT1-MMP). Co-expression of MT1-MMP with syndecan-1 in HEK293T cells
      promoted syndecan-1 shedding, and concentration of cell-associated
      syndecan-1 was reduced. Treatment of cells with MMP inhibitor BB-94 or
      tissue inhibitor of MMP (TIMP)-2 but not TIMP-1 interfered with the
      syndecan-1 shedding promoted by MT1-MMP expression. In contrast,
      syndecan-1 shedding induced by 12-O-tetradecanoylphorbol-13-acetate (TPA)
      treatment was inhibited by BB-94 but not by either TIMP-1 or TIMP-2.
      Shedding of syndecan-1 was also induced by MT3-MMP, but not by other
      MT-MMPs. Recombinant syndecan-1 core protein was shown to be cleaved by
      recombinant MT1-MMP or MT3-MMP preferentially at G245-L246 peptide bond.
      HT1080 fibrosarcoma cells stably transfected with the syndecan-1 cDNA
      (HT1080/SDC), which express endogenous MT1-MMP, spontaneously shed
      syndecan-1. Migration of HT1080/SDC cells on collagen-coated dishes was
      significantly slow compared with that of control HT1080 cells. Treatment
      of HT1080/SDC cells with BB-94 or TIMP-2 induced accumulation of
      syndecan-1 on cell surface, concomitant with further retardation of cell
      migration. Substitution of Gly245 of syndecan-1 with Leu significantly
      reduced shedding from HT1080/SDC cells and cell migration. These results
      suggest that the shedding of syndecan-1 promoted by MT1-MMP through the
      preferential cleavage of G245-L246 peptide bond stimulates cell migration.
AD  - Department of Molecular Virology and Oncology, Cancer Research Institute,
      Kanazawa University, Kanazawa, Ishikawa 920-0934.
AU  - Endo K
AU  - Takino T
AU  - Miyamori H
AU  - Kinsen H
AU  - Yoshizaki T
AU  - Furukawa M
AU  - Sato H
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - J Biol Chem
JID - 2985121R
EDAT- 2003/08/09 05:00
MHDA- 2003/08/09 05:00
AID - 10.1074/jbc.M306736200 [doi]
AID - M306736200 [pii]
PST - aheadofprint
SO  - J Biol Chem 2003 Aug 6;.

PMID- 12902511
UI  - 22784267
OWN - NLM
STAT- in-process
DA  - 20030806
IS  - 0022-1767
VI  - 171
IP  - 4
DP  - 2003 Aug 15
TI  - Plasminogen activator inhibitor-1 supports IL-8-mediated neutrophil
      transendothelial migration by inhibition of the constitutive shedding of
      endothelial IL-8/heparan sulfate/syndecan-1 complexes.
PG  - 2057-65
AB  - The endothelium is the primary barrier to leukocyte recruitment at sites
      of inflammation. Neutrophil recruitment is directed by transendothelial
      gradients of IL-8 that, in vivo, are bound to the endothelial cell
      surface. We have investigated the identity and function of the binding
      site(s) in an in vitro model of neutrophil transendothelial migration. In
      endothelial culture supernatants, IL-8 was detected in a trimolecular
      complex with heparan sulfate and syndecan-1. Constitutive shedding of IL-8
      in this form was increased in the presence of a neutralizing Ab to
      plasminogen activator inhibitor-1 (PAI-1), indicating a role for
      endothelial plasminogen activator in the shedding of IL-8. Increased
      shedding of IL-8/heparan sulfate/syndecan-1 complexes was accompanied by
      inhibition of neutrophil transendothelial migration, and aprotinin, a
      potent plasmin inhibitor, reversed this inhibition. Platelets, added as an
      exogenous source of PAI-1, had no effect on shedding of the complexes or
      neutrophil migration. Our results indicate that IL-8 is immobilized on the
      endothelial cell surface through binding to syndecan-1 ectodomains, and
      that plasmin, generated by endothelial plasminogen activator, induces the
      shedding of this form of IL-8. PAI-1 appears to stabilize the
      chemoattractant form of IL-8 at the cell surface and may represent a
      therapeutic target for novel anti-inflammatory strategies.
AD  - School of Pharmacy and Biomedical Sciences, University of Portsmouth,
      Portsmouth, Hampshire, United Kingdom.
FAU - Marshall, Lindsay J
AU  - Marshall LJ
FAU - Ramdin, Lara S P
AU  - Ramdin LS
FAU - Brooks, Teresa
AU  - Brooks T
FAU - DPhil, Peter Charlton
AU  - DPhil PC
FAU - Shute, Janis K
AU  - Shute JK
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JID - 2985117R
SB  - AIM
SB  - IM
EDAT- 2003/08/07 05:00
MHDA- 2003/08/07 05:00
PST - ppublish
SO  - J Immunol 2003 Aug 15;171(4):2057-65.

PMID- 12901703
UI  - 22783241
OWN - NLM
STAT- completed
DA  - 20030806
DCOM- 20030822
IS  - 0022-3069
VI  - 62
IP  - 7
DP  - 2003 Jul
TI  - Heparan sulfate proteoglycans modulate monocyte migration across cerebral
      endothelium.
PG  - 780-90
AB  - Heparan sulfate proteoglycans (HSPGs) are known to participate in a wide
      range of biological events, including cellular trafficking. In this study
      we report that in situ cerebral blood vessels highly express HSPGs. Of the
      syndecan family, syndecan-2 is highly expressed on virtually all brain
      vessels and syndecan-1 and -3 are only present on larger blood vessels.
      These endothelial HSPGs have a functional role in monocyte diapedesis
      across brain endothelium, as assessed in our in vitro adhesion and
      migration assays. Our data indicate that heparin prevents monocyte
      adhesion to brain endothelium by interacting solely with the monocyte.
      Transendothelial migration of monocytes can be prevented by preincubation
      of brain endothelium with heparin by enzymatic removal of heparan sulphate
      side chains or by inhibition of cellular sulfation. Blocking of
      G-protein-dependent signaling in the monocytes prevented monocyte adhesion
      and migration to similar extent, suggesting that G-dependent signaling may
      be involved in HSPG-mediated monocyte adhesion and transendothelial
      migration. Our data demonstrate that brain endothelial HSPGs have a
      modulatory role in the transendothelial migration of monocytes in a direct
      and indirect fashion and may therefore contribute to the formation of
      neuroinflammatory lesions.
AD  - Department of Molecular Cell Biology , Vrije Universiteit Medical Center,
      Amsterdam, The Netherlands.
FAU - Floris, Sarah
AU  - Floris S
FAU - van den Born, Jacob
AU  - van den Born J
FAU - van der Pol, Susanne M A
AU  - van der Pol SM
FAU - Dijkstra, Christine D
AU  - Dijkstra CD
FAU - De Vries, Helga E
AU  - De Vries HE
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Neuropathol Exp Neurol
JID - 2985192R
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Sulfates)
RN  - 149769-25-5 (fibroglycan)
RN  - 9005-49-6 (Heparin)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Animal
MH  - Cell Adhesion/drug effects/physiology
MH  - Cerebral Cortex/blood supply/*metabolism/physiopathology
MH  - Chemotaxis, Leukocyte/drug effects/*physiology
MH  - Disease Models, Animal
MH  - Encephalitis/drug therapy/*metabolism/physiopathology
MH  - Encephalomyelitis, Experimental Autoimmune
MH  - Endothelium, Vascular/drug effects/*metabolism
MH  - Extracellular Matrix/drug effects/metabolism
MH  - GTP-Binding Proteins/antagonists & inhibitors/metabolism
MH  - Heparan Sulfate Proteoglycan/*metabolism
MH  - Heparin/pharmacology
MH  - Male
MH  - Membrane Glycoproteins/*metabolism
MH  - Monocytes/drug effects/*metabolism
MH  - Protein Structure, Secondary/drug effects/physiology
MH  - Proteoglycans/*metabolism
MH  - Rats
MH  - Rats, Inbred Lew
MH  - Rats, Wistar
MH  - Signal Transduction/drug effects/physiology
MH  - Sulfates/antagonists & inhibitors
MH  - Support, Non-U.S. Gov't
EDAT- 2003/08/07 05:00
MHDA- 2003/08/23 05:00
PST - ppublish
SO  - J Neuropathol Exp Neurol 2003 Jul;62(7):780-90.

PMID- 12894525
UI  - 22776783
OWN - NLM
STAT- completed
DA  - 20030804
DCOM- 20030828
IS  - 0250-7005
VI  - 23
IP  - 3B
DP  - 2003 May-Jun
TI  - Growth factors regulate the expression profile of their syndecan
      co-receptors and the differentiation of mesothelioma cells.
PG  - 2435-44
AB  - BACKGROUND: Diffuse malignant pleural mesotheliomas are locally aggressive
      and highly lethal tumors that are becoming more common. The tumor derives
      from pluripotential mesothelial stem cells, which differentiate into
      epithelial or mesenchymal elements. Tumors with a predominantly epithelial
      growth pattern have a better prognosis than the sarcomatous and mixed
      types, the phenotype being important for the biology of the tumor. We have
      previously shown that mesotheliomas express a wide range of cell surface
      heparan sulfate proteoglycans (HSPGs), particularly syndecans, which
      interact with growth factors and matrix components. MATERIALS AND METHODS:
      This study was undertaken to examine the epithelial-mesenchymal transition
      of mesothelioma cells by exposing epithelially-differentiated cells to an
      array of growth factors. Following substitution with TGF-beta 2, EGF,
      FGF-2, IGF-I and PDGF-BB, the expression levels of syndecans-1, -2 and -4
      were monitored at selected times (30 minutes, 6 hours and 18 hours) by
      semi-quantitative RT-PCR and FACS analysis. The morphological appearance
      and proliferation rate of the treated cells was correlated to the PG
      profile obtained and to the subcellular compartmentalization of PGs.
      RESULTS: An early response was obtained only for syndecan-4. Changes in
      the differentiation pattern appeared later. Exposure to EGF and IGF-I
      induced a fibroblast-like morphology, simultaneously with a reduced
      expression of syndecans-1 and 2. TGF-beta 2 enhanced the focal contacts
      and showed a marked up-regulation of syndecan-4 and down-regulation of
      syndecan-1. Interestingly, TGF-beta 2 delayed the nuclear transport of
      syndecan-1 concomitantly with an antiproliferative effect. CONCLUSION:
      Growth factor signalling seems to be delicately controlled by an
      autoregulatory loop involving the syndecan expression levels and amounts
      of soluble HS chains shed into the medium.
AD  - Department of Laboratory Medicine, Division of Pathology, Karolinska
      Institutet, F46, Huddinge University Hospital, S-14186 Huddinge, Sweden.
      katalin.dobra@impi.ki.se
FAU - Dobra, Katalin
AU  - Dobra K
FAU - Nurminen, Mervi
AU  - Nurminen M
FAU - Hjerpe, Anders
AU  - Hjerpe A
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JID - 8102988
RN  - 0 (Growth Substances)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 149769-25-5 (fibroglycan)
SB  - IM
MH  - Cell Differentiation/drug effects/physiology
MH  - Cell Division/physiology
MH  - Cell Nucleus/metabolism
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Growth Substances/*pharmacology
MH  - Human
MH  - Membrane Glycoproteins/biosynthesis/metabolism
MH  - Mesothelioma/*metabolism/*pathology
MH  - Pleural Neoplasms/*metabolism/*pathology
MH  - Proteoglycans/*biosynthesis/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Support, Non-U.S. Gov't
EDAT- 2003/08/05 05:00
MHDA- 2003/08/29 05:00
PST - ppublish
SO  - Anticancer Res 2003 May-Jun;23(3B):2435-44.

PMID- 12883204
UI  - 22766511
OWN - NLM
STAT- completed
DA  - 20030728
DCOM- 20030904
IS  - 0041-1337
VI  - 76
IP  - 2
DP  - 2003 Jul 27
TI  - Increased levels of syndecan-1 in serum during acute graft-versus-host
      disease.
PG  - 423-6
AB  - Acute graft-versus-host disease (GVHD) may affect several organs.
      Syndecan-1 is a heparan sulfate proteoglycan that can be shed from the
      surface of most epithelial cells (skin, liver, and gut among others),
      which are target organs for GVHD. Syndecan-1 was measured in serum samples
      from 60 patients after allogeneic stem-cell transplantation and was
      related to the degree of GVHD. Syndecan-1 levels increased in patients who
      developed acute GVHD but not in patients without GVHD. The difference
      between groups was significant 3 to 10 weeks after transplantation. The
      peak level of syndecan-1 in serum correlated with the degree of acute GVHD
      (r=0.46, P<0.001). Combined, the peak levels of syndecan-1 and soluble
      interleukin-2 receptor detected patients with acute GVHD (sensitivity 82%,
      specificity 89%). This study shows that syndecan-1 levels are increased
      during acute GVHD. Syndecan-1 may be a marker for acute GVHD, especially
      if combined with determination of soluble interleukin-2 receptor.
AD  - Division of Pathology, Department of Laboratory Medicine, Karolinska
      Institute, Huddinge University Hospital, Stockholm, Sweden.
      carina.seidel@labmed.ki.se.
FAU - Seidel, Carina
AU  - Seidel C
FAU - Ringden, Olle
AU  - Ringden O
FAU - Remberger, Mats
AU  - Remberger M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Transplantation
JID - 0132144
RN  - 0 (Biological Markers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Acute Disease
MH  - Adolescent
MH  - Adult
MH  - Biological Markers
MH  - Child
MH  - Child, Preschool
MH  - Epithelial Cells/metabolism
MH  - Female
MH  - Graft vs Host Disease/*blood/*diagnosis
MH  - Human
MH  - Leukemia, Lymphocytic, Acute/blood/therapy
MH  - Leukemia, Myelocytic, Acute/blood/therapy
MH  - Leukemia, Myeloid, Chronic/blood/therapy
MH  - Male
MH  - Membrane Glycoproteins/*blood
MH  - Middle Age
MH  - Proteoglycans/*blood
MH  - Sensitivity and Specificity
MH  - *Stem Cell Transplantation
MH  - Support, Non-U.S. Gov't
EDAT- 2003/07/29 05:00
MHDA- 2003/09/05 05:00
AID - 10.1097/01.TP.0000074316.76104.A5 [doi]
PST - ppublish
SO  - Transplantation 2003 Jul 27;76(2):423-6.

UI  - 0
PMID- 12881311
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030725
IS  - 0006-4971
DP  - 2003 Jul 24
TI  - Complexity within the plasma cell compartment of mice deficient in both E-
      and P-selectin: implications for plasma cell differentiation.
AB  - Antibody secreting plasma cells represent the critical end-stage effector
      cells of the humoral immune response. Here, we show that several distinct
      plasma cell subsets are concurrently present in the lymph nodes, spleen,
      and bone marrow of mice deficient in both E- and P-selectin. One of these
      subsets was a B220-negative IgG plasma cell population expressing low to
      negative surface levels of syndecan-1. Examination of the chemotactic
      responsiveness of IgG plasma cell subsets revealed that migration towards
      SDF-1/CXCL12 was primarily limited to the B220-lo subset regardless of
      tissue source. Although B220-negative plasma cells did not migrate
      efficiently in response to CXCL12 or to other chemokines for which
      receptor mRNA was expressed, these cells expressed substantial surface
      CXCR4, and CXCL12 stimulation rapidly induced ERK1/ERK2 phosphorylation,
      demonstrating that CXCR4 retained signaling capacity. Therefore,
      B220-negative plasma cells exhibit a selective uncoupling of chemokine
      receptor expression and signaling from migration. Taken together, our
      findings document the presence of significant heterogeneity within the
      plasma cell compartment, which suggests a complex step-wise scheme of
      plasma cell differentiation in which the degree of differentiation and
      tissue location can influence the chemotactic responsiveness of IgG plasma
      cells.
AU  - Underhill GH
AU  - Kolli KP
AU  - Kansas GS
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Blood
JID - 7603509
EDAT- 2003/07/26 05:00
MHDA- 2003/07/26 05:00
AID - 10.1182/blood-2003-03-0947 [doi]
AID - 2003-03-0947 [pii]
PST - aheadofprint
SO  - Blood 2003 Jul 24;.

PMID- 12879463
UI  - 22760456
OWN - NLM
STAT- completed
DA  - 20030724
DCOM- 20030814
IS  - 0008-543X
VI  - 98
IP  - 3
DP  - 2003 Aug 1
TI  - High syndecan-1 expression in breast carcinoma is related to an aggressive
      phenotype and to poorer prognosis.
PG  - 474-83
AB  - BACKGROUND: Syndecan-1 is a transmembrane heparan sulphate proteoglycan
      that is involved in cell-cell adhesion, organization of cell-matrix
      adhesion, and regulation of growth factor signaling. METHODS: Specimens
      from 254 consecutive breast carcinoma (BC) cases (110 N0, 144 N1/2) with
      long-term follow-up (median, 95 months) were immunostained for syndecan-1,
      estrogen receptor (ER), progesterone receptor (PgR), and p53; in 154
      cases, c-erbB-2 status was known. Syndecan-1 mRNA and protein expression
      also were evaluated in 20 breast tissue samples (10 normal and tumor
      pairs). RESULTS: Syndecan-1 was expressed at high levels in 106 (42%) BCs;
      syndecan-1 up-regulation was confirmed by reverse transcriptase-polymerase
      chain reaction (RT-PCR) studies. High syndecan-1 expression was associated
      with high histologic grade, large tumor size, high mitotic count, c-erbB-2
      overexpression, and ER and PgR negative status. At univariate survival
      analysis syndecan overexpression was related to poor prognosis (P < 0.01
      for both overall survival (OS) and disease-free survival). Bivariate
      survival analysis showed an additive adverse effect for syndecan-1 and
      c-erbB-2 overexpression. At multivariate analysis, syndecan-1
      overexpression was independently associated with poor OS (hazard ratio
      [HR], 1.71; 95% confidence interval [CI], 1.08-2.69). High syndecan-1
      expression also was of independent prognostic value for OS in the group of
      102 ER-negative patients (HR, 2.42; 95% CI, 1.21-4.82). Stratifying
      patients on the basis of the type of adjuvant therapy given, high
      syndecan-1 expression was associated with a higher risk of death only in
      patients treated with the cyclophosphamide-methotrexate-fluorouracil
      regimen (HR, 1.9; P = 0.09); at multivariate analysis for OS, this
      association proved to be of independent statistical significance (P =
      0.03; HR, 2.15). CONCLUSIONS: Syndecan-1 is expressed at high levels in a
      significant percentage of breast carcinomas and is related to an
      aggressive phenotype and poor clinical behavior.
CI  - Copyright 2003 American Cancer Society.DOI 10.1002/cncr.11515
AD  - Department of Pathology, Santa Chiara Hospital, Trento, Italy.
FAU - Barbareschi, Mattia
AU  - Barbareschi M
FAU - Maisonneuve, Patrick
AU  - Maisonneuve P
FAU - Aldovini, Daniela
AU  - Aldovini D
FAU - Cangi, Maria Giulia
AU  - Cangi MG
FAU - Pecciarini, Lorenza
AU  - Pecciarini L
FAU - Angelo Mauri, Francesco
AU  - Angelo Mauri F
FAU - Veronese, Silvio
AU  - Veronese S
FAU - Caffo, Orazio
AU  - Caffo O
FAU - Lucenti, Antonio
AU  - Lucenti A
FAU - Palma, Paolo Dalla
AU  - Palma PD
FAU - Galligioni, Enzo
AU  - Galligioni E
FAU - Doglioni, Claudio
AU  - Doglioni C
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer
JID - 0374236
RN  - 0 (Antineoplastic Agents)
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (Receptors, Estrogen)
RN  - 0 (Receptors, Progesterone)
RN  - 0 (syndecan)
RN  - EC 2.7.1.112 (Receptor, erbB-2)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma/*metabolism/pathology/therapy
MH  - Antineoplastic Agents/therapeutic use
MH  - Breast Neoplasms/*metabolism/pathology/therapy
MH  - Chemotherapy, Adjuvant
MH  - DNA Primers/chemistry
MH  - Female
MH  - Follow-Up Studies
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Lymphatic Metastasis
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Middle Age
MH  - Prognosis
MH  - Proteoglycans/genetics/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA, Neoplasm/metabolism
MH  - Receptor, erbB-2/genetics/metabolism
MH  - Receptors, Estrogen/genetics/metabolism
MH  - Receptors, Progesterone/genetics/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Stromal Cells/pathology
MH  - Support, Non-U.S. Gov't
MH  - Survival Rate
EDAT- 2003/07/25 05:00
MHDA- 2003/08/15 05:00
AID - 10.1002/cncr.11515 [doi]
PST - ppublish
SO  - Cancer 2003 Aug 1;98(3):474-83.

PMID- 12877731
UI  - 22760758
OWN - NLM
STAT- in-process
DA  - 20030724
IS  - 0309-0167
VI  - 43
IP  - 2
DP  - 2003 Aug
TI  - Syndecan-1 expression in thyroid carcinoma: stromal expression followed by
      epithelial expression is significantly correlated with dedifferentiation.
PG  - 157-64
AB  - AIM: To investigate the expression of syndecan-1 in thyroid neoplasia.
      Syndecan-1 is a proteoglycan regulating cell adhesion. Previous studies
      have demonstrated that decreased expression of syndecan-1 is linked to
      malignant progression. METHODS AND RESULTS: Syndecan-1 expression in
      thyroid neoplasia was studied immunohistochemically. Syndecan-1 was
      expressed in stromal cells as well as neoplastic epithelial cells. Stromal
      syndecan-1 expression was observed more frequently in papillary carcinomas
      larger than 10 mm in size than in microcarcinomas and in widely invasive
      than in minimally invasive follicular carcinomas. Furthermore, poorly
      differentiated carcinomas showed this phenomenon more than
      well-differentiated carcinomas, but the expression in undifferentiated
      carcinomas was similar to that of poorly differentiated carcinomas.
      Epithelial syndecan-1 expression was more frequently observed in
      anaplastic (undifferentiated) carcinomas than in papillary and follicular
      carcinomas. No significant difference in epithelial expression was found
      between well and poorly differentiated carcinomas, but undifferentiated
      carcinomas expressed epithelial syndecan-1 more frequently than did poorly
      differentiated carcinomas. CONCLUSIONS: These results are in contrast to
      those previously reported for carcinomas at other sites. It is suggested
      that the role of syndecan-1 in thyroid carcinomas might be unique. Stromal
      syndecan-1 expression followed by its epithelial expression is
      significantly related to progression, including dedifferentiation of
      thyroid carcinoma.
AD  - Kuma Hospital, Kobe, Japan. ito01@kuma-h.or.jp
FAU - Ito, Y
AU  - Ito Y
FAU - Yoshida, H
AU  - Yoshida H
FAU - Nakano, K
AU  - Nakano K
FAU - Takamura, Y
AU  - Takamura Y
FAU - Miya, A
AU  - Miya A
FAU - Kobayashi, K
AU  - Kobayashi K
FAU - Yokozawa, T
AU  - Yokozawa T
FAU - Matsuzuka, F
AU  - Matsuzuka F
FAU - Matsuura, N
AU  - Matsuura N
FAU - Kuma, K
AU  - Kuma K
FAU - Miyauchi, A
AU  - Miyauchi A
LA  - eng
PT  - Journal Article
PL  - England
TA  - Histopathology
JID - 7704136
SB  - IM
EDAT- 2003/07/25 05:00
MHDA- 2003/07/25 05:00
AID - 1656 [pii]
PST - ppublish
SO  - Histopathology 2003 Aug;43(2):157-64.

PMID- 12871780
UI  - 22754374
OWN - NLM
STAT- in-process
DA  - 20030721
IS  - 0169-5002
VI  - 41
IP  - 2
DP  - 2003 Aug
TI  - Pretreatment serum syndecan-1 levels and outcome in small cell lung cancer
      patients treated with platinum-based chemotherapy.
PG  - 171-7
AB  - Syndecan-1 is a multifunctional transmembrane heparan sulphate
      proteoglycan (HSPG) that is present on a variety of cell types. The
      extracellular syndecan domains can be shed from the cell surface in a
      highly regulated process called ectodomain shedding. We studied the
      influence of soluble syndecan-1 on outcome in 88 small cell lung cancer
      (SCLC) patients treated within the context of two randomised clinical
      trials with platinum-based therapy. Serum syndecan-1 concentrations were
      determined using enzyme-linked immunosorbent assay (ELISA) from sera taken
      prior to initiation of chemotherapy. Patients with the serum syndecan-1
      level within the highest tertile (>212 microg/l) had only 38% 1-year and
      3% 2-year survival, whereas 58% of those with a lower serum level survived
      for 1 year and 25% for 2 years following the diagnosis (P=0.0034). A high
      serum syndecan-1 level (>212 microg/l) was associated with a high
      pretreatment lactate dehydrogenase (LDH) level (P=0.0024) and a poor
      Karnofsky's performance status (P=0.021), but not with the clinical stage
      or the presence of distant metastases at diagnosis. A high serum
      syndecan-1 level had independent influence on survival also in a
      multivariate analysis (the relative risk, RR, 1.68; 95% CI, 1.02-2.77;
      P=0.044) together with the clinical stage (RR, 1.72; 95% CI, 1.05-2.82;
      P=0.032). We conclude that high pretreatment serum syndecan-1 level is
      associated with poor prognosis in SCLC treated with platinum-based
      chemotherapy.
AD  - Department of Oncology, Helsinki University Central Hospital, P.O. Box
      180, FIN-00029, Helsinki, Finland. anu.anttonen@hus.fi
FAU - Anttonen, Anu
AU  - Anttonen A
FAU - Leppa, Sirpa
AU  - Leppa S
FAU - Ruotsalainen, Tarja
AU  - Ruotsalainen T
FAU - Alfthan, Henrik
AU  - Alfthan H
FAU - Mattson, Karin
AU  - Mattson K
FAU - Joensuu, Heikki
AU  - Joensuu H
LA  - eng
PT  - Journal Article
PL  - Ireland
TA  - Lung Cancer
JID - 8800805
SB  - IM
EDAT- 2003/07/23 05:00
MHDA- 2003/07/23 05:00
AID - S016950020300196X [pii]
PST - ppublish
SO  - Lung Cancer 2003 Aug;41(2):171-7.

PMID- 12859973
UI  - 22744250
OWN - NLM
STAT- in-process
DA  - 20030715
IS  - 0006-291X
VI  - 307
IP  - 2
DP  - 2003 Jul 25
TI  - Changes in gene expression induced by H(2)O(2) in cardiac myocytes.
PG  - 416-21
AB  - Oxidative stress induces cardiac myocyte apoptosis. At least some effects
      are probably mediated through changes in gene expression. Using Affymetrix
      arrays, we examined the changes in gene expression induced by H(2)O(2)
      (0.04, 0.1, and 0.2mM; 2 and 4h) in rat neonatal ventricular myocytes.
      Changes in selected upregulated genes were confirmed by ratiometric
      RT-PCR. p21(Cip1/Waf1) was one of the only two genes upregulated in all
      conditions studied. Of the heat shock proteins, only Hsp70/70.1 was
      induced by H(2)O(2) with no change in the expression of Hsp25, Hsp60 or
      Hsp90. Heme oxygenase 1 was also potently upregulated, but not heme
      oxygenases 2 or 3. Of the intercellular adhesion proteins, syndecan-1 was
      significantly upregulated in response to H(2)O(2), with little change in
      the expression of other syndecans and no change in expression of any of
      the integrins studied. Thus, oxidative stress, exemplified by H(2)O(2),
      selectively promotes the expression of specific gene family members.
AD  - NHLI Division (Cardiac Medicine), Faculty of Medicine, Imperial College
      London, London, UK.
FAU - Kemp, Timothy J
AU  - Kemp TJ
FAU - Causton, Helen C
AU  - Causton HC
FAU - Clerk, Angela
AU  - Clerk A
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochem Biophys Res Commun
JID - 0372516
SB  - IM
EDAT- 2003/07/16 05:00
MHDA- 2003/07/16 05:00
AID - S0006291X03012154 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun 2003 Jul 25;307(2):416-21.

PMID- 12824007
UI  - 22707716
OWN - NLM
STAT- completed
DA  - 20030625
DCOM- 20030711
IS  - 1043-4666
VI  - 21
IP  - 5
DP  - 2003 Mar 7
TI  - Regulation of epithelial syndecan-1 expression by inflammatory cytokines.
PG  - 224-33
AB  - Syndecan-1 is expressed on the basolateral surface of columnar epithelium
      and contributes to wound repair by facilitating increased growth factor
      binding. Inflammatory bowel disease (IBD) is associated with reduced
      syndecan-1 expression in areas of inflamed mucosa that is likely to impair
      mucosal healing. Reduced syndecan-1 expression in IBD may be related to
      the presence of increased inflammatory cytokines. To test this hypothesis,
      monolayers of HT29 and T84 colonic epithelial cells were stimulated with
      tumour necrosis factor (TNF)-alpha, interleukin (IL)-1beta or IL-6.
      Stimulation of HT29 cells with TNF-alpha and IL-1beta resulted in
      reversible down-regulation of syndecan-1 at both protein and mRNA levels
      but little effect was observed with IL-6. Loss of syndecan-1 expression
      was caused by shedding of the ectodomain as revealed by increased levels
      of soluble syndecan-1 measured in the conditioned medium of stimulated
      cells. No increase in cytoplasmic staining accompanied the loss of cell
      surface syndecan-1 expression. TNF-alpha and IL-1beta are capable of
      down-regulating syndecan-1 expression and may account in part for the
      reduced expression of syndecan-1 seen in IBD.
AD  - IBD Research Group, St Mark's Hospital, Watford Road, Harrow, Middlesex
      HA1 3UJ, UK. r.day@ic.ac.uk
FAU - Day, Richard M
AU  - Day RM
FAU - Mitchell, Tracey J
AU  - Mitchell TJ
FAU - Knight, Stella C
AU  - Knight SC
FAU - Forbes, Alastair
AU  - Forbes A
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cytokine
JID - 9005353
RN  - 0 (Cytokines)
RN  - 0 (Interleukin-1)
RN  - 0 (Interleukin-6)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (Tumor Necrosis Factor)
RN  - 0 (syndecan)
RN  - 126547-89-5 (Intercellular Adhesion Molecule-1)
SB  - IM
MH  - Cells, Cultured
MH  - Coculture
MH  - Cytokines/*pharmacology
MH  - Epithelial Cells/*drug effects/*metabolism
MH  - Gene Expression Regulation/*drug effects
MH  - Human
MH  - Intercellular Adhesion Molecule-1/analysis
MH  - Interleukin-1/pharmacology
MH  - Interleukin-6/pharmacology
MH  - Leukocytes, Mononuclear/cytology/metabolism
MH  - Membrane Glycoproteins/chemistry/*genetics/metabolism
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/chemistry/*genetics/metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
MH  - Tumor Necrosis Factor/pharmacology
EDAT- 2003/06/26 05:00
MHDA- 2003/07/12 05:00
AID - S1043466603000917 [pii]
PST - ppublish
SO  - Cytokine 2003 Mar 7;21(5):224-33.

PMID- 12811819
UI  - 22695170
OWN - NLM
STAT- completed
DA  - 20030617
DCOM- 20030811
IS  - 0021-9541
VI  - 196
IP  - 2
DP  - 2003 Aug
TI  - CTGF/Hcs24, hypertrophic chondrocyte-specific gene product, interacts with
      perlecan in regulating the proliferation and differentiation of
      chondrocytes.
PG  - 265-75
AB  - Connective tissue growth factor/hypertrophic chondrocyte-specific gene
      product 24 (CTGF/Hcs24) plays important roles in the control of the
      proliferation and differentiation of chondrocytes in vitro. To clarify the
      mechanisms of regulation by CTGF/Hcs24 with respect to cartilage
      metabolism, we investigated the interaction between CTGF/Hcs24 and heparan
      sulfate proteoglycan perlecan. An immunofluorescence study showed that
      CTGF/Hcs24 was colocalized with heparan sulfate and perlecan in human
      chondrosarcoma-derived chondrocytic cell line HCS-2/8 in vitro. Northern
      blot analysis showed that perlecan, syndecan-1, -2, and -4 transcripts
      were detected in HCS-2/8 cells. Particularly, expression of the perlecan
      gene increased markedly in HCS-2/8 cells by recombinant CTGF/Hcs24
      (rCTGF/Hcs24) treatment. We also found that CTGF/Hcs24 interacted with
      perlecan from HCS-2/8 cells in vitro. Furthermore, CTGF/Hcs24-stimulated
      gene expression of the aggrecan gene, as well as DNA/proteoglycan
      synthesis, was diminished when HCS-2/8 cells were pretreated with
      heparinase, indicating that the effects of CTGF/Hcs24 on chondrocytes
      occurred through the interaction between CTGF/Hcs24 and heparan sulfate on
      the cells. An in vivo study using mouse growth plate revealed that
      CTGF/Hcs24 produced by hypertrophic chondrocytes was localized from the
      proliferative to the hypertrophic zone, whereas perlecan was predominantly
      localized in the prehyphertrophic zone. Consistent with such findings in
      vivo, the binding of (125)I-rCTGF/Hcs24 to maturing chondrocytes was at
      higher levels than that to chondrocytes in hypertrophic stages. These
      findings suggest that CTGF/Hcs24 produced in the hypertrophic region may
      act on chondrocytes in the proliferative and maturative zone via some
      heparan sulfate proteoglycan, such as perlecan.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Department of Biochemistry and Molecular Dentistry, Okayama University
      Graduate School of Medicine and Dentistry, Okayama, Japan.
FAU - Nishida, Takashi
AU  - Nishida T
FAU - Kubota, Satoshi
AU  - Kubota S
FAU - Fukunaga, Tomohiro
AU  - Fukunaga T
FAU - Kondo, Seiji
AU  - Kondo S
FAU - Yosimichi, Gen
AU  - Yosimichi G
FAU - Nakanishi, Tohru
AU  - Nakanishi T
FAU - Takano-Yamamoto, Teruko
AU  - Takano-Yamamoto T
FAU - Takigawa, Masaharu
AU  - Takigawa M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Physiol
JID - 0050222
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Ligands)
RN  - 0 (Recombinant Proteins)
RN  - 139568-91-5 (connective tissue growth factor)
RN  - 143972-95-6 (perlecan)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
MH  - Aged
MH  - Animal
MH  - Blotting, Northern
MH  - Cell Differentiation/physiology
MH  - Cell Division/physiology
MH  - Chondrocytes/*cytology
MH  - Heparan Sulfate Proteoglycan/*physiology
MH  - Heparin Lyase/pharmacology
MH  - Human
MH  - Immediate-Early Proteins/*physiology
MH  - Immunologic Techniques
MH  - Intercellular Signaling Peptides and Proteins/*physiology
MH  - Ligands
MH  - Male
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Recombinant Proteins/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
EDAT- 2003/06/18 05:00
MHDA- 2003/08/12 05:00
AID - 10.1002/jcp.10277 [doi]
PST - ppublish
SO  - J Cell Physiol 2003 Aug;196(2):265-75.

PMID- 12782806
UI  - 22667163
OWN - NLM
STAT- completed
DA  - 20030603
DCOM- 20030723
IS  - 0023-852X
VI  - 113
IP  - 6
DP  - 2003 Jun
TI  - Fibronectin and adhesion molecules on canine scarred vocal folds.
PG  - 966-72
AB  - OBJECTIVE: To examine the expressions of fibronectin and other adhesion
      molecules on the scarred vocal folds in a short- and long-term animal
      model. STUDY DESIGN: Animal model. METHODS: Six beagles' vocal folds were
      stripped unilaterally and left untreated. After wounding the vocal folds
      were harvested from three dogs at 2 months and three dogs at 6 months. The
      untouched vocal fold was used as a control, and the stripped vocal fold as
      scarred. Subsequently, the expressions of fibronectin, cadherin,
      syndecan-1 and syndecan-4 on both vocal folds were examined by
      immunohistochemical and image analysis. RESULTS: Compared with the control
      vocal folds, fibronectin significantly increased in the superficial layer
      of the lamina propria on the scarred vocal folds at both 2 and 6 months.
      Co-deposition of collagen was observed only at 6 months. Syndecan-4 was
      significantly overexpressed at the basal layer cells of the epithelium at
      both 2 and 6 months. No significant expression of either cadherin or
      syndecan-1 was detected. CONCLUSIONS: Scar characteristics at 2 and 6
      months are not identical, suggesting that a 2-month period may not be a
      sufficient to study vocal fold scarring. Adhesion molecules are important
      in reorganization of extracellular matrix during wound healing because of
      their binding and adhesion characteristics. The results indicate that
      fibronectin might be important in providing a scaffold for the deposition
      of other proteins such as collagen, and the binding characteristics might
      affect the stiffness of the scarred vocal fold. Prolonged expression of
      syndecan-4 may reflect the role of focal adhesion during the assembly of
      scar structure. Ultimately, better understanding of the histological
      features of the scarred vocal fold might lead to new approaches to
      treatment.
AD  - Department of Surgery, University of Wisconsin-Madison, 53792, USA.
      hirano@surgery.wisc.edu
FAU - Hirano, Shigeru
AU  - Hirano S
FAU - Bless, Diane M
AU  - Bless DM
FAU - Rousseau, Bernard
AU  - Rousseau B
FAU - Welham, Nathan
AU  - Welham N
FAU - Scheidt, Troy
AU  - Scheidt T
FAU - Ford, Charles N
AU  - Ford CN
LA  - eng
GR  - R01DC4428/DC/NIDCD
PT  - Journal Article
PL  - United States
TA  - Laryngoscope
JID - 8607378
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Animal
MH  - Cadherins/analysis
MH  - Cell Adhesion Molecules/*analysis
MH  - Cicatrix/*pathology
MH  - Collagen/analysis
MH  - Disease Models, Animal
MH  - Dogs
MH  - Fibronectins/*analysis
MH  - Immunoenzyme Techniques
MH  - Membrane Glycoproteins/analysis
MH  - Proteoglycans/analysis
MH  - Respiratory Mucosa/pathology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Vocal Cords/*pathology
MH  - Wound Healing/physiology
EDAT- 2003/06/05 05:00
MHDA- 2003/07/24 05:00
PST - ppublish
SO  - Laryngoscope 2003 Jun;113(6):966-72.

PMID- 12782143
UI  - 22667232
OWN - NLM
STAT- in-process
DA  - 20030603
IS  - 0945-053X
VI  - 22
IP  - 2
DP  - 2003 Apr
TI  - Syndecan-1 accumulates in lysosomes of poorly differentiated breast
      carcinoma cells.
PG  - 163-77
AB  - Expression patterns of syndecan-1, the cell surface heparan sulfate
      proteoglycan (HSPG) predominant on epithelial cells, were analyzed in
      tissue samples from 30 infiltrating human breast carcinomas and in 9 human
      breast carcinoma cell lines. Immunohistochemical staining demonstrates
      that while a subset of the breast carcinomas lose syndecan-1, this
      proteoglycan is expressed or overexpressed in a majority of the cases.
      Interestingly, cells in poor grade tumors contain intracellular
      syndecan-1, an observation that has not been previously described and was
      thus further investigated. Examination of cultured breast carcinoma cell
      lines indicates that they also display the phenotype of the syndecan-1
      positive tumors and thereby provide a model system for analysis of
      intracellular syndecan-1. All cell lines examined express syndecan-1, and
      poorly differentiated lines such as BT549 cells internalize the
      proteoglycan from the cell surface where it accumulates as intact HSPG in
      intracellular vesicles. Colocalization studies using fluorescent markers
      identify these to be lysosomes. This finding is unexpected, as the
      accepted mechanism for degradation of syndecan HSPG following endocytosis
      is fragmentation of the protein core and glycosaminoglycan chains in
      endosomes, followed by delivery of the fragments to lysosomes. Lysosomal
      inactivation using ammonium chloride demonstrates that well-differentiated
      lines such as T47D and MCF-7 cells, which maintain the majority of
      syndecan-1 on their cell surfaces, also target intact constitutively
      endocytosed syndecan-1 to lysosomes. Taken together, these results suggest
      that mammary epithelial cells utilize a previously uncharacterized
      mechanism for syndecan-1 catabolism. In this pathway the proteoglycan
      remains intact as it passes through the endosomal system, prior to
      arriving at its site of intracellular degradation in lysosomes.
AD  - Department of Pathology and Laboratory Medicine, University of
      Wisconsin-Madison, 1300 University Avenue, Madison, WI 53706, USA.
FAU - Burbach, Brandon J
AU  - Burbach BJ
FAU - Friedl, Andreas
AU  - Friedl A
FAU - Mundhenke, Christoph
AU  - Mundhenke C
FAU - Rapraeger, Alan C
AU  - Rapraeger AC
LA  - eng
GR  - R01 HD 21881/HD/NICHD
GR  - T32 GM 08688/GM/NIGMS
PT  - Journal Article
PL  - Germany
TA  - Matrix Biol
JID - 9432592
SB  - IM
EDAT- 2003/06/05 05:00
MHDA- 2003/06/05 05:00
AID - S0945053X0300009X [pii]
PST - ppublish
SO  - Matrix Biol 2003 Apr;22(2):163-77.

PMID- 12773479
UI  - 22814021
OWN - NLM
STAT- in-process
DA  - 20030822
IS  - 0959-6658
VI  - 13
IP  - 9
DP  - 2003 Sep
TI  - Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed
      on HeLa cells.
PG  - 623-34
AB  - It is believed that proteoglycans influence biological properties of
      chemokines. We show that the CC chemokine RANTES binds not only to
      high-affinity binding sites on CCR5-positive HeLa cells but also to
      low-affinity binding sites on HeLa cells expressing or lacking RANTES G
      protein-coupled receptors. Coimmunoprecipitation studies demonstrate that
      RANTES forms complexes with glycanated syndecan (SD)-1 and -4, in addition
      to CCR5 on the CCR5-positive HeLa cells. Moreover, confocal microscopy
      analysis shows the colocalization of RANTES with SD-1 and -4.
      Glycosaminoglycans removal from the cells by glycosaminidases treatment
      prevented RANTES binding to SD-1 and -4 and decreased RANTES binding to
      CCR5 on the CCR5-positive HeLa cells. Removal of glycosaminoglycans by
      glycosaminidases treatment of the complexes, RANTES/SD-1/SD-4/+/-CCR5,
      immobilized on beads, reversed SD-1 and -4 bindings. Therefore, RANTES
      bindings to SD-1 and -4 depend on glycosaminoglycans and facilitate RANTES
      interaction with CCR5. Extracting plasma membrane cholesterol abolished
      the coimmunoprecipitation of SD-1 with RANTES, suggesting that rafts are
      involved in RANTES association to SD-1. Confocal microscopy analysis as
      well as coimmunoprecipitation experiments show a RANTES-independent
      heteromeric complex on the CCR5-positive HeLa cells, SD-1, SD-4, and CCR5.
      This complex is likely a functional unit in which proteoglycans may
      modulate RANTES binding to CCR5.
AD  - Laboratoire de Biologie Cellulaire, Biotherapies Benefices et Risques,
      UPRES 3410, UFR-SMBH, Universite Paris XIII, 74, rue Marcel Cachin, 93017,
      Bobigny, France.
FAU - Slimani, Hocine
AU  - Slimani H
FAU - Charnaux, Nathalie
AU  - Charnaux N
FAU - Mbemba, Elisabeth
AU  - Mbemba E
FAU - Saffar, Line
AU  - Saffar L
FAU - Vassy, Roger
AU  - Vassy R
FAU - Vita, Claudio
AU  - Vita C
FAU - Gattegno, Liliane
AU  - Gattegno L
LA  - eng
PT  - Journal Article
PL  - England
TA  - Glycobiology
JID - 9104124
SB  - IM
EDAT- 2003/05/30 05:00
MHDA- 2003/05/30 05:00
PHST- 2003/May/28 [aheadofprint]
AID - 10.1093/glycob/cwg083 [doi]
AID - cwg083 [pii]
PST - ppublish
SO  - Glycobiology 2003 Sep;13(9):623-34.

PMID- 12761845
UI  - 22645910
OWN - NLM
STAT- in-process
DA  - 20030522
IS  - 1058-8388
VI  - 227
IP  - 2
DP  - 2003 Jun
TI  - Localisation of specific heparan sulfate proteoglycans during the
      proliferative phase of brain development.
PG  - 170-84
AB  - Early brain development is characterised by the proliferation of neural
      precursor cells. Several families of signalling molecules such as the
      fibroblast growth factors (FGFs) and Wnts are known to play important
      roles in this early phase of brain development. Accumulating evidence
      demonstrates that signalling of these molecules requires the presence of
      heparan sulfate chains attached to a proteoglycan core protein (HSPG).
      However, the specific identity of the HSPG components in the developing
      brain is unknown. To determine which HSPGs might be involved at this early
      phase, we analysed the expression of the major cell surface HSPG families
      in the developing brain at a time of most active proliferation. Syndecan-1
      and glypican-4 were the most highly expressed in the developing brain
      during the time of peak proliferation and localise to ventricular regions
      of the brain, where the precursor cells are proliferating. Syndecan-4,
      although less abundant, also localises to cells in the ventricular zone.
      We have also examined HSPG involvement in brain development using cultures
      of embryonic neural precursor cells. We find that FGF2 stimulation of
      proliferation is inhibited in the presence of sodium chlorate, an
      inhibitor of heparan sulfate synthesis, and is rescued by addition of
      exogenous heparan sulfate. These data support a requirement for heparan
      sulfate in FGF signalling for proliferation of brain precursor cells. The
      expression of these specific HSPGs within the proliferative zone of the
      brain suggests that they may be involved in regulation of early brain
      development, such as FGF-stimulated proliferation. Developmental Dynamics
      227:170-184, 2003.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Department of Anatomy and Cell Biology, University of Melbourne,
      Parkville, Victoria, Australia.
FAU - Ford-Perriss, Miriam
AU  - Ford-Perriss M
FAU - Turner, Kirsty
AU  - Turner K
FAU - Guimond, Scott
AU  - Guimond S
FAU - Apedaile, Anwyn
AU  - Apedaile A
FAU - Haubeck, Hans-Dieter
AU  - Haubeck HD
FAU - Turnbull, Jeremy
AU  - Turnbull J
FAU - Murphy, Mark
AU  - Murphy M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Dev Dyn
JID - 9201927
SB  - IM
EDAT- 2003/05/23 05:00
MHDA- 2003/05/23 05:00
AID - 10.1002/dvdy.10298 [doi]
PST - ppublish
SO  - Dev Dyn 2003 Jun;227(2):170-84.

UI  - 0
PMID- 12754183
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030519
IS  - 1040-0605
DP  - 2003 May 16
TI  - Lung endothelial heparan sulfates mediate cationic peptide-induced barrier
      dysfunction: a new role for the glycocalyx.
AB  - The endothelial glycocalyx is believed to play a major role in
      microvascular permeability. We tested the hypothesis that specific
      components of the glycocalyx, via cytoskeletal-mediated signaling,
      actively participate in barrier regulation. Using polymers of arginine and
      lysine as models of neutrophil-derived inflammatory cationic proteins, we
      determined size- and dose-dependent responses of cultured bovine lung
      microvascular endothelial cell permeability as assessed by
      transendothelial electrical resistance (TER). Polymers of arginine and
      lysine greater than 11kDa produced maximal barrier dysfunction as
      demonstrated by a 70% decrease in TER. Monomers of L-arginine and L-lysine
      did not alter barrier function suggesting a cross-linking requirement of
      cell surface "receptors". To test the hypothesis that glycosaminoglycans
      (GAGS) are candidate "receptors" for this response, we used highly
      selective enzymes to remove specific GAGs prior to polyarginine (PA)
      treatment and examined the effect on TER. Heparanase III attenuated
      PA-induced barrier dysfunction by 50% whereas heparinase I had no effect.
      To link changes in barrier function with structural alterations, we
      examined actin organization and syndecan localization after PA. PA-
      induced actin stress fiber formation and clustering of syndecan-1 and
      syndecan-4 which was significantly attenuated by heparanase III.
      PA-induced cytoskeletal rearrangement and barrier function did not involve
      myosin light chain kinase or p38 MAP kinase, as ML-7, a selective MLCK
      inhibitor, or SB20358, a p38 MAP kinase inhibitor did not alter PA-induced
      barrier dysfunction. In summary, lung endothelial cell heparan sulfate
      proteoglycans are key participants in inflammatory cationic
      peptide-induced signaling that links cytoskeletal re-organization with
      subsequent barrier dysfunction.
AD  - Anesthesiology & Critical Care Medicine, Johns Hopkins School of Medicine,
      Baltimore, MD, USA.
AU  - Dull RO
AU  - Dinavahi R
AU  - Schwartz L
AU  - Humphries DE
AU  - Berry D
AU  - Sasisekharan R
AU  - Garcia JG
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Am J Physiol Lung Cell Mol Physiol
JID - 100901229
EDAT- 2003/05/20 05:00
MHDA- 2003/05/20 05:00
AID - 10.1152/ajplung.00022.2003 [doi]
AID - 00022.2003 [pii]
PST - aheadofprint
SO  - Am J Physiol Lung Cell Mol Physiol 2003 May 16;.

PMID- 12749851
UI  - 22635437
OWN - NLM
STAT- completed
DA  - 20030516
DCOM- 20030711
IS  - 0014-4827
VI  - 286
IP  - 2
DP  - 2003 Jun 10
TI  - Syndecan-1-mediated cell spreading requires signaling by alphavbeta3
      integrins in human breast carcinoma cells.
PG  - 219-32
AB  - Syndecans are cell surface heparan sulfate proteoglycans with regulatory
      roles in cell adhesion, proliferation, and differentiation [Annu. Rev.
      Biochem. 68 (1999) 729]. While the syndecan heparan sulfate chains are
      essential for matrix binding, less is known about the signaling role of
      their core proteins. To mimic syndecan-specific adhesion, MDA-MB-231
      mammary carcinoma cells were plated on antibodies against syndecan-4 or
      syndecan-1. While cells adherent via syndecan-4 spread, cells adherent via
      syndecan-1 do not. However, cells adherent via syndecan-1 can be induced
      to spread by Mn(2+), suggesting that activation of a beta(1) or beta(3)
      integrin partner is required. Surprisingly, pretreatment of cells with a
      function-activating beta(1) antibody does not induce spreading, whereas
      function-blocking beta(1) integrin antibodies do, suggesting involvement
      of a beta(1)-to-beta(3) integrin cross-talk. Indeed, blockade of beta(1)
      integrin activation induces alpha(v)beta(3) integrin activation detectable
      by soluble fibrinogen binding. Spreading in response to syndecan-1 is
      independent of integrin-ligand binding. Furthermore, competition with
      soluble murine syndecan-1 ectodomain, which does not disrupt cell
      adhesion, nonetheless blocks the spreading mechanism. These data suggest
      that the ectodomain of the syndecan-1 core protein directly participates
      in the formation of a signaling complex that signals in cooperation with
      alpha(v)beta(3) integrins; signaling via this complex is negatively
      regulated by beta(1) integrins.
AD  - Department of Pathology and Laboratory Medicine, and Program in Molecular
      and Cellular Pharmacology, University of Wisconsin-Madison, Madison, WI
      53706, USA.
FAU - Beauvais, DeannaLee M
AU  - Beauvais DM
FAU - Rapraeger, Alan C
AU  - Rapraeger AC
LA  - eng
GR  - R01-HD21881/HD/NICHD
GR  - T32-GM08688/GM/NIGMS
PT  - Journal Article
PL  - United States
TA  - Exp Cell Res
JID - 0373226
RN  - 0 (Antigens, CD29)
RN  - 0 (Integrin alphaVbeta3)
RN  - 0 (Integrin beta3)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 7439-95-4 (Magnesium)
SB  - IM
MH  - Antigens, CD29/drug effects/metabolism
MH  - Breast Neoplasms/*metabolism
MH  - Cell Adhesion/drug effects/*physiology
MH  - Cell Movement/drug effects/*physiology
MH  - Eukaryotic Cells/cytology/drug effects/*metabolism
MH  - Female
MH  - Human
MH  - Integrin alphaVbeta3/*metabolism
MH  - Integrin beta3/drug effects/metabolism
MH  - Magnesium/pharmacology
MH  - Membrane Glycoproteins/antagonists & inhibitors/*metabolism
MH  - Protein Structure, Tertiary/drug effects/physiology
MH  - Proteoglycans/antagonists & inhibitors/*metabolism
MH  - Signal Transduction/drug effects/physiology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Cells, Cultured
EDAT- 2003/05/17 05:00
MHDA- 2003/07/12 05:00
AID - S0014482703001265 [pii]
PST - ppublish
SO  - Exp Cell Res 2003 Jun 10;286(2):219-32.

PMID- 12709506
UI  - 22595498
OWN - NLM
STAT- completed
DA  - 20030423
DCOM- 20030529
IS  - 0022-0345
VI  - 82
IP  - 5
DP  - 2003 May
TI  - Different mechanisms of syndecan-1 activation through a
      fibroblast-growth-factor-inducible response element (FiRE) in mucosal and
      cutaneous wounds.
PG  - 382-7
AB  - Syndecan-1 expression is enhanced in cutaneous and mucosal wounds. We have
      previously demonstrated that wounding-induced syndecan-1 expression in the
      skin occurs transcriptionally, through a
      fibroblast-growth-factor-inducible element (FiRE). Here, we show that FiRE
      is also activated in mucosal wounds. However, both the expression patterns
      and the activation mechanisms of FiRE are different from those in the
      skin. In the mucosa in vivo, the activation starts and ends earlier than
      in cutaneous wounds. FiRE is first detected at around 12 hours in
      keratinocytes, and the activation declines by the third day after wounding
      occurs. The activation is seen on the migrating sheet of epithelial
      mucosa, as in the case of cutaneous wounding. In contrast to the situation
      in vivo, organ-cultured mucosal wounds exhibit no FiRE activity, while
      organ-cultured cutaneous wounds show robust activity. Activation in
      mucosal wounds is enhanced, however, by the application of epidermal
      growth factor. This suggests that exogenous growth factor activity is
      required for activation of syndecan-1 in mucosal wounds but not in
      cutaneous wounds.
AD  - Department of Oral and Maxillofacial Surgery, Institute of Dentistry,
      University of Turku, Lemminkaisenkatu 2, Finland. jaana.rautava@utu.fi
FAU - Rautava, J
AU  - Rautava J
FAU - Soukka, T
AU  - Soukka T
FAU - Heikinheimo, K
AU  - Heikinheimo K
FAU - Miettinen, P J
AU  - Miettinen PJ
FAU - Happonen, R-P
AU  - Happonen RP
FAU - Jaakkola, P
AU  - Jaakkola P
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Dent Res
JID - 0354343
RN  - 0 (FGF-regulated protein 1)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - 62229-50-9 (Epidermal Growth Factor)
SB  - D
SB  - IM
MH  - Animal
MH  - Comparative Study
MH  - Enzyme Activation
MH  - Epidermal Growth Factor/physiology
MH  - Fibroblast Growth Factors/*physiology
MH  - Gene Expression Regulation
MH  - Immunohistochemistry
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Mice
MH  - Mice, Mutant Strains
MH  - Mouth Mucosa/*injuries/*metabolism
MH  - Organ Culture
MH  - Promoter Regions (Genetics)/physiology
MH  - Proteins/*biosynthesis
MH  - Proteoglycans/*biosynthesis
MH  - Skin/injuries/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Up-Regulation
MH  - Wound Healing/*genetics
EDAT- 2003/04/24 05:00
MHDA- 2003/05/30 05:00
PST - ppublish
SO  - J Dent Res 2003 May;82(5):382-7.

PMID- 12702549
UI  - 22732831
OWN - NLM
STAT- completed
DA  - 20030709
DCOM- 20030821
IS  - 1073-449X
VI  - 168
IP  - 2
DP  - 2003 Jul 15
TI  - Sputum sol neutrophil elastase activity in bronchiectasis: differential
      modulation by syndecan-1.
PG  - 192-8
AB  - The persistently dominant activity of neutrophil elastase in bronchial
      secretions replete with antielastases is crucial to the pathogenesis of
      bronchiectasis. We hypothesize that components in the bronchial secretions
      bind neutrophil elastase and compromise the inhibitory efficiency of
      prevailing antielastases. Zymographic analysis of sputum sols from
      patients with bronchiectasis found elastase activity in a polydisperse,
      alcian blue-stained zone of high molecular mass. This suggested that
      neutrophil elastase was complexed with polyanionic partners. Western blot
      analysis found not only the polyanionic partner, heparan
      sulfate/syndecan-1, but also the physiological antielastases, secretory
      leukoproteinase inhibitor and alpha1-antitrypsin, in the complex. Both
      dissociative density gradient ultracentrifugation and heparin displacement
      revealed that elastase dissociated from heparan sulfate/syndecan-1 was
      fully inhibited by the endogenous antielastases. This contrasts with the
      effects of exogenous antielastases on sputum neutrophil elastase
      activity-that of alpha1-antitrypsin was limited, but that of secretory
      leukoproteinase inhibitor was facilitated. Similarly, complexed elastase
      on blots of sputum sol zymographs was bound and inhibited by exogenous
      secretory leukoproteinase inhibitor but not by exogenous
      alpha1-antitrypsin. Taken together, the results bring a new focus to
      heparan sulfate/syndecan-1 complexed with neutrophil elastase in inflamed
      bronchial secretions as a target for modulating elastase susceptibility to
      physiological antielastases.
AD  - Department of Biochemistry, University of Hong Kong, 21 Sassoon Road, Hong
      Kong, China. shumdkhk@hkucc.hku.hk
FAU - Chan, Stanley C H
AU  - Chan SC
FAU - Shum, Daisy K Y
AU  - Shum DK
FAU - Ip, Mary S M
AU  - Ip MS
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Am J Respir Crit Care Med
JID - 9421642
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Serine Proteinase Inhibitors)
RN  - 0 (alpha 1-Antitrypsin)
RN  - 0 (antileukoprotease)
RN  - 0 (syndecan)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 3.4.21.37 (Leukocyte Elastase)
SB  - AIM
SB  - IM
CIN - Am J Respir Crit Care Med. 2003 Jul 15;168(2):144-5. PMID: 12851241
MH  - Blotting, Western
MH  - Bronchiectasis/*enzymology
MH  - Female
MH  - Heparitin Sulfate/metabolism
MH  - Human
MH  - Leukocyte Elastase/*metabolism
MH  - Male
MH  - Membrane Glycoproteins/metabolism
MH  - Middle Age
MH  - Proteins/metabolism
MH  - Proteoglycans/metabolism
MH  - Serine Proteinase Inhibitors/metabolism
MH  - Sputum/*enzymology
MH  - Support, Non-U.S. Gov't
MH  - alpha 1-Antitrypsin/metabolism
EDAT- 2003/04/19 05:00
MHDA- 2003/08/22 05:00
PHST- 2003/Apr/17 [aheadofprint]
AID - 10.1164/rccm.200208-829OC [doi]
AID - 200208-829OC [pii]
PST - ppublish
SO  - Am J Respir Crit Care Med 2003 Jul 15;168(2):192-8.

PMID- 12695118
UI  - 22582095
OWN - NLM
STAT- completed
DA  - 20030415
DCOM- 20030529
IS  - 0161-5890
VI  - 39
IP  - 15
DP  - 2003 May
TI  - Activation of terminal B cell differentiation by inhibition of histone
      deacetylation.
PG  - 923-32
AB  - A role for histone acetylation, which can alter the accessibility of DNA
      to transcriptional regulatory proteins and contribute to gene expression,
      in regulating terminal B cell differentiation was investigated in the
      mature B lymphoma L10A and mouse splenic B cells. Incubation of the L10A
      cells with the histone deacetylase (HDAC) inhibitors trichostatin A (TSA)
      and butyrate increased expression of Blimp-1, J chain, and mad genes,
      decreased expression of c-myc and BSAP/Pax-5 genes, increased the
      expression of surface CD43 and Syndecan-1, and decreased surface IgM.
      Incubation of splenic B cells with TSA and dextran conjugated anti-IgD Ab
      increased Blimp-1 gene and Syndecan-1 surface expression. The alteration
      in gene expression and cell surface markers was consistent with induction
      of the onset of terminal B cell differentiation. Co-incubation of L10A
      cells with TSA and cycloheximide (CHX) abrogated the up-regulation of
      Blimp-1 expression, indicating that TSA-activated Blimp-1 expression
      required synthesis of a transcriptional activator. In contrast, mad
      expression was increased in L10A cells cultured with TSA and cycloheximide
      or cycloheximide alone, suggesting mad expression may occur independent of
      Blimp-1 expression and is regulated by a labile, HDAC associated
      transcriptional repressor. The results demonstrate that histone
      acetylation regulates transcription of genes controlling terminal B cell
      differentiation.
AD  - Department of Microbiology and Immunology, University of Rochester Medical
      Center, 601 Elmwood Avenue, Rochester, New York, NY 14642, USA.
FAU - Lee, Sang C
AU  - Lee SC
FAU - Bottaro, Andrea
AU  - Bottaro A
FAU - Insel, Richard A
AU  - Insel RA
LA  - eng
GR  - AI07285/AI/NIAID
GR  - AI37123/AI/NIAID
GR  - AI45012/AI/NIAID
GR  - HD36293/HD/NICHD
PT  - Journal Article
PL  - England
TA  - Mol Immunol
JID - 7905289
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Hydroxamic Acids)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Mad protein)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Repressor Proteins)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (Transcription Factors)
RN  - 0 (sialophorin)
RN  - 0 (syndecan)
RN  - 138415-26-6 (B lymphocyte-induced maturation protein 1)
RN  - 58880-19-6 (trichostatin A)
RN  - EC 3.5.1.- (Histone Deacetylases)
SB  - IM
MH  - Animal
MH  - B-Lymphocytes/drug effects/*enzymology/immunology
MH  - Cell Differentiation
MH  - Cells, Cultured
MH  - DNA-Binding Proteins/biosynthesis/genetics
MH  - Enzyme Inhibitors/pharmacology
MH  - Gene Expression Regulation
MH  - Histone Deacetylases/*antagonists & inhibitors
MH  - Hydroxamic Acids/pharmacology
MH  - Immunoglobulin M/metabolism
MH  - Membrane Glycoproteins/biosynthesis
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Models, Genetic
MH  - Proteins/biosynthesis
MH  - Proteoglycans/biosynthesis
MH  - Repressor Proteins/biosynthesis/genetics
MH  - Sialoglycoproteins/biosynthesis
MH  - Spleen/immunology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transcription Factors/biosynthesis/genetics
MH  - Tumor Cells, Cultured
EDAT- 2003/04/16 05:00
MHDA- 2003/05/30 05:00
AID - S0161589003000294 [pii]
PST - ppublish
SO  - Mol Immunol 2003 May;39(15):923-32.

PMID- 12680958
UI  - 22568681
OWN - NLM
STAT- in-process
DA  - 20030408
IS  - 0303-6987
VI  - 30
IP  - 4
DP  - 2003 Apr
TI  - Sweet syndrome in multiple myeloma: a series of six cases.
PG  - 261-4
AB  - BACKGROUND: Sweet syndrome (SS), a paraneoplastic syndrome characterized
      by fever, neutrophilia, multiple erythematous painful plaques, and a dense
      dermal neutrophilic infiltration, has a known association with hematologic
      malignancies such as acute myelogenous leukemia. However, no clear
      association with multiple myeloma (MM) has been reported. MATERIALS AND
      METHODS: Pathology reports of the 2357 patients with multiple myeloma at
      the University of Arkansas for Medical Sciences were reviewed to retrieve
      cases who had developed SS. Cytogenetic studies and immunoglobulin
      secretory status were retrieved. Five cases of SS in MM and 25 cases of SS
      in patients without MM underwent syndecan-1 immunohistochemistry.
      OBSERVATIONS: Six cases of SS occurring in the setting of MM showed a
      predominance in patients secreting IgG paraprotein. Five of the six
      patients received granulocyte-colony stimulating factor while the sixth
      received granulocyte-monocyte-colony stimulating factor. Fifty percent
      showed a non-specific cytogenetic anomaly. CONCLUSIONS: There is no
      specific cytogenetic anomaly associated with SS in the setting of MM. This
      paraneoplastic syndrome may be secondary to elevated levels of granulocyte
      colony stimulating factor (G-CSF), possibly with a component of enhanced
      sensitivity to endogenous G-CSF. The immunoglobulin secretory status
      parallels that seen in MM with cutaneous involvement, but IgG secretors
      may be at an increased risk of developing SS compared with their
      counterparts who secrete other immunoglobulins.
AD  - Department of Pathology, Baylor Medical College, Houston, TX,
      USA;Departments of Pathology and Dermatology and Myeloma Institute for
      Research and Therapy, University of Arkansas for Medical Sciences, AR,
      USA.
FAU - Bayer-Garner, I B
AU  - Bayer-Garner IB
FAU - Cottler-Fox, M
AU  - Cottler-Fox M
FAU - Smoller, B R
AU  - Smoller BR
LA  - eng
PT  - Journal Article
PL  - Denmark
TA  - J Cutan Pathol
JID - 0425124
SB  - IM
EDAT- 2003/04/12 05:00
MHDA- 2003/04/12 05:00
AID - 029 [pii]
PST - ppublish
SO  - J Cutan Pathol 2003 Apr;30(4):261-4.

PMID- 12684764
UI  - 22583138
OWN - NLM
STAT- in-process
DA  - 20030416
IS  - 0340-2061
VI  - 206
IP  - 5
DP  - 2003 Apr
TI  - Comparison of expression patterns between CREB family transcription factor
      OASIS and proteoglycan core protein genes during murine tooth development.
PG  - 373-80
AB  - The transcription factor OASIS gene, which encodes for a CREB/ATF family
      member, is specifically expressed in the salivary gland, the cartilage and
      the tooth germs of the mouse embryo. In the present study, the expression
      patterns were compared between OASIS mRNA and major vertebrate
      proteoglycans, which might be the downstream genes of OASIS in the tooth
      germs of mouse first mandibular molars, through in situ hybridization
      histochemistry. OASIS mRNA expression was observed in the inner enamel
      epithelium during the cap and bell stages (E14.5-E18.5) in the
      preodontoblasts during differentiation stage (E18.5-P0) and in the
      differentiating odontoblasts during the early secretory stage (P2.5-P4.5).
      Proteoglycans (versican, decorin, biglycan, glypican, syndecan-1, and
      syndecan-3) were expressed in the tooth germs in various patterns.
      Decorin, biglycan, syndecan-1 and syndecan-3 showed gene expressions
      overlapping with OASIS. Especially the expression pattern of decorin and
      syndecan-3 coincided temporally and spatially exactly with that of OASIS.
      These results suggest that the OASIS gene might be related to proteoglycan
      expression and may play an important role in the differentiation of the
      odontoblast and cells in inner enamel epithelium.
AD  - Department of Cell Science, Institute of Biomedical Sciences, Fukushima
      Medical University School of Medicine, 960-1295, Fukushima, Japan.
FAU - Hikake, Tsuyoshi
AU  - Hikake T
FAU - Mori, Tetsuji
AU  - Mori T
FAU - Iseki, Ken
AU  - Iseki K
FAU - Hagino, Seita
AU  - Hagino S
FAU - Zhang, Yuxiang
AU  - Zhang Y
FAU - Takagi, Hiromi
AU  - Takagi H
FAU - Yokoya, Sachihiko
AU  - Yokoya S
FAU - Wanaka, Akio
AU  - Wanaka A
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Anat Embryol (Berl)
JID - 7505194
SB  - IM
EDAT- 2003/04/10 05:00
MHDA- 2003/04/10 05:00
PHST- 2003/Jan/28 [accepted]
PHST- 2003/Mar/21 [aheadofprint]
AID - 10.1007/s00429-003-0311-z [doi]
PST - ppublish
SO  - Anat Embryol (Berl) 2003 Apr;206(5):373-80.

PMID- 12684756
UI  - 22621927
OWN - NLM
STAT- in-process
DA  - 20030508
IS  - 0300-8584
VI  - 192
IP  - 2
DP  - 2003 May
TI  - Role of heparan sulfate in interactions of Listeria monocytogenes with
      enterocytes.
PG  - 107-15
AB  - Heparan sulfate is known to participate in binding a wide variety of
      microbes to mammalian cells, but few studies have focused on the
      enterocyte. Normal human colonic and small intestinal enterocytes, and
      cultured HT-29 (but not Caco-2) enterocytes, reacted prominently with
      antibodies specific for heparan sulfate and for the core protein of
      syndecan-1 (a heparan sulfate proteoglycan). The heparan sulfate analog,
      heparin, inhibited interactions of Listeria monocytogenes (adherence and
      internalization) with HT-29, but not Caco-2, enterocytes. Internalization
      of L. monocytogenes by HT-29 enterocytes was inhibited by heparan sulfate
      and to a lesser extent by chondroitin sulfate, but not by the non-sulfated
      glycosaminoglycan hyaluronic acid. Compared to plasmid control ARH-77
      cells, adherence of L. monocytogenes, was increased using ARH-77 cells
      transfected with syndecan-1 cDNA. Heparin binding protein(s) on L.
      monocytogenes were confirmed using biotinylated heparin. To determine if
      these in vitro observations might have in vivo relevance, L. monocytogenes
      was preincubated with heparin and then orally inoculated into mice.
      Compared to L. monocytogenes not pretreated with heparin, L. monocytogenes
      pretreated with heparin was associated with decreased extraintestinal
      dissemination to the mesenteric lymph nodes and liver of orally inoculated
      mice. Thus, heparan sulfate (possibly as the heparan sulfate proteoglycan
      syndecan-1) appears to participate in interactions of L. monocytogenes
      with enterocytes.
AD  - Department of Laboratory Medicine and Pathology, University of Minnesota,
      Mayo Mail Code 609, 420 Delaware Street, SE, MN 55455, USA.
FAU - Henry-Stanley, Michelle  J
AU  - Henry-Stanley MJ
FAU - Hess, Donavon J
AU  - Hess DJ
FAU - Erickson, Elizabeth  A
AU  - Erickson EA
FAU - Garni, Robb M
AU  - Garni RM
FAU - Wells, Carol  L
AU  - Wells CL
LA  - eng
GR  - AI 23484/AI/NIAID
PT  - Journal Article
PL  - Germany
TA  - Med Microbiol Immunol (Berl)
JID - 0314524
SB  - IM
EDAT- 2003/04/10 05:00
MHDA- 2003/04/10 05:00
PHST- 2002/Aug/05 [received]
PHST- 2003/Mar/05 [aheadofprint]
AID - 10.1007/s00430-002-0165-7 [doi]
PST - ppublish
SO  - Med Microbiol Immunol (Berl) 2003 May;192(2):107-15.

PMID- 12665470
UI  - 22552229
OWN - NLM
STAT- completed
DA  - 20030331
DCOM- 20030421
IS  - 1530-6860
VI  - 17
IP  - 6
DP  - 2003 Apr
TI  - Syndecans in inflammation.
PG  - 575-91
AB  - Cell surface heparan sulfate (HS) influences a multitude of molecules,
      cell types, and processes relevant to inflammation. HS binds to cell
      surface and matrix proteins, cytokines, and chemokines. These interactions
      modulate inflammatory cell maturation and activation, leukocyte rolling,
      and tight adhesion to endothelium, as well as extravasation and
      chemotaxis. The syndecan family of transmembrane proteoglycans is the
      major source of cell surface HS on all cell types. Recent in vitro and in
      vivo data suggest the involvement of syndecans in the modulation of
      leukocyte-endothelial interactions and extravasation, the formation of
      chemokine and kininogen gradients, participation in chemokine and growth
      factor signaling, as well as repair processes. Thus, the complex role of
      HS in inflammation is reflected by multiple functions of its physiological
      carriers, the syndecans. Individual and common functions of the four
      mammalian syndecan family members can be distinguished. Recently generated
      transgenic and knockout mouse models will facilitate analysis of the
      individual processes that each syndecan is involved in.
AD  - Protogeneia, Inc., Munster, Germany. protogenia@technologiehof-ms.de
FAU - Gotte, Martin
AU  - Gotte M
LA  - eng
GR  - R01-CA-28735/CA/NCI
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
PL  - United States
TA  - FASEB J
JID - 8804484
RN  - 0 (Chemokines)
RN  - 0 (Cytokines)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animal
MH  - Chemokines/metabolism
MH  - Cytokines/metabolism
MH  - Heparitin Sulfate/metabolism
MH  - Human
MH  - Inflammation/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Proteoglycans/*metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
RF  - 204
EDAT- 2003/04/01 05:00
MHDA- 2003/04/22 05:00
AID - 10.1096/fj.02-0739rev [doi]
AID - 17/6/575 [pii]
PST - ppublish
SO  - FASEB J 2003 Apr;17(6):575-91.

PMID- 12665334
UI  - 22551427
OWN - NLM
STAT- completed
DA  - 20030331
DCOM- 20030404
IS  - 0284-186X
VI  - 42
IP  - 1
DP  - 2003
TI  - Syndecan-1 (CD138) expression in acute myeloblastic leukemia cells--an
      immuno electron microscopic study.
PG  - 71-4
AB  - Syndecan-1 (CD138), an important transmembrane heparan sulfate
      proteoglycan is expressed in distinct stages of cell differentiation.
      Although its expression in acute lymphoblastic leukemia (ALL) cells is
      well known: its function or presence in acute myeloblastic leukemia (AML)
      cells is still largely unknown. The expression of syndecan-1 was studied
      in bone marrow biopsies of three patients with AML using electron
      microscopic immunocytochemistry. Positive expression of syndecan-1 was
      found in AML cells. These results suggest that syndecan-1 expression is
      not only a characteristic phenotypic marker for ALL, but is also expressed
      in AML cells.
AD  - Department of Histology & Embryology, Faculty of Medicine, Hacettepe
      University, Ankara, Turkey.
FAU - Seftalioglu, Aysel
AU  - Seftalioglu A
FAU - Karakus, Sema
AU  - Karakus S
FAU - Dundar, Semra
AU  - Dundar S
FAU - Can, Belgin
AU  - Can B
FAU - Erdemli, Esra
AU  - Erdemli E
FAU - Irmak, M Kemal
AU  - Irmak MK
FAU - Oztas, Emin
AU  - Oztas E
FAU - Korkmaz, Cem
AU  - Korkmaz C
FAU - Yazar, Fatih
AU  - Yazar F
FAU - Cavusoglu, Ilkin
AU  - Cavusoglu I
LA  - eng
PT  - Journal Article
PL  - Norway
TA  - Acta Oncol
JID - 8709065
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Antibodies, Monoclonal
MH  - Bone Marrow/metabolism
MH  - Human
MH  - Leukemia, Myelocytic, Acute/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Microscopy, Immunoelectron
MH  - Middle Age
MH  - Proteoglycans/*metabolism
EDAT- 2003/04/01 05:00
MHDA- 2003/04/05 05:00
PST - ppublish
SO  - Acta Oncol 2003;42(1):71-4.

PMID- 12660231
UI  - 22651116
OWN - NLM
STAT- completed
DA  - 20030526
DCOM- 20030710
IS  - 0021-9258
VI  - 278
IP  - 22
DP  - 2003 May 30
TI  - Syndecan-1 expression is regulated in an isoform-specific manner by the
      farnesoid-X receptor.
PG  - 20420-8
AB  - Syndecan-1 (SDC1), a transmembrane heparan sulfate proteoglycan that
      participates in the binding and internalization of extracellular ligands,
      was identified in a screen designed to isolate genes that are regulated by
      the farnesoid X-receptor (FXR, NR1H4). Treatment of human hepatocytes with
      either naturally occurring (chenodeoxycholic acid) or synthetic (GW4064)
      FXR ligands resulted in both induction of SDC1 mRNA and enhanced binding,
      internalization, and degradation of low density lipoprotein. Transient
      transfection assays, using wild-type and mutant SDC1 promoter-luciferase
      genes, led to the identification of a nuclear hormone receptor-binding
      hexad arranged as a direct repeat separated by one nucleotide (DR-1) in
      the proximal promoter that was necessary and sufficient for activation by
      FXR. The wild-type, but not a mutated DR-1 element, conferred FXR
      responsiveness to a heterologous thymidine kinase promoter-reporter gene.
      Four murine FXR isoforms have been identified recently that differ either
      at their amino terminus and/or by the presence or absence of four amino
      acids in the hinge region. Interestingly, the activities of the human SDC1
      promoter-reporter constructs were highly induced by the two FXR isoforms
      that do not contain the four-amino acid insert and were unresponsive to
      the isoforms containing the four amino acids. Thus, current studies
      demonstrate that hepatic SDC1 is induced in an FXR isoform-specific
      manner. Increased expression of SDC1 may account in part for the
      hypotriglyceridemic effect that can result from the administration of
      chenodeoxycholic acid to humans.
AD  - Department of Biological Chemistry and Medicine, UCLA, Los Angeles,
      California 90095, USA.
FAU - Anisfeld, Andrew M
AU  - Anisfeld AM
FAU - Kast-Woelbern, Heidi R
AU  - Kast-Woelbern HR
FAU - Meyer, Marie E
AU  - Meyer ME
FAU - Jones, Stacey A
AU  - Jones SA
FAU - Zhang, Yanqiao
AU  - Zhang Y
FAU - Williams, Kevin J
AU  - Williams KJ
FAU - Willson, Timothy
AU  - Willson T
FAU - Edwards, Peter A
AU  - Edwards PA
LA  - eng
GR  - HL30568/HL/NHLBI
GR  - HL68445/HL/NHLBI
GR  - P50-HL56984/HL/NHLBI
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NR1H4 protein, human)
RN  - 0 (Protein Isoforms)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (syndecan)
RN  - EC 1.13.12.- (Luciferase)
SB  - IM
MH  - Base Sequence
MH  - Cell Line
MH  - DNA Primers
MH  - Gene Expression Regulation/*physiology
MH  - Human
MH  - Luciferase/genetics
MH  - Membrane Glycoproteins/*genetics
MH  - Promoter Regions (Genetics)
MH  - Protein Isoforms/*genetics
MH  - Proteoglycans/*genetics
MH  - RNA, Messenger/genetics
MH  - Receptors, Cytoplasmic and Nuclear/*physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, Non-P.H.S.
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2003/03/28 05:00
MHDA- 2003/07/11 05:00
PHST- 2003/Mar/26 [aheadofprint]
AID - 10.1074/jbc.M302505200 [doi]
AID - M302505200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 May 30;278(22):20420-8.

PMID- 12648064
UI  - 22535306
OWN - NLM
STAT- completed
DA  - 20030321
DCOM- 20030807
IS  - 0007-1048
VI  - 120
IP  - 6
DP  - 2003 Mar
TI  - Soluble urokinase-type plasminogen activator receptor (suPAR) as an
      independent factor predicting worse prognosis and extra-bone marrow
      involvement in multiple myeloma patients.
PG  - 953-9
AB  - The urokinase-type plasminogen activator (uPA) system, which consists of a
      proteinase (uPA), a receptor (uPAR or CD87) and inhibitors, is involved in
      proteolysis, cell migration, tissue remodelling, angiogenesis and cell
      adhesion. Recent findings suggest that malignant plasma cells express uPA
      and uPAR. The expression of these factors could represent a process by
      which myeloma plasma cells interact with the bone marrow (BM) environment
      and influence important biological events such as bone matrix degradation,
      plasma cell invasion and homing and, possibly, clinical evolution. We
      evaluated uPAR (CD87) and its soluble form (suPAR) in 49 multiple myeloma
      (MM) patients and correlated their expression and levels with
      clinico-biological characteristics of the disease. Flow cytometric
      analysis demonstrated that CD87 was expressed in all MM patients. High
      CD87 expression was associated with higher intensity of expression of CD56
      (P = 0.038), CD38 (P = 0.058) and CD138 (P = 0.054) and CD45bright
      positivity (P = 0.014). suPAR levels correlated positively with soluble
      serum CD138 (P = 0.001), creatinine (P = 0.001), beta2-microglobulin (P <
      0.001), disease stage (P = 0.017) and extra-BM involvement (P = 0.002). In
      the 46 evaluable patients, multivariate analysis showed that high levels
      of suPAR (P = 0.0214) and disease stage (P = 0.0064) were predictive of
      extra-BM involvement. In multivariate Cox analysis, 13q deletion (P =
      0.0278), high soluble serum CD138 (P = 0.0201) and high suPAR (P = 0.0229)
      were the only parameters that independently affected survival. We conclude
      that CD87 is expressed on myeloma plasma cells and that suPAR, which
      predicts extra-BM involvement and poor prognosis, possibly represents a
      molecule with a relevant role in the biology of MM.
AD  - Section of Haematology, Department of Biomedical Sciences, University of
      Ferrara, Ferrara, Italy. sse@dns.unife.it
FAU - Rigolin, Gian Matteo
AU  - Rigolin GM
FAU - Tieghi, Alessia
AU  - Tieghi A
FAU - Ciccone, Maria
AU  - Ciccone M
FAU - Bragotti, Letizia Zenone
AU  - Bragotti LZ
FAU - Cavazzini, Francesco
AU  - Cavazzini F
FAU - Della Porta, Matteo
AU  - Della Porta M
FAU - Castagnari, Barbara
AU  - Castagnari B
FAU - Carroccia, Rosanna
AU  - Carroccia R
FAU - Guerra, Giovanni
AU  - Guerra G
FAU - Cuneo, Antonio
AU  - Cuneo A
FAU - Castoldi, Gianluigi
AU  - Castoldi G
LA  - eng
PT  - Journal Article
PL  - England
TA  - Br J Haematol
JID - 0372544
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, CD56)
RN  - 0 (Biological Markers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (beta 2-Microglobulin)
RN  - 0 (plasminogen activator, urokinase receptors)
RN  - 0 (syndecan)
RN  - 60-27-5 (Creatinine)
RN  - EC 3.2.2.5 (ADP-ribosyl Cyclase)
RN  - EC 3.2.2.5 (CD38 antigen)
SB  - IM
MH  - ADP-ribosyl Cyclase/analysis
MH  - Aged
MH  - Antigens, CD/analysis
MH  - Antigens, CD56/analysis
MH  - Biological Markers/analysis
MH  - Case-Control Studies
MH  - Creatinine/analysis
MH  - Flow Cytometry
MH  - Human
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Middle Age
MH  - Multiple Myeloma/*immunology
MH  - Multivariate Analysis
MH  - Neoplasm Staging
MH  - Plasma Cells/*immunology
MH  - Prognosis
MH  - Proteoglycans/analysis
MH  - Receptors, Cell Surface/*analysis
MH  - Support, Non-U.S. Gov't
MH  - beta 2-Microglobulin/*analysis
EDAT- 2003/03/22 04:00
MHDA- 2003/08/09 05:00
AID - 4176 [pii]
PST - ppublish
SO  - Br J Haematol 2003 Mar;120(6):953-9.

PMID- 12640657
UI  - 22527353
OWN - NLM
STAT- completed
DA  - 20030317
DCOM- 20030424
IS  - 0270-4137
VI  - 55
IP  - 1
DP  - 2003 Apr 1
TI  - Tissue microarray analysis reveals prognostic significance of syndecan-1
      expression in prostate cancer.
PG  - 20-9
AB  - BACKGROUND: Tissue microarrays (TMA) have recently emerged as powerful
      tools to rapidly analyze the clinical significance of new molecular
      markers in human tumors. Here, we have tested several molecular markers on
      a prostate TMA containing 637 different specimens. METHODS: The specimens
      were from 551 patients with prostate cancer and long-term follow-up
      information on progression (median 5.3 years), tumor-specific and overall
      survival (median 5.9 years). Eighty-six specimens from benign prostatic
      hyperplasia were included as controls. Expression of Ki67, Bcl-2, p53,
      CD-10 (neutral endopeptidase), and syndecan-1 (CD-138) was analyzed by
      immunohistochemistry. RESULTS: Gleason grade and Ki67 Labeling Index (LI)
      were independent predictors of early recurrence and poor survival. Bcl-2
      predicted early recurrence, whereas p53 was associated with poor survival.
      Syndecan-1 overexpression also predicted early recurrence and was
      significantly associated with tumor specific survival, high Gleason grade,
      Ki67 LI, and Bcl-2 overexpression. Neoadjuvant hormonal therapy was
      associated with overexpression of Bcl-2 and inhibition of Ki67 LI and
      CD-10, but did not affect the expression of the remaining markers.
      CONCLUSIONS: The results of this TMA study confirm a dominant prognostic
      significance of Gleason grading and Ki67 LI in prostate cancer, as
      compared to a less pronounced role of Bcl-2, and p53. We identified
      syndecan-1 as a new prognostic factor and provide evidence for an
      androgen-dependent regulation of CD-10 expression.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Department of Urology, University of Basel, Schonbeinstrasse 40, 4031
      Basel, Switzerland.
FAU - Zellweger, Tobias
AU  - Zellweger T
FAU - Ninck, Christoph
AU  - Ninck C
FAU - Mirlacher, Martina
AU  - Mirlacher M
FAU - Annefeld, Matthias
AU  - Annefeld M
FAU - Glass, Andrew G
AU  - Glass AG
FAU - Gasser, Thomas C
AU  - Gasser TC
FAU - Mihatsch, Michael J
AU  - Mihatsch MJ
FAU - Gelmann, Edward P
AU  - Gelmann EP
FAU - Bubendorf, Lukas
AU  - Bubendorf L
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Prostate
JID - 8101368
RN  - 0 (Ki-67 Antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Protein p53)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - EC 3.4.24.11 (Neprilysin)
SB  - IM
MH  - Aged
MH  - Aged, 80 and over
MH  - Down-Regulation
MH  - Genes, bcl-2/physiology
MH  - Human
MH  - Immunohistochemistry
MH  - Ki-67 Antigen/metabolism
MH  - Male
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Middle Age
MH  - Neoplasm Recurrence, Local/*metabolism/pathology
MH  - Neprilysin/metabolism
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Proportional Hazards Models
MH  - Prostatic Neoplasms/*metabolism/pathology
MH  - Protein Array Analysis/methods
MH  - Protein p53/metabolism
MH  - Proteoglycans/*biosynthesis
MH  - Retrospective Studies
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, Non-P.H.S.
EDAT- 2003/03/18 04:00
MHDA- 2003/04/25 05:00
AID - 10.1002/pros.10209 [doi]
PST - ppublish
SO  - Prostate 2003 Apr 1;55(1):20-9.

PMID- 12635139
UI  - 22521323
OWN - NLM
STAT- completed
DA  - 20030313
DCOM- 20030606
IS  - 0022-3417
VI  - 199
IP  - 4
DP  - 2003 Apr
TI  - Proteoglycans and WT1 as markers for distinguishing adenocarcinoma,
      epithelioid mesothelioma, and benign mesothelium.
PG  - 479-87
AB  - Malignant mesothelioma is a tumour frequently accompanied by an effusion
      with elevated hyaluronan levels. To distinguish malignant mesothelioma,
      adenocarcinoma, and reactive benign mesothelium with cytological and
      histological methods including immunocytochemistry is a major diagnostic
      challenge. The Wilms' tumour susceptibility gene 1 (WT1), expressed during
      transition of mesenchyme to epithelial tissues, is regarded as a marker
      for the mesothelial lineage. Its effect on the cell phenotype may be
      regulated via the syndecans, i.e. proteoglycans on the cell surface. To
      determine how WT1, proteoglycans, and hyaluronan synthase are expressed in
      mesothelioma, adenocarcinoma, and reactive benign mesothelium, we studied
      these molecules at the mRNA and protein levels, with the additional
      purpose of finding diagnostic parameters. Adenocarcinoma cells produced
      more mRNA for syndecan-1, but cells derived from mesothelium expressed
      WT1, biglycan, and larger amounts of syndecan-2. The difference in gene
      expression of these two syndecans was best monitored by the ratio between
      them. Syndecan-4 was highly expressed in all malignant cell lines, this
      expression being 1.7-5 times greater than in benign mesothelial cells.
      Although hyaluronan synthase-1 and versican could not distinguish between
      the three conditions, versican expression was associated with a high rate
      of proliferation. These findings suggest that syndecan-1 and syndecan-2
      together may be useful diagnostic markers, with stronger staining for the
      latter epitope in mesothelial tissues. The alternating appearance of these
      two syndecans can be shown not only by RT-PCR and FACS in vitro, but also
      by immunohistochemistry on clinical material.
CI  - Copyright 2003 John Wiley & Sons, Ltd.
AD  - Department of IMPI, Division of Pathology, Karolinska Institutet, Huddinge
      University Hospital, Stockholm, Sweden. miklos.gulyas@impi.ki.se
FAU - Gulyas, Miklos
AU  - Gulyas M
FAU - Hjerpe, Anders
AU  - Hjerpe A
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Pathol
JID - 0204634
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteochondroitin Sulfates)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (WT1 Proteins)
RN  - 0 (syndecan)
RN  - 123939-84-4 (biglycan)
RN  - 126968-45-4 (versican)
SB  - IM
MH  - Adenocarcinoma/*diagnosis/metabolism
MH  - Diagnosis, Differential
MH  - Epithelial Cells/metabolism
MH  - Human
MH  - Membrane Glycoproteins/metabolism
MH  - Mesothelioma/*diagnosis/metabolism
MH  - Neoplasm Proteins/metabolism
MH  - Proteochondroitin Sulfates/metabolism
MH  - Proteoglycans/*metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
MH  - Tumor Markers, Biological/*metabolism
MH  - WT1 Proteins/*metabolism
EDAT- 2003/03/14 04:00
MHDA- 2003/06/07 05:00
AID - 10.1002/path.1312 [doi]
PST - ppublish
SO  - J Pathol 2003 Apr;199(4):479-87.

PMID- 12601486
UI  - 22488496
OWN - NLM
STAT- completed
DA  - 20030225
DCOM- 20030507
IS  - 0939-5555
VI  - 82
IP  - 2
DP  - 2003 Feb
TI  - Tc-99m methoxyisobutylisonitrile bone marrow imaging for predicting the
      levels of myeloma cells in bone marrow in multiple myeloma: correlation
      with CD38/CD138 expressing myeloma cells.
PG  - 88-92
AB  - The percentage of myeloma cells in bone marrow is subsequently an
      important index of disease in patients with multiple myeloma (MM). Bone
      marrow myeloma cells can be detected by strong CD38/CD138 positivity and
      light scatter characteristics using flow cytometry. The aim of the study
      was to evaluate the relationship between the degree of Tc-99m
      methoxyisobutylisonitrile (MIBI) uptake and the percentage of CD38/CD138
      expressing myeloma cells in the bone marrow of patients with MM. A total
      of 15 patients with MM (mean age: 61.7+/-2.4 years; 7 F and 8 M) were
      included in the study. Tc-99m MIBI imaging was obtained 20 min after
      injection of 740 MBq Tc-99m MIBI. Planar spot images of the pelvis and
      thorax were acquired. The uptake of Tc-99m MIBI in the bone marrow was
      evaluated using a qualitative and also a semiquantitative scoring system
      for the bone marrow in areas that included the proximal femurs, anterior
      iliac crest, and sternum. In all patients, flow cytometry was performed
      for assessing the percentage of CD38/CD138 expressing myeloma cells in the
      bone marrow samples. There was a statistically significant positive
      correlation between the percentage of CD38/CD138 expressing plasma cells
      in bone marrow and both mean qualitative (r=0.689, p=0.005) and
      semiquantitative (r=0.669, p=0.006) results of Tc-99m MIBI uptake. In
      conclusion, our results indicate that increased Tc-99m MIBI uptake of bone
      marrow is related to the percentage of plasma cell infiltration of bone
      marrow. Tc-99m MIBI bone marrow imaging may be a useful tool for
      predicting the levels of myeloma cells in bone marrow of patients with MM.
AD  - Department of Nuclear Medicine, Osmangazi University Medical Faculty,
      26480, Eskischir, Turkey. ilknur_ak@yahoo.com
FAU - Ak, I
AU  - Ak I
FAU - Aslan, V
AU  - Aslan V
FAU - Vardareli, E
AU  - Vardareli E
FAU - Gulbas, Z
AU  - Gulbas Z
LA  - eng
PT  - Clinical Trial
PT  - Controlled Clinical Trial
PT  - Journal Article
PL  - Germany
TA  - Ann Hematol
JID - 9107334
RN  - 0 (Antigens, CD)
RN  - 0 (Biological Markers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 109581-73-9 (Technetium Tc 99m Sestamibi)
RN  - EC 3.2.2.5 (ADP-ribosyl Cyclase)
RN  - EC 3.2.2.5 (CD38 antigen)
SB  - IM
MH  - ADP-ribosyl Cyclase/analysis
MH  - Aged
MH  - Antigens, CD/analysis
MH  - Biological Markers/blood
MH  - Bone Marrow/pathology/*radionuclide imaging
MH  - Female
MH  - Flow Cytometry
MH  - Human
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Middle Age
MH  - Multiple Myeloma/*pathology/radionuclide imaging
MH  - Neoplasm Invasiveness/radionuclide imaging
MH  - Plasma Cells/pathology
MH  - Predictive Value of Tests
MH  - Proteoglycans/analysis
MH  - Severity of Illness Index
MH  - Technetium Tc 99m Sestamibi/administration & dosage/*diagnostic
      use/pharmacokinetics
EDAT- 2003/02/26 04:00
MHDA- 2003/05/08 05:00
PHST- 2002/Jul/31 [received]
PHST- 2002/Dec/09 [accepted]
PHST- 2003/Feb/11 [aheadofprint]
AID - 10.1007/s00277-002-0600-2 [doi]
PST - ppublish
SO  - Ann Hematol 2003 Feb;82(2):88-92.

PMID- 12591930
UI  - 22602705
OWN - NLM
STAT- completed
DA  - 20030428
DCOM- 20030617
IS  - 0021-9258
VI  - 278
IP  - 18
DP  - 2003 May 2
TI  - Heparan sulfate proteoglycans as regulators of fibroblast growth factor-2
      signaling in brain endothelial cells. Specific role for glypican-1 in
      glioma angiogenesis.
PG  - 16045-53
AB  - Fibroblast growth factor-2 (FGF2) is a potent angiogenic factor in
      gliomas. Heparan sulfate promotes ligand binding to receptor tyrosine
      kinase and regulates signaling. The goal of this study was to examine the
      contribution of heparan sulfate proteoglycans (HSPGs) to glioma
      angiogenesis. Here we show that all brain endothelial cell HSPGs carry
      heparan sulfate chains similarly capable of forming a ternary complex with
      FGF2 and fibroblast growth factor receptor-1c and of promoting a mitogenic
      signal. Immunohistochemical analysis revealed that glypican-1 was
      overexpressed in glioma vessel endothelial cells, whereas this
      cell-surface HSPG was consistently undetectable in normal brain vessels.
      To determine the effect of increased glypican-1 expression on FGF2
      signaling, we transfected normal brain endothelial cells, which express
      low base-line levels of glypican-1, with this proteoglycan. Glypican-1
      expression enhanced growth of brain endothelial cells and sensitized them
      to FGF2-induced mitogenesis despite the fact that glypican-1 remained a
      minor proteoglycan. In contrast, overexpression of syndecan-1 had no
      effect on growth or FGF2 sensitivity. We conclude that the glypican-1 core
      protein has a specific role in FGF2 signaling. Glypican-1 overexpression
      may contribute to angiogenesis and the radiation resistance characteristic
      of this malignancy.
AD  - Department of Pathology and Laboratory Medicine, University of Wisconsin,
      Clinical Sciences Center K4/850, Madison, WI 53562-8550, USA.
FAU - Qiao, Dianhua
AU  - Qiao D
FAU - Meyer, Kristy
AU  - Meyer K
FAU - Mundhenke, Christoph
AU  - Mundhenke C
FAU - Drew, Sally A
AU  - Drew SA
FAU - Friedl, Andreas
AU  - Friedl A
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - EC 2.7.1.112 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animal
MH  - Cell Division
MH  - Endothelium, Vascular/cytology/*metabolism
MH  - Fibroblast Growth Factor 2/*metabolism/pharmacology
MH  - Glioma/*blood supply
MH  - Heparan Sulfate Proteoglycan/*physiology
MH  - Human
MH  - Mice
MH  - Neovascularization, Pathologic/*etiology
MH  - Receptor Protein-Tyrosine Kinases/physiology
MH  - Receptors, Fibroblast Growth Factor/physiology
MH  - Support, Non-U.S. Gov't
EDAT- 2003/02/20 04:00
MHDA- 2003/06/18 05:00
PHST- 2003/Feb/18 [aheadofprint]
AID - 10.1074/jbc.M211259200 [doi]
AID - M211259200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 May 2;278(18):16045-53.

PMID- 12576441
UI  - 22464176
OWN - NLM
STAT- completed
DA  - 20030210
DCOM- 20030801
IS  - 1078-0432
VI  - 9
IP  - 2
DP  - 2003 Feb
TI  - Immunohistochemical expression of CD23 and CD40 may identify
      prognostically favorable subgroups of diffuse large B-cell lymphoma: a
      Nordic Lymphoma Group Study.
PG  - 722-8
AB  - PURPOSE: In search for subgroups of diffuse large B-cell lymphoma (DLBCL)
      with different histogenetic origin and prognosis, as has been described by
      gene expression profiling, we examined tumor specimens from 125 patients
      with DLBCL, uniformly treated by either
      cyclophosphamideAdriamycin-vincristine-prednisone or methotrexate,
      doxorubicin, cyclophosphamide, vincristine, prednisone, and bleomycin in a
      multicenter trial set by the Nordic Lymphoma Group 1989-1994. EXPERIMENTAL
      DESIGN: Bcl-6, CD10, and CD40 were chosen as markers for a germinal center
      phenotype, CD23 as a marker of pre/early germinal center origin, and CD138
      as a marker for postgerminal center origin. In addition, expression of the
      apoptotic regulators bcl-2 and bax was analyzed. Immunohistochemical
      analysis was performed using the EnVision method. RESULTS: CD10 was
      positive in 51%, bcl-6 in 97%, and CD138 only in 2% of the cases. No
      prognostic conclusions could be drawn from analysis of these factors. CD40
      was positive in 76% of the cases. This group was associated with superior
      time to treatment failure (P = 0.027) and overall survival (OS; P =
      0.0068). By Cox regression analysis, positivity for CD40 was shown to be a
      prognostic factor for OS, independent of International Prognostic Index.
      CD23 was positive in 16% of the cases (all CD5 negative and all CD40
      positive). This group showed a strong tendency for better OS (P = 0.033).
      CD40 expression correlated with bax but not with bcl-2 expression.
      CONCLUSIONS: CD23 and CD40 expression seems to be prognostically favorable
      in DLBCL. This may be secondary to a germinal center origin or
      attributable to increased apoptosis via induction of bax and/or enhanced
      T-cell interaction, resulting in improved autologous tumor response.
      Confirmatory studies are necessary.
AD  - Department of Oncology, Lund University Hospital, 221 85 Lund, Sweden.
      johan.linderoth@onk.lu.se
FAU - Linderoth, Johan
AU  - Linderoth J
FAU - Jerkeman, Mats
AU  - Jerkeman M
FAU - Cavallin-Stahl, Eva
AU  - Cavallin-Stahl E
FAU - Kvaloy, Stein
AU  - Kvaloy S
FAU - Torlakovic, Emina
AU  - Torlakovic E
CN  - Nordic Lymphoma Group Study.
LA  - eng
PT  - Journal Article
PT  - Multicenter Study
PL  - United States
TA  - Clin Cancer Res
JID - 9502500
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, CD40)
RN  - 0 (Epitopes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, IgE)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, CD/blood
MH  - Antigens, CD40/*blood
MH  - Disease-Free Survival
MH  - Epitopes/analysis
MH  - Follow-Up Studies
MH  - Human
MH  - Immunohistochemistry/methods
MH  - Lymphoma, B-Cell/*immunology/mortality/pathology
MH  - Lymphoma, Large-Cell/*immunology/mortality/pathology
MH  - Membrane Glycoproteins/blood
MH  - Middle Age
MH  - Neoplasm Staging
MH  - Patient Selection
MH  - Prognosis
MH  - Proteoglycans/blood
MH  - Receptors, IgE/*blood
MH  - Retrospective Studies
MH  - Support, Non-U.S. Gov't
MH  - Survival Analysis
MH  - Tumor Markers, Biological/blood
EDAT- 2003/02/11 04:00
MHDA- 2003/08/02 05:00
PST - ppublish
SO  - Clin Cancer Res 2003 Feb;9(2):722-8.

PMID- 12571251
UI  - 22566079
OWN - NLM
STAT- completed
DA  - 20030407
DCOM- 20030703
IS  - 0021-9258
VI  - 278
IP  - 15
DP  - 2003 Apr 11
TI  - Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland
      epithelial cells bear heparan sulfate chains that are apparently
      structurally indistinguishable.
PG  - 13561-9
AB  - Many of the biological functions attributed to cell surface heparan
      sulfate (HS) proteoglycans, including the Syndecan family, are elicited
      through the interaction of their HS chains with soluble extracellular
      molecules. Tightly controlled, cell-specific sulfation and epimerization
      of HS precursors endows these chains with highly sulfated, iduronate-rich
      regions, which are major determinants of cytokine and matrix-protein
      binding and which are interspersed by N-acetylated, poorly sulfated
      regions. Until this study, there have been no comprehensive structural
      comparisons made on HS chains decorating simultaneously expressed, but
      different, syndecan core proteins. In this paper we demonstrate that the
      HS chains on affinity-purified syndecan-1 and -4 from murine mammary gland
      cells are essentially identical by a number of parameters. Size
      determination, disaccharide analyses, enzymatic and chemical scission
      methods, and affinity co-electrophoresis all failed to reveal any
      significant differences in fine structure, domain organization, or
      ligand-binding properties of these HS species. These findings lead us to
      suggest that the imposition of the fine structure onto HS occurs
      independently of the core protein to which it is attached and that these
      core proteins, in addition to the HS chains, may play a pivotal role in
      the various biological functions ascribed to these macromolecules.
AD  - Division of Newborn Medicine, Children's Hospital, Harvard Medical School,
      Boston, Massachusetts 02215, USA. zako@aichi-med.ac.jp
FAU - Zako, Masahiro
AU  - Zako M
FAU - Dong, Jianying
AU  - Dong J
FAU - Goldberger, Olga
AU  - Goldberger O
FAU - Bernfield, Merton
AU  - Bernfield M
FAU - Gallagher, John T
AU  - Gallagher JT
FAU - Deakin, Jon A
AU  - Deakin JA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Disaccharides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Sulfates)
RN  - 0 (Sulfur Radioisotopes)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 9007-34-5 (Collagen)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
MH  - Animal
MH  - Cell Line
MH  - Chromatography, Gel
MH  - Chromatography, High Pressure Liquid
MH  - Collagen/biosynthesis/isolation & purification
MH  - Disaccharides/chemistry/isolation & purification
MH  - Epithelial Cells/cytology/*metabolism
MH  - Female
MH  - Heparin Lyase/metabolism
MH  - Heparitin Sulfate/*chemistry/isolation & purification
MH  - Mammae/cytology/metabolism
MH  - Membrane Glycoproteins/*biosynthesis/*chemistry
MH  - Mice
MH  - Proteoglycans/*biosynthesis/*chemistry
MH  - Sulfates/metabolism
MH  - Sulfur Radioisotopes
EDAT- 2003/02/07 04:00
MHDA- 2003/07/04 05:00
PHST- 2003/Feb/05 [aheadofprint]
AID - 10.1074/jbc.M209658200 [doi]
AID - M209658200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Apr 11;278(15):13561-9.

PMID- 12566461
UI  - 22566054
OWN - NLM
STAT- completed
DA  - 20030407
DCOM- 20030703
IS  - 0021-9258
VI  - 278
IP  - 15
DP  - 2003 Apr 11
TI  - Heparan sulfate regulates targeting of syndecan-1 to a functional domain
      on the cell surface.
PG  - 12888-93
AB  - In polarized B lymphoid cells, syndecan-1 is targeted specifically to a
      discrete membrane domain termed the uropod that is located at the cell's
      trailing edge. Within this functional domain, syndecan-1 promotes
      cell-cell adhesion and concentration of heparin binding growth factors.
      The present study reveals the surprising finding that targeting of
      syndecan-1 to uropods is mediated by its heparan sulfate chains and that
      targeting is regulated by cell surface events rather than solely by
      intracellular mechanisms. The addition of exogenous heparin or the
      treatment of polarized cells with heparitinase initiates a rapid and
      dramatic redistribution of uropod syndecan-1 over the entire cell surface,
      and a mutated syndecan-1 lacking heparan sulfate chains fails to
      concentrate within uropods. Interestingly, the heparan sulfate-bearing
      proteoglycans glypican-1 and beta glycan fail to concentrate in uropods,
      indicating that targeting may require heparan sulfate structural motifs
      unique to syndecan-1 or that the core protein of syndecan-1 participates
      in specific interactions that promote heparan sulfate-mediated targeting.
      These findings suggest functional specificity for syndecan-1 within
      uropods and, in addition, reveal a novel mechanism for the targeting of
      molecules to discrete membrane subcellular domains via heparan sulfate.
AD  - Department of Pathology, Arkansas Cancer Research Center, University of
      Arkansas for Medical Sciences, Little Rock, Arkansas 72205, USA.
FAU - Yang, Yang
AU  - Yang Y
FAU - Borset, Magne
AU  - Borset M
FAU - Langford, J Kevin
AU  - Langford JK
FAU - Sanderson, Ralph D
AU  - Sanderson RD
LA  - eng
GR  - CA 68494/CA/NCI
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (syndecan)
RN  - 9005-49-6 (Heparin)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 4.2.2. (Polysaccharide-Lyases)
RN  - EC 4.2.2.8 (heparitinsulfate lyase)
SB  - IM
MH  - Animal
MH  - Cell Line
MH  - Cell Membrane/drug effects/physiology
MH  - Cell Polarity/physiology
MH  - DNA, Complementary/genetics
MH  - Heparan Sulfate Proteoglycan/pharmacology
MH  - Heparin/pharmacology
MH  - Heparitin Sulfate/*pharmacology
MH  - Human
MH  - Kinetics
MH  - Membrane Glycoproteins/isolation & purification/*metabolism
MH  - Mice
MH  - Polysaccharide-Lyases/pharmacology
MH  - Protein Transport/drug effects
MH  - Proteoglycans/isolation & purification/*metabolism
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transfection
EDAT- 2003/02/05 04:00
MHDA- 2003/07/04 05:00
PHST- 2003/Feb/03 [aheadofprint]
AID - 10.1074/jbc.M209440200 [doi]
AID - M209440200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Apr 11;278(15):12888-93.

PMID- 12534799
UI  - 22423472
OWN - NLM
STAT- completed
DA  - 20030121
DCOM- 20030805
IS  - 0303-6987
VI  - 30
IP  - 1
DP  - 2003 Jan
TI  - Expression of syndecan-1 is a sensitive marker for cutaneous plasmacytoma.
PG  - 18-22
AB  - BACKGROUND: Cutaneous plasmacytoma is a well-recognized, yet infrequent,
      occurrence in multiple myeloma (MM). There are limitations in the
      morphologic assessment, and as such, the diagnosis presents some
      difficulty, particularly with the plasmablastic type. METHODS: Pathology
      reports of 2357 patients with a diagnosis of MM were reviewed. Twenty
      patients yielded a total of 25 plasmacytomas, 10 of which were analyzed
      for syndecan-1 immunoreactivity. Bartl grade of bone marrow and cutaneous
      plasmacytoma was compared and immunoglobulin secretory status of the
      patients was assessed. RESULTS: The incidence of cutaneous plasmacytoma
      was found to be 1 in 118 patients with MM. Immunoglobulin secretion was
      found to be predominantly IgG. There was a trend for the plasmacytoma
      Bartl grade to be equal to or greater than that of the corresponding bone
      marrow Bartl grade, suggesting a more aggressive phenotype in the
      metastatic lesion. CONCLUSION: Syndecan-1 was found to be a sensitive
      marker for plasmacytomas, independent of cytologic differentiation.
AD  - Department of Pathology, University of Arkansas for Medical Sciences, 4301
      West Markham Street, Little Rock, AR 72205, USA.
FAU - Bayer-Garner, Ilene B
AU  - Bayer-Garner IB
FAU - Joseph, Lija
AU  - Joseph L
FAU - Sanderson, Ralph D
AU  - Sanderson RD
FAU - Smoller, Bruce R
AU  - Smoller BR
LA  - eng
GR  - CA 55819/CA/NCI
GR  - CA 68494/CA/NCI
PT  - Journal Article
PL  - Denmark
TA  - J Cutan Pathol
JID - 0425124
RN  - 0 (Immunoglobulin G)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Bone Marrow/pathology
MH  - Female
MH  - Human
MH  - Immunoglobulin G/analysis
MH  - Male
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Middle Age
MH  - Multiple Myeloma/pathology
MH  - Plasmacytoma/*metabolism/pathology
MH  - Proteoglycans/*biosynthesis
MH  - Retrospective Studies
MH  - Skin Neoplasms/*metabolism/pathology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Markers, Biological/*biosynthesis
EDAT- 2003/01/22 04:00
MHDA- 2003/08/06 05:00
AID - cup300103 [pii]
PST - ppublish
SO  - J Cutan Pathol 2003 Jan;30(1):18-22.

PMID- 12530973
UI  - 22419338
OWN - NLM
STAT- completed
DA  - 20030117
DCOM- 20030228
IS  - 1074-7613
VI  - 18
IP  - 1
DP  - 2003 Jan
TI  - Syndecan captures, protects, and transmits HIV to T lymphocytes.
PG  - 27-39
AB  - This study demonstrates that syndecan functions as an in trans HIV
      receptor. We show that syndecan, when expressed in nonpermissive cells,
      becomes the major mediator for HIV adsorption. This adsorption is mediated
      by the binding of gp120 to the heparan sulfate chains of syndecan.
      Although syndecan does not substitute for HIV entry receptors, it enhances
      the in trans infectivity of a broad range of primate lentiviruses
      including primary viruses produced from PBMCs. Furthermore, syndecan
      preserves virus infectivity for a week, whereas unbound virus loses its
      infectivity in less than a day. Moreover, we obtain evidence suggesting
      that the vast syndecan-rich endothelial lining of the vasculature can
      provide a microenvironment which boosts HIV replication in T cells.
AD  - Department of Immunology, The Scripps Research Institute, La Jolla, CA
      92037, USA.
FAU - Bobardt, Michael D
AU  - Bobardt MD
FAU - Saphire, Andrew C S
AU  - Saphire AC
FAU - Hung, Hsiu-Cheng
AU  - Hung HC
FAU - Yu, Xiaocong
AU  - Yu X
FAU - Van der Schueren, Bernadette
AU  - Van der Schueren B
FAU - Zhang, Zhe
AU  - Zhang Z
FAU - David, Guido
AU  - David G
FAU - Gallay, Philippe A
AU  - Gallay PA
LA  - eng
GR  - AI 46958/AI/NIAID
GR  - MH 62261/MH/NIMH
PT  - Journal Article
PL  - United States
TA  - Immunity
JID - 9432918
RN  - 0 (HIV Envelope Protein gp120)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, HIV)
RN  - 0 (syndecan)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animal
MH  - Cell Line
MH  - Endothelium, Vascular/virology
MH  - HIV/*pathogenicity/physiology
MH  - HIV Envelope Protein gp120/physiology
MH  - Heparitin Sulfate/physiology
MH  - Human
MH  - In Vitro
MH  - Membrane Glycoproteins/chemistry/genetics/*physiology
MH  - Models, Biological
MH  - Proteoglycans/chemistry/genetics/*physiology
MH  - Receptors, HIV/chemistry/genetics/*physiology
MH  - SIV/pathogenicity/physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - T-Lymphocytes/virology
MH  - Virus Replication
EDAT- 2003/01/18 04:00
MHDA- 2003/03/01 04:00
AID - S1074761302005046 [pii]
PST - ppublish
SO  - Immunity 2003 Jan;18(1):27-39.

PMID- 12529625
UI  - 22417559
OWN - NLM
STAT- completed
DA  - 20030116
DCOM- 20030225
IS  - 0028-0836
VI  - 421
IP  - 6920
DP  - 2003 Jan 16
TI  - Immunology: Mobilizing the army.
PG  - 223-4
FAU - Shapiro, Steven D
AU  - Shapiro SD
LA  - eng
PT  - News
PL  - England
TA  - Nature
JID - 0410462
RN  - 0 (Chemokines)
RN  - 0 (Chemotactic Factors)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (growth regulated protein)
RN  - 0 (syndecan)
RN  - 11056-06-7 (Bleomycin)
RN  - EC 3.4.24.23 (Matrilysin)
SB  - IM
MH  - Animal
MH  - Bleomycin/pharmacology
MH  - Chemokines/*metabolism
MH  - Chemotactic Factors/*metabolism
MH  - Chemotaxis, Leukocyte
MH  - Inflammation/chemically induced/immunology/metabolism
MH  - Intercellular Signaling Peptides and Proteins/*metabolism
MH  - Lung/drug effects/*immunology/metabolism/pathology
MH  - Matrilysin/genetics/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - *Neutrophil Infiltration
MH  - Neutrophils/cytology/*immunology
MH  - Proteoglycans/*metabolism
EDAT- 2003/01/17 04:00
MHDA- 2003/02/26 04:00
AID - 10.1038/421223a [doi]
AID - 421223a [pii]
PST - ppublish
SO  - Nature 2003 Jan 16;421(6920):223-4.

PMID- 12480692
UI  - 22559989
OWN - NLM
STAT- completed
DA  - 20030403
DCOM- 20030618
IS  - 0006-4971
VI  - 101
IP  - 8
DP  - 2003 Apr 15
TI  - Multiple myeloma tumor progression in the 5T2MM murine model is a
      multistage and dynamic process of differentiation, proliferation,
      invasion, and apoptosis.
PG  - 3136-41
AB  - At clinical presentation, multiple myeloma (MM) is already a
      well-established disease. The processes involved in earlier stages are,
      however, unknown. Here the 5T2MM murine model was used to analyze
      differentiation, proliferation, invasion, and apoptosis of MM cells during
      disease progression. Naive mice were injected with 5T2MM cells and from
      the onset of the experiment 3 mice were killed each week until the end
      stage. Myeloma cells were isolated from the bone marrow and selected by
      sequential gating of 5T2MM idiotype(+) cells by flow cytometry.
      Microscopic analysis of these sorted 5T2MM idiotype(+) cells confirmed
      their identity as true myeloma cells. Based on serum paraprotein
      concentration and bone marrow tumor load, 3 disease stages were
      distinguished: a quiescent stage, an intermediate stage, and an end stage,
      of slow, moderate, and accelerated tumor progression, respectively. In the
      quiescent stage, the majority of the myeloma cells were
      CD45(+)CD138(-)IL-6R alpha(+), corresponding to an immature, invasive, and
      apoptosis-resistant phenotype. In the end stage the majority of the
      myeloma cells had differentiated into CD45(-)CD138(+)IL-6R alpha(-) cells,
      corresponding to a mature, less invasive, and apoptosis-sensitive
      phenotype. In the intermediate stage a gradual transition from the
      quiescent toward the end stage was observed. In line with these data,
      analysis of sorted 5T2MM cells demonstrated a significant decrease in
      invasive capacity and a significant increase in (dexamethasone-induced)
      apoptosis sensitivity and in proliferation during the disease progression.
      These data suggest that myeloma disease progression is a multistage and
      dynamic process of differentiation, proliferation, invasion, and
      apoptosis.
AD  - Department of Hematology and Immunology, Vrije Universiteit Brussel,
      Brussels, Belgium. asosingh@vub.ac.be
FAU - Asosingh, Kewal
AU  - Asosingh K
FAU - De Raeve, Hendrik
AU  - De Raeve H
FAU - Van Riet, Ivan
AU  - Van Riet I
FAU - Van Camp, Benjamin
AU  - Van Camp B
FAU - Vanderkerken, Karin
AU  - Vanderkerken K
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Antigens, CD45)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Myeloma Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Interleukin-6)
RN  - 0 (syndecan)
RN  - 50-02-2 (Dexamethasone)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Antigens, CD45/analysis
MH  - Apoptosis/drug effects
MH  - Bone Marrow Cells/cytology
MH  - Bone Marrow Transplantation
MH  - Cell Differentiation
MH  - Cell Division
MH  - Coculture
MH  - Dexamethasone/pharmacology
MH  - Disease Progression
MH  - Flow Cytometry
MH  - Immunophenotyping
MH  - Membrane Glycoproteins/analysis
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Multiple Myeloma/blood/*pathology
MH  - Myeloma Proteins/analysis
MH  - Neoplasm Invasiveness
MH  - Proteoglycans/analysis
MH  - Receptors, Interleukin-6/analysis
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured/drug effects
EDAT- 2002/12/14 04:00
MHDA- 2003/06/19 05:00
PHST- 2002/Dec/12 [aheadofprint]
AID - 10.1182/blood-2002-10-3000 [doi]
AID - 2002-10-3000 [pii]
PST - ppublish
SO  - Blood 2003 Apr 15;101(8):3136-41.

PMID- 12393520
UI  - 22417174
OWN - NLM
STAT- completed
DA  - 20030116
DCOM- 20030421
IS  - 0006-4971
VI  - 101
IP  - 3
DP  - 2003 Feb 1
TI  - Gene expression profiling of human plasma cell differentiation and
      classification of multiple myeloma based on similarities to distinct
      stages of late-stage B-cell development.
PG  - 1128-40
AB  - To identify genes linked to normal plasma cell (PC) differentiation and to
      classify multiple myeloma (MM) with respect to the expression patterns of
      these genes, we analyzed global mRNA expression in CD19-enriched B cells
      (BCs) from 7 tonsils, CD138-enriched PCs from 11 tonsils, 31 normal bone
      marrow samples, and 74 MM bone marrow samples using microarrays
      interrogating 6800 genes. Hierarchical clustering analyses with 3288 genes
      clearly segregated the 4 cell types, and chi-square and Wilcoxin rank sum
      tests (P <.0005) identified 359 and 500 previously defined and novel genes
      that distinguish tonsil BCs from tonsil PCs (early differentiation genes
      [EDGs]), and tonsil PCs from bone marrow PCs (late differentiation genes
      [LDGs]), respectively. MM as a whole was found to have dramatically
      variable expression of EDGs and LDGs, and one-way analysis of variance
      (ANOVA) was used to identify the most variable EDGs (vEDGs) and LDGs
      (v1LDG and v2LDG). Hierarchical cluster analysis with these genes revealed
      that previously defined MM gene expression subgroups (MM1-MM4) could be
      linked to one of the 3 normal cell types. Clustering with 30 vEDGs
      revealed that 13 of 18 MM4 cases clustered with tonsil BCs (P =.000 05),
      whereas 14 of 15 MM3 cases clustered with tonsil PCs when using 50 v1LDG
      (P =.000 008), and 14 of 20 MM2 cases clustered with bone marrow PCs when
      using 50 v2LDG (P =.000 09). MM1 showed no significant linkage with normal
      cell types studied. Thus, genes whose expression is linked to distinct
      transitions in late-stage B-cell differentiation can be used to classify
      MM.
AD  - Donna and Donald Lambert Laboratory of Myeloma Genetics at the Myeloma
      Institute for Research and Therapy, University of Arkansas for Medical
      Sciences, Little Rock 72205, USA.
FAU - Zhan, Fenghuang
AU  - Zhan F
FAU - Tian, Erming
AU  - Tian E
FAU - Bumm, Klaus
AU  - Bumm K
FAU - Smith, Ruston
AU  - Smith R
FAU - Barlogie, Bart
AU  - Barlogie B
FAU - Shaughnessy, John Jr
AU  - Shaughnessy J Jr
LA  - eng
GR  - CA55819/CA/NCI
GR  - CA97513/CA/NCI
PT  - Journal Article
PL  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Antigens, CD19)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
SB  - AIM
SB  - IM
MH  - Antigens, CD19
MH  - B-Lymphocytes/cytology/immunology
MH  - Bone Marrow Cells
MH  - Cell Differentiation/genetics
MH  - Cluster Analysis
MH  - Comparative Study
MH  - *Gene Expression Profiling
MH  - Gene Expression Regulation/genetics
MH  - Human
MH  - Membrane Glycoproteins
MH  - Multiple Myeloma/*classification/*pathology
MH  - Plasma Cells/*cytology
MH  - Proteoglycans
MH  - RNA, Messenger/analysis
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tonsil/cytology
EDAT- 2002/10/24 04:00
MHDA- 2003/04/22 05:00
PHST- 2002/Sep/26 [aheadofprint]
AID - 10.1182/blood-2002-06-1737 [doi]
AID - 2002-06-1737 [pii]
PST - ppublish
SO  - Blood 2003 Feb 1;101(3):1128-40.

