UI  - 22667163
PMID- 12782806
OWN - NLM
STAT- in-process
DA  - 20030603
IS  - 0023-852X
VI  - 113
IP  - 6
DP  - 2003 Jun
TI  - Fibronectin and adhesion molecules on canine scarred vocal folds.
PG  - 966-72
AB  - OBJECTIVETo examine the expressions of fibronectin and other adhesion
      molecules on the scarred vocal folds in a short- and long-term animal
      model.STUDY DESIGNAnimal model.METHODSSix 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.RESULTSCompared 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.CONCLUSIONSScar 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.
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
PT  - Journal Article
PL  - United States
TA  - Laryngoscope
JID - 8607378
SB  - IM
EDAT- 2003/06/05 05:00
MHDA- 2003/06/05 05:00
PST - ppublish
SO  - Laryngoscope 2003 Jun;113(6):966-72.

UI  - 22667232
PMID- 12782143
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, 53706, Madison, WI, 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
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.

UI  - 0
PMID- 12773479
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030529
IS  - 0959-6658
DP  - 2003 May 28
TI  - Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed
      on HeLa cells.
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. Co-immunoprecipitation studies demonstrate
      that RANTES forms complexes with glycanated syndecan-1 and syndecan-4, in
      addition to CCR5 on the CCR5 positive HeLa cells. Moreover, confocal
      microscopy analysis shows the co-localization of RANTES with syndecan-1
      and syndecan-4. Glycosaminoglycans removal from the cells by
      glycosaminidases treatment prevented RANTES binding to syndecan-1 and
      syndecan-4 and decreased RANTES binding to CCR5 on the CCR5 positive HeLa
      cells. Removal of glycosaminoglycans by glycosaminidases treatment of the
      complexes, RANTES/syndecan-1/syndecan-4/+/-CCR5, immobilized on beads,
      reversed syndecan-1 and syndecan-4 bindings. Therefore, RANTES bindings to
      syndecan-1 and syndecan-4 depend from glycosaminoglycans and facilitate
      RANTES interaction with CCR5. Extracting plasma membrane cholesterol
      abolished the co-immunoprecipitation of syndecan-1 with RANTES, suggesting
      that rafts are involved in RANTES association to syndecan-1. Confocal
      microscopy analysis as well as co-immunoprecipitation experiments show a
      RANTES-independent heteromeric complex, which comprises on the CCR5
      positive HeLa cells, syndecan-1, syndecan-4 and CCR5. This complex is
      likely a functional unit in which PGs 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.
AU  - Slimani H
AU  - Charnaux N
AU  - Mbemba E
AU  - Saffar L
AU  - Vassy R
AU  - Vita C
AU  - Gattegno L
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Glycobiology
JID - 9104124
EDAT- 2003/05/30 05:00
MHDA- 2003/05/30 05:00
AID - 10.1093/glycob/cwg083 [doi]
AID - cwg083 [pii]
PST - aheadofprint
SO  - Glycobiology 2003 May 28;.

UI  - 22645910
PMID- 12761845
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;.

UI  - 22635437
PMID- 12749851
OWN - NLM
STAT- in-process
DA  - 20030516
IS  - 0014-4827
VI  - 286
IP  - 2
DP  - 2003 Jun 10
TI  - Syndecan-1-mediated cell spreading requires signaling by alpha(v)beta(3)
      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, 53706,
      Madison, WI, USA
FAU - Beauvais, DeannaLee M
AU  - Beauvais DM
FAU - Rapraeger, Alan C
AU  - Rapraeger AC
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Exp Cell Res
JID - 0373226
SB  - IM
EDAT- 2003/05/17 05:00
MHDA- 2003/05/17 05:00
AID - S0014482703001265 [pii]
PST - ppublish
SO  - Exp Cell Res 2003 Jun 10;286(2):219-32.

UI  - 22595498
PMID- 12709506
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.

UI  - 0
PMID- 12702549
OWN - NLM
STAT- pubmed-not-medline
DA  - 20030418
IS  - 1073-449X
DP  - 2003 Apr 17
TI  - Sputum sol neutrophil elastase activity in bronchiectasis. Differential
      modulation by syndecan-1.
AB  - The persistently dominant activity of neutrophil elastase in bronchial
      secretions replete with anti-elastases 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 anti-elastases. 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 anti-elastases, secretory
      leukoproteinase inhibitor and alpha-1-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 anti-elastases. This contrasts with the
      effects of exogenous anti-elastases on sputum neutrophil elastase
      activity- that of alpha-1-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
      alpha-1-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 anti-elastases.
AD  - Biochemistry, The University of Hong Kong, Hong Kong, China.
AU  - Chan SC
AU  - Shum DK
AU  - Ip MS
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Am J Respir Crit Care Med
JID - 9421642
EDAT- 2003/04/19 05:00
MHDA- 2003/04/19 05:00
AID - 10.1164/rccm.200208-829OC [doi]
AID - 200208-829OC [pii]
PST - aheadofprint
SO  - Am J Respir Crit Care Med 2003 Apr 17;.

UI  - 22582095
PMID- 12695118
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.

UI  - 22568681
PMID- 12680958
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.

UI  - 22583138
PMID- 12684764
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.

UI  - 22621927
PMID- 12684756
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 W L K A U J
AU  - Henry-Stanley MW
FAU - Hess, Donavon W L K A U J J
AU  - Hess DW
FAU - Erickson, Elizabeth W L K A U J J A
AU  - Erickson EW
FAU - Garni, Robb W L K A U J J A M
AU  - Garni RW
FAU - Wells, Carol W L K A U J J A M L
AU  - Wells CW
LA  - eng
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.

UI  - 22552229
PMID- 12665470
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.

UI  - 22551427
PMID- 12665334
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.

UI  - 22651116
PMID- 12660231
OWN - NLM
STAT- in-process
DA  - 20030526
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.
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
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
SB  - IM
EDAT- 2003/03/28 05:00
MHDA- 2003/03/28 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.

UI  - 22527353
PMID- 12640657
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.

UI  - 22521323
PMID- 12635139
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.

UI  - 22488496
PMID- 12601486
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.

UI  - 22602705
PMID- 12591930
OWN - NLM
STAT- in-process
DA  - 20030428
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,
      Madison, Wisconsin 53562-8550.
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
SB  - IM
EDAT- 2003/02/20 04:00
MHDA- 2003/02/20 04:00
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.

UI  - 22566079
PMID- 12571251
OWN - NLM
STAT- in-process
DA  - 20030407
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 and the Department of Medical Oncology, Cancer
      Research UK and University of Manchester, Christie Hospital NHS Trust,
      Manchester M20 4BX, United Kingdom.
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
SB  - IM
EDAT- 2003/02/07 04:00
MHDA- 2003/02/07 04:00
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.

UI  - 22566054
PMID- 12566461
OWN - NLM
STAT- in-process
DA  - 20030407
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 betaglycan 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  - Departments of Pathology and Anatomy and Neurobiology, Arkansas Cancer
      Research Center, University of Arkansas for Medical Sciences, Little Rock,
      Arkansas 72205.
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
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JID - 2985121R
SB  - IM
EDAT- 2003/02/05 04:00
MHDA- 2003/02/05 04:00
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.

UI  - 22423472
PMID- 12534799
OWN - NLM
STAT- in-process
DA  - 20030121
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  - Departments of Pathology, Dermatology and Anatomy, and the Arkansas Cancer
      Research Center, University of Arkansas for Medical Sciences, Little Rock,
      AR, 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
PT  - Journal Article
PL  - Denmark
TA  - J Cutan Pathol
JID - 0425124
SB  - IM
EDAT- 2003/01/22 04:00
MHDA- 2003/01/22 04:00
AID - cup300103 [pii]
PST - ppublish
SO  - J Cutan Pathol 2003 Jan;30(1):18-22.

UI  - 22419338
PMID- 12530973
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.

UI  - 22417559
PMID- 12529625
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.

UI  - 22417174
PMID- 12393520
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.

