UI  - 22219954
PMID- 12234986
DA  - 20020917
IS  - 0008-5472
VI  - 62
IP  - 18
DP  - 2002 Sep 15
TI  - Soluble syndecan-1 and serum basic fibroblast growth factor are new
      prognostic factors in lung cancer.
PG  - 5210-7
AB  - Syndecan-1 is a ubiquitous and multifunctional extracellular matrix
      proteoglycan,which mediates basic fibroblast growth factor (bFGF) binding
      and activity. Shedding of syndecan-1 ectodomain from the plasma membrane
      is highly regulated. We evaluated the influence of soluble syndecan-1 and
      serum bFGF determined by ELISA on outcome in 184 lung cancer patients
      (non-small cell lung cancer, n = 138; small cell lung cancer, n = 46).
      Serum syndecan-1 and bFGF levels were determined from sera taken before
      treatment. The median follow-up of the patients alive (n = 21) was 8.1
      years (range, 6.6-8.9 years). High serum syndecan-1 and bFGF levels tended
      to occur in the same patients (P = 0.044). When the serum values
      corresponding to the highest tertile were used as the cutoff value, the
      median survival time of the patients with a high serum syndecan-1 level
      (>59 ng/ml) was 4 months [95% confidence interval (CI), 3-6 months] as
      compared with 11 months (9-16 months) among those with lower serum levels
      (P = 0.0001), and the median survival time of the patients with a high
      bFGF level (>3.4 pg/ml) was 5 months (3-8 months) versus 11 months (8-14
      months) in those with a lower level (P = 0.023). In general, the
      prognostic influence of both factors was independent of the histological
      subtype. Both serum syndecan-1 level (relative risk, 1.8; 95% CI, 1.1-3.1)
      and serum bFGF level (relative risk, 1.6; 95% CI, 1.0-2.7) had independent
      influence on survival in a multivariate survival analysis in non-small
      cell lung cancer. We conclude that high serum syndecan-1 and bFGF levels
      at diagnosis are associated with poor outcome in lung cancer.
AD  - Departments of Oncology [H. J., A. A., S. L.] and Clinical Chemistry [H.
      A.], Helsinki University Central Hospital, FIN-00029 Helsinki.
FAU - Joensuu, Heikki
AU  - Joensuu H
FAU - Anttonen, Anu
AU  - Anttonen A
FAU - Eriksson, Minna
AU  - Eriksson M
FAU - Makitaro, Riitta
AU  - Makitaro R
FAU - Alfthan, Henrik
AU  - Alfthan H
FAU - Kinnula, Vuokko
AU  - Kinnula V
FAU - Leppa, Sirpa
AU  - Leppa S
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JID - 2984705R
SB  - IM
EDAT- 2002/09/18 10:00
MHDA- 2002/09/18 10:00
PST - ppublish
SO  - Cancer Res 2002 Sep 15;62(18):5210-7.



UI  - 22189813
PMID- 12200974
DA  - 20020830
IS  - 0022-3484
VI  - 37
IP  - 4
DP  - 2002 Aug
TI  - Differential expression and distribution of syndecan-1 and -2 in
      periodontal wound healing of the rat.
PG  - 293-9
AB  - Cell-surface proteoglycans participate in several biological functions
      including interactions with adhesion molecules, growth factors and a
      variety of other effector molecules. Accordingly, these molecules play a
      central role in various aspects of cell-cell and cell-matrix interactions.
      To investigate the expression and distribution of the cell surface
      proteoglycans, syndecan-1 and -2, during periodontal wound healing,
      immunohistochemical analyses were carried out using monoclonal antibodies
      against syndecan-1, or -2 core proteins. Both syndecan-1 and -2 were
      expressed and distributed differentially at various stages of early
      inflammatory cell infiltration, granulation tissue formation, and tissue
      remodeling in periodontal wound healing. Expression of syndecan-1 was
      noted in inflammatory cells within and around the fibrin clots during the
      earliest stages of inflammatory cells infiltration. During granulation
      tissue formation it was noted in fibroblast-like cells and newly formed
      blood vessels. Syndecan-1 was not seen in newly formed bone or cementum
      matrix at any of the time periods studied. Syndecan-1 expression was
      generally less during the late stages of wound healing but was markedly
      expressed in cells that were close to the repairing junctional epithelium.
      In contrast, syndecan-2 expression and distribution was not evident at the
      early stages of inflammatory cell infiltration. During the formation of
      granulation tissue and subsequent tissue remodeling, syndecan-2 was
      expressed extracellularly in the newly formed fibrils which were oriented
      toward the root surface. Syndecan-2 was found to be significantly
      expressed on cells that were close to the root surface and within the
      matrix of repaired cementum covering root dentin as well as at the
      alveolar bone edge. These findings indicate that syndecan-1 and -2 may
      have distinctive functions during wound healing of the periodontium. The
      appearance of syndecan-1 may involve both cell-cell and cell-matrix
      interactions, while syndecan-2 showed a predilection to associate with
      cell-matrix interactions during hard tissue formation.
AD  - Faculty of Dentistry, Prince of Songkhla University, Thailand.
FAU - Worapamorn, W
AU  - Worapamorn W
FAU - Xiao, Y
AU  - Xiao Y
FAU - Li, H
AU  - Li H
FAU - Young, W G
AU  - Young WG
FAU - Bartold, P M
AU  - Bartold PM
LA  - eng
PT  - Journal Article
CY  - Denmark
TA  - J Periodontal Res
JID - 0055107
SB  - D
SB  - IM
EDAT- 2002/08/31 10:00
MHDA- 2002/08/31 10:00
PST - ppublish
SO  - J Periodontal Res 2002 Aug;37(4):293-9.



UI  - 22189810
PMID- 12200971
DA  - 20020830
IS  - 0022-3484
VI  - 37
IP  - 4
DP  - 2002 Aug
TI  - Cytokine regulation of syndecan-1 and -2 gene expression in human
      periodontal fibroblasts and osteoblasts.
PG  - 273-8
AB  - Cell-surface proteoglycans participate in several biological functions
      including interactions with a variety of growth factors and cytokines.
      Regulation of syndecan-1 and -2 gene expression was investigated in human
      periodontal ligament fibroblasts (PDLF), osteoblasts (OB) and gingival
      fibroblasts (GF), in response to platelet-derived growth factor (PDGF-BB),
      transforming growth factor (TGF-beta 1), and interleukin (IL-1 beta) by
      Northern blot analyses. We also compared the effect of PDGF-BB and
      TGF-beta 1, separately and in combination, in the prolonged presence of
      IL-1 beta on the expression of both syndecan genes. The results
      demonstrated that the three cell lines regulated the expression of
      syndecan-1 and -2 in response to growth factors and cytokines in different
      manners. These cell lines increased syndecan-1 mRNA levels in response to
      either PDGF-BB or TGF-beta 1 and decreased levels in response to IL-1
      beta. The effect of IL-1 beta on syndecan-1 mRNA synthesis was partially
      reversed after adding PDGF-BB and TGF-beta 1, separately or in
      combination, in the presence of IL-1 beta. In contrast, syndecan-2 mRNA
      level was markedly upregulated in response to either TGF-beta 1 or IL-1
      beta in OB when compared with the other two cell lines. However, the
      stimulatory effect of TGF-beta 1 on syndecan-2 mRNA production in OB was
      abolished in the prolonged presence of IL-1 beta. These findings lend
      support to the notion that syndecan-1 and syndecan-2 have distinct
      functions which correlate with their source and functions within the
      periodontium.
AD  - School of Dentistry, Department of Physiology and Pharmacology, The
      University of Queensland, Brisbane, QLD, Australia.
FAU - Worapamorn, W
AU  - Worapamorn W
FAU - Tam, S P
AU  - Tam SP
FAU - Li, H
AU  - Li H
FAU - Haase, H R
AU  - Haase HR
FAU - Bartold, P M
AU  - Bartold PM
LA  - eng
PT  - Journal Article
CY  - Denmark
TA  - J Periodontal Res
JID - 0055107
SB  - D
SB  - IM
EDAT- 2002/08/31 10:00
MHDA- 2002/08/31 10:00
PST - ppublish
SO  - J Periodontal Res 2002 Aug;37(4):273-8.



UI  - 22188920
PMID- 12200708
DA  - 20020829
DCOM- 20020926
IS  - 0887-6924
VI  - 16
IP  - 9
DP  - 2002 Sep
TI  - DNA profiling and cytogenetic analysis of cell line WSU-CLL reveal
      cross-contamination with cell line REH (pre B-ALL).
PG  - 1868-70
FAU - Drexler, H G
AU  - Drexler HG
FAU - Quentmeier, H
AU  - Quentmeier H
FAU - Dirks, W G
AU  - Dirks WG
FAU - Uphoff, C C
AU  - Uphoff CC
FAU - MacLeod, R A F
AU  - MacLeod RA
LA  - eng
PT  - Letter
CY  - England
TA  - Leukemia
JID - 8704895
RN  - 0 (DNA, Neoplasm)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - *Coculture
MH  - Comparative Study
MH  - Cytogenetic Analysis
MH  - DNA Fingerprinting
MH  - DNA, Neoplasm/analysis
MH  - Fluorescent Antibody Technique
MH  - Human
MH  - Leukemia, Lymphocytic, Chronic/*genetics
MH  - Leukemia, Pre-B-Cell/*genetics
MH  - Lymphoma, B-Cell/*genetics
MH  - Membrane Glycoproteins/metabolism
MH  - Proteoglycans/metabolism
MH  - *Tumor Cells, Cultured
EDAT- 2002/08/30 10:00
MHDA- 2002/09/27 06:00
PHST- 2002/Feb/22 [received]
PHST- 2002/Mar/26 [accepted]
AID - 10.1038/sj.leu.2402610 [doi]
PST - ppublish
SO  - Leukemia 2002 Sep;16(9):1868-70.



UI  - 22177317
PMID- 12189505
DA  - 20020821
IS  - 0945-6317
VI  - 441
IP  - 2
DP  - 2002 Aug
TI  - Anaplastic plasmacytoma with malignant pleural effusion lacking evidence
      of monoclonal gammopathy.
PG  - 154-8
AB  - A case of plasmacytoma of the pleural cavity is reported with massive
      malignant pleural effusion, which, most unusually, lacked monoclonal
      gammopathy, thereby making it difficult to distinguish from lymphoma. The
      pleural tumor and pleural effusion contained large mononuclear
      lymphoma-like cells with distinct nucleoli. Immunohistochemistry revealed
      neither lymphoma markers nor clonal cytoplasmic nor cell surface
      immunoglobulins. Tumor cells were stained with vimentin and the plasma
      cell markers, VS38c, CD138 (syndecan-1), and MUM1 antibodies. Bone marrow
      contained small amounts of tumor consisting of similar cells. Electron
      microscopy showed well developed rough endoplasmic reticulum and
      peripherally positioned nuclei with euchromatin. Flow cytometry of bone
      marrow revealed a minimal involvement of CD38-positive cells. Chromosomal
      analysis of marrow cells revealed a complex abnormal karyotype. A
      polymerase chain reaction demonstrated clonal re-arrangement of the
      immunoglobulin heavy-chain gene. The overall results indicate a clonal
      expansion of tumor cells with primitive plasma cell differentiation with
      the highly unusual feature of absent monotypic immunoglobulin. The study
      illustrates the need for a comprehensive array of techniques to
      distinguish such rare non-synthesizing and non-secretory plasmacytomas
      from lymphoma.
AD  - Department of Internal Medicine, Saiseikai Central Hospital, Tokyo, Japan.
FAU - Aoki, Takuya
AU  - Aoki T
FAU - Okita, Hajime
AU  - Okita H
FAU - Kayano, Hidekazu
AU  - Kayano H
FAU - Orikasa, Hideki
AU  - Orikasa H
FAU - Watanabe, Kentaro
AU  - Watanabe K
FAU - Eyden, Brian P
AU  - Eyden BP
FAU - Yamazaki, Kazuto
AU  - Yamazaki K
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Virchows Arch
JID - 9423843
SB  - IM
EDAT- 2002/08/22 10:00
MHDA- 2002/08/22 10:00
PHST- 2001/Oct/12 [received]
PHST- 2001/Oct/24 [accepted]
PHST- 2002/Jan/12 [aheadofprint]
AID - 10.1007/s00428-001-0579-4 [doi]
PST - ppublish
SO  - Virchows Arch 2002 Aug;441(2):154-8.



UI  - 22131310
PMID- 12135485
DA  - 20020723
DCOM- 20020917
IS  - 0014-2956
VI  - 269
IP  - 14
DP  - 2002 Jul
TI  - Regulation of glypican-1, syndecan-1 and syndecan-4 mRNAs expression by
      follicle-stimulating hormone, cAMP increase and calcium influx during rat
      Sertoli cell development.
PG  - 3461-9
AB  - In seminiferous tubules, Sertoli cells provide structural and nutritional
      support for the developing germinal cells. Cell- to-cell signaling and
      cell adhesion require proteoglycans expressed at the cell membrane. A
      preliminary biochemical and structural approach indicated that cell
      surface proteoglycans are mostly heparan sulfate proteoglycans (HSPG).
      Glypican-1, syndecans-1 and -4 were identified using a molecular approach.
      Their differential regulation was demonstrated in immature rat Sertoli
      cells. Follicle-stimulating hormone (FSH) is the main regulator of Sertoli
      cell function. Signal transduction triggered by FSH involves both an
      increased intracellular cAMP synthesis and a calcium influx. This study
      demonstrates that FSH, through its second messengers (increase in
      intracellular cAMP and intracellular calcium), downregulated the
      glypican-1 mRNA expression in Sertoli cells from 20-day-old rats. On the
      other hand, syndecan-1 mRNA expression is not modulated by FSH as it would
      result from the antagonistic effects of increased intracellular cAMP and
      intracellular calcium levels. Finally, syndecan-4 mRNA expression is not
      regulated by this pathway. The present study was extended during Sertoli
      cell development. Indeed, Sertoli cells undergo extensive changes during
      the postnatal period both in structure and function. These important
      transformations are critical for the establishment of spermatogenesis and
      development of the adult pattern of testicular function. Our data
      indicated that the regulation of HSPG mRNA expression is HSPG-specific and
      depends on the Sertoli cell developmental stage.
AD  - Laboratoire de Biochimie IRBA, UPRES, Universite de Caen, France.
      s_brucato@yahoo.fr
FAU - Brucato, Sylvie
AU  - Brucato S
FAU - Bocquet, Jean
AU  - Bocquet J
FAU - Villers, Corinne
AU  - Villers C
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Eur J Biochem
JID - 0107600
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 29925-17-5 (Ro 20-1724)
RN  - 362-74-3 (Bucladesine)
RN  - 60-92-4 (Cyclic AMP)
RN  - 9002-68-0 (Follicle Stimulating Hormone)
RN  - 9012-63-9 (Cholera Toxin)
RN  - EC 3.1.4.17 (3',5'-Cyclic-Nucleotide Phosphodiesterase)
SB  - IM
MH  - 3',5'-Cyclic-Nucleotide Phosphodiesterase/antagonists & inhibitors
MH  - Animal
MH  - Bucladesine/pharmacology
MH  - Calcium Signaling/*drug effects
MH  - Cholera Toxin/pharmacology
MH  - Cyclic AMP/*physiology
MH  - Enzyme Inhibitors/pharmacology
MH  - Follicle Stimulating Hormone/*pharmacology
MH  - Gene Expression Regulation/*drug effects
MH  - Heparan Sulfate Proteoglycan/biosynthesis/*genetics
MH  - Male
MH  - Membrane Glycoproteins/biosynthesis/*genetics
MH  - Proteoglycans/biosynthesis/*genetics
MH  - RNA, Messenger/*biosynthesis/genetics
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Ro 20-1724/pharmacology
MH  - Second Messenger Systems/*physiology
MH  - Sertoli Cells/*drug effects/metabolism
MH  - Testis/cytology/growth & development
EDAT- 2002/07/24 10:00
MHDA- 2002/09/18 10:01
AID - 3027 [pii]
PST - ppublish
SO  - Eur J Biochem 2002 Jul;269(14):3461-9.



UI  - 22120034
PMID- 12124810
DA  - 20020718
DCOM- 20020816
IS  - 0020-7136
VI  - 100
IP  - 5
DP  - 2002 Aug 10
TI  - Application of differential display to identify genes for lung cancer
      detection in peripheral blood.
PG  - 592-9
AB  - A blood assay for detection of lung cancer biomarkers could significantly
      improve cancer patient prognosis and survival rates. Amplified fragment
      length polymorphism-differential display (AFLP-DD) was used to identify
      gene transcripts found in lung cancer tissue and the peripheral blood of
      lung cancer patients. The clones were evaluated for gene expression in
      lung cancer tissue, peripheral blood of lung cancer patients and healthy
      volunteers' blood. The isolated gene transcript clones were found to be
      from the syndecan 1 gene, collagen 1 gene and 2 novel genes. All 4
      transcripts were expressed in normal lung tissue, 4 cultured primary lung
      cells and 6 lung cancer cell lines. RNA was isolated from peripheral blood
      samples of 69 lung cancer patients. Reverse transcriptase polymerase chain
      reaction (RT-PCR) was used to test for the presence of cytokeratin 19 and
      the 4 gene mRNA transcripts in blood RNA. The positive detection rate of
      at least 1 of the 5 transcripts was 79% for lung adenocarcinoma and 62%
      for squamous carcinoma. Using RT-PCR, at least 1 of the markers was found
      in 53% of stage I patients, 100% of stage II, 71% of stage III and 81% of
      stage IV lung cancer patients. Blood samples from 20 healthy volunteers
      were also tested, but only 1 of the 5 transcripts was found in 1 patient.
      These new molecular markers may aid early detection, staging and follow-up
      of lung cancer patients by RNA isolated from blood.
CI  - Copyright 2002 Wiley-Liss, Inc.
AD  - Hitachi Ltd., Central Research Laboratory, Tokyo, Japan.
FAU - Matsunaga, Hiroko
AU  - Matsunaga H
FAU - Hangai, Nanae
AU  - Hangai N
FAU - Aso, Yoshimasa
AU  - Aso Y
FAU - Okano, Kazunori
AU  - Okano K
FAU - Kawamura, Masafumi
AU  - Kawamura M
FAU - Kobayashi, Kouichi
AU  - Kobayashi K
FAU - Kambara, Hideki
AU  - Kambara H
FAU - Hoger, Jeff H
AU  - Hoger JH
FAU - Mitsuhashi, Masato
AU  - Mitsuhashi M
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Int J Cancer
JID - 0042124
RN  - 0 (RNA, Neoplasm)
RN  - 0 (Tumor Markers, Biological)
SB  - IM
MH  - Adult
MH  - Aged
MH  - *Gene Expression Profiling/*methods
MH  - Gene Expression Regulation, Neoplastic
MH  - Human
MH  - Lung Neoplasms/blood/*diagnosis/*genetics/pathology
MH  - Male
MH  - Middle Age
MH  - Neoplasm Staging
MH  - Polymorphism (Genetics)
MH  - RNA, Neoplasm/genetics/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Tumor Markers, Biological/*blood/*genetics
EDAT- 2002/07/19 10:00
MHDA- 2002/08/17 10:01
AID - 10.1002/ijc.10534 [doi]
PST - ppublish
SO  - Int J Cancer 2002 Aug 10;100(5):592-9.



UI  - 22110755
PMID- 12115879
DA  - 20020712
DCOM- 20020909
LR  - 20020920
IS  - 0022-3417
VI  - 197
IP  - 3
DP  - 2002 Jul
TI  - Extranodal marginal zone B cell lymphomas of the uvea: an analysis of 13
      cases.
PG  - 333-40
AB  - The majority of primary lymphoproliferative lesions of the uvea represent
      low-grade B cell lymphomas and often display a prominent plasmacellular
      differentiation. The purpose of the current study was to classify the
      uveal lymphoproliferations according to the REAL classification; examine
      the immune profile of the plasmacellular differentiated tumour cells using
      the plasma cell-related antigens multiple myeloma oncogene-1-protein
      (MUM1), Vs38c, CD38 and CD138; and to compare this profile with that of
      mature reactive plasma cells. Following fixation, 13 lymphoproliferative
      lesions of the uvea were categorized on the basis of their morphology and
      immunophenotype according to the REAL classification. Included in the
      immunohistochemistry were B cell-specific activator protein (BSAP), MUM1,
      Vs38c, CD38 and CD138. Nested polymerase chain reaction (PCR) was also
      performed on DNA extracted from paraffin sections for the detection of
      gene rearrangements of the heavy immunoglobulin chain (IgH). All of the 13
      uveal tract lymphoproliferative lesions represented malignant lymphoma of
      B cell non-Hodgkin type and could be diagnosed as 'extranodal marginal
      zone B cell lymphomas' (EMZL). The degree of plasmacellular
      differentiation varied between the tumours. In contrast to their
      non-plasmacytoid counterparts, the 'plasmacytoid' EMZL tumour cells were
      negative for the B cell markers CD20 and BSAP, and demonstrated
      heterogeneous positivity for the markers MUM1, Vs38c, CD38 and CD138. The
      most consistent marker was MUM1, being observed in all tumours.
      Co-expression of all plasma cell markers was observed in four (31%) uveal
      EMZL. Loss of CD138 expression was observed in six (46%) tumours, of Vs38c
      expression in five (38%) and of CD38 in one (7%) tumour. Although the
      diagnosis of malignant lymphoma was unequivocally based on morphological
      and immunophenotypical features, the molecular analysis was able to
      demonstrate clonal B cell populations in only one uveal EMZL. All uveal
      lymphoid proliferations investigated represented EMZL, with the
      corresponding morphology and immunophenotype as seen in EMZL in other
      extranodal locations. MUM1, followed by CD38 expression, were the most
      constant plasma cell antigens in the plasmacytoid EMZL tumour cells, with
      both Vs38c and CD138 positivity being lost in many tumours. Aberrant
      immune profiles of plasma cell-related antigens may be of help in the
      establishment of malignancy in uveal lymphoproliferative lesions,
      particularly where interpretation of light chain expression and/or PCR
      results is difficult.
CI  - Copyright 2002 John Wiley & Sons, Ltd.
AD  - Department of Pathology, University Hospital Benjamin Franklin, Free
      University, Berlin, Germany. secoupland@yahoo.de
FAU - Coupland, Sarah E
AU  - Coupland SE
FAU - Foss, Hans-Dieter
AU  - Foss HD
FAU - Hidayat, Ahmed A
AU  - Hidayat AA
FAU - Cockerham, Glenn C
AU  - Cockerham GC
FAU - Hummel, Michael
AU  - Hummel M
FAU - Stein, Harald
AU  - Stein H
LA  - eng
PT  - Journal Article
CY  - England
TA  - J Pathol
JID - 0204634
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Biological Markers)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (IRF4 protein, human)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Transcription Factors)
RN  - 0 (monoclonal antibody VS38)
RN  - 0 (syndecan)
RN  - EC 3.2.2.- (T10 antigen)
RN  - EC 3.2.2.5 (NAD+ Nucleosidase)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal/analysis
MH  - Antigens, Differentiation/analysis
MH  - Biological Markers/analysis
MH  - Cell Differentiation
MH  - DNA-Binding Proteins/analysis
MH  - Female
MH  - Human
MH  - Immunohistochemistry/methods
MH  - Lacrimal Apparatus/chemistry
MH  - Lymphoma, B-Cell/*classification/pathology
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Middle Age
MH  - NAD+ Nucleosidase/analysis
MH  - Plasma Cells/pathology
MH  - Polymerase Chain Reaction/methods
MH  - Proteoglycans/analysis
MH  - Transcription Factors/analysis
MH  - Uveal Neoplasms/*classification/pathology
EDAT- 2002/07/13 10:00
MHDA- 2002/09/11 10:01
AID - 10.1002/path.1130 [doi]
PST - ppublish
SO  - J Pathol 2002 Jul;197(3):333-40.



UI  - 22106017
PMID- 12112370
DA  - 20020711
DCOM- 20020823
IS  - 0894-1491
VI  - 39
IP  - 1
DP  - 2002 Jul
TI  - Increased syndecan expression by pleiotrophin and FGF receptor-expressing
      astrocytes in injured brain tissue.
PG  - 1-9
AB  - Syndecan-1, -2, -3, and -4 are heparan sulfate proteoglycans that are
      differentially expressed during development and wound repair. To determine
      whether syndecans are also involved in brain injury, we examined the
      expression of syndecan core proteins genes in cryo-injured mouse brain,
      using in situ hybridization. All syndecan mRNA transcripts were similarly
      expressed in the region surrounding the necrotic tissue, exhibiting peak
      levels at day 7 after injury. Comparison with cellular markers showed that
      reactive astrocytes were the primary source of syndecans. Syndecans serve
      as co-receptors for fibroblast growth factor (FGF) and as a reservoir for
      another heparin-binding growth factor, pleiotrophin (PTN, or
      heparin-binding growth-associated molecule. In our model, FGF receptor1
      (FGFR1) and PTN mRNA levels were upregulated in reactive astrocytes. The
      distribution patterns of FGFR1 and PTN overlapped considerably with those
      of syndecan-1 and -3 mRNAs, respectively. These results suggest that
      syndecans are expressed primarily in reactive astrocytes, and may provide
      a supportive environment for regenerating axons in concert with
      heparin-binding growth factors (e.g., FGF and PTN) in the injured brain.
CI  - Copyright 2002 Wiley-Liss, Inc.
AD  - Department of Cell Science, Institute of Biomedical Sciences, Fukushima,
      Japan. ken@fmu.ac.jp
FAU - Iseki, Ken
AU  - Iseki K
FAU - Hagino, Seita
AU  - Hagino S
FAU - Mori, Tetsuji
AU  - Mori T
FAU - Zhang, Yuxiang
AU  - Zhang Y
FAU - Yokoya, Sachihiko
AU  - Yokoya S
FAU - Takaki, Hiromi
AU  - Takaki H
FAU - Tase, Choichiro
AU  - Tase C
FAU - Murakawa, Masahiro
AU  - Murakawa M
FAU - Wanaka, Akio
AU  - Wanaka A
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Glia
JID - 8806785
RN  - 0 (Carrier Proteins)
RN  - 0 (Cytokines)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (syndecan)
RN  - 134034-50-7 (pleiotrophin)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animal
MH  - Astrocytes/*metabolism
MH  - Brain Injuries/*metabolism/pathology
MH  - Carrier Proteins/*biosynthesis/genetics
MH  - Cytokines/*biosynthesis/genetics
MH  - Male
MH  - Membrane Glycoproteins/*biosynthesis/genetics
MH  - Mice
MH  - Mice, Inbred ICR
MH  - Proteoglycans/*biosynthesis/genetics
MH  - RNA, Messenger/biosynthesis
MH  - Receptor Protein-Tyrosine Kinases/*biosynthesis/genetics
MH  - Receptors, Fibroblast Growth Factor/*biosynthesis/genetics
MH  - Support, Non-U.S. Gov't
MH  - Up-Regulation/genetics
EDAT- 2002/07/12 10:00
MHDA- 2002/08/24 10:01
AID - 10.1002/glia.10078 [doi]
PST - ppublish
SO  - Glia 2002 Jul;39(1):1-9.



UI  - 22091931
PMID- 12097281
DA  - 20020704
DCOM- 20020808
IS  - 0008-5472
VI  - 62
IP  - 13
DP  - 2002 Jul 1
TI  - Neoglycans, carbodiimide-modified glycosaminoglycans: a new class of
      anticancer agents that inhibit cancer cell proliferation and induce
      apoptosis.
PG  - 3722-8
AB  - The soluble form of the syndecan-1 heparan sulfate proteoglycan acts as a
      tumor suppressor molecule that inhibits growth and induces apoptosis of
      some cancer cell lines in vitro. Analogs of syndecan-1 were produced by
      carbodiimide (EDAC) conjugation of glycosaminoglycan (GAG) chains to a
      protein scaffold, thereby generating synthetic proteoglycans that were
      evaluated for anticancer properties. Surprisingly, when analyzing
      activities of the controls, we discovered that EDAC modified GAG chains
      inhibit myeloma cell viability even in the absence of protein. Here, we
      describe the production and the activities of these novel molecules called
      neoglycans. The GAG chains heparin and chondroitin sulfate (CS) were
      exposed to EDAC to generate the neoglycans neoheparin and neoCS,
      respectively. Heparin and CS in the absence of EDAC modification have no
      effect or a slight growth promoting effect on cancer and normal cell
      lines. However, neoheparin and neoCS substantially reduce cell viability
      by induction of apoptosis of myeloma and breast cancer cells in vitro.
      NeoCS when injected directly into breast tumors growing in nude mice
      reduces or abolishes their growth without causing apparent toxicity to the
      adjacent normal tissue. The neoglycans need not be continuously present in
      cell cultures because a short pulse exposure is sufficient to reduce cell
      viability. NeoCS fractions purified by size exclusion chromatography
      reduce myeloma cell viability, confirming the specificity of neoglycan
      activity. Collectively, the results of this study demonstrate the
      anticancer activities of this new class of GAG chain-based molecules and
      provide the foundation for future development of neoglycans as novel
      therapeutic agents.
AD  - Arkansas Cancer Research Center, Department of Pathology, University of
      Arkansas for Medical Sciences, Little Rock, Arkansas 72205, USA.
FAU - Pumphrey, Carla Y
AU  - Pumphrey CY
FAU - Theus, Allison M
AU  - Theus AM
FAU - Li, Shulin
AU  - Li S
FAU - Parrish, Rudolph S
AU  - Parrish RS
FAU - Sanderson, Ralph D
AU  - Sanderson RD
LA  - eng
ID  - CA55819/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (Antineoplastic Agents)
RN  - 0 (Carbodiimides)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 141650-20-6 (1-ethyl-3-(3-dimethylaminoethyl)carbodiimide)
RN  - 9005-49-6 (Heparin)
RN  - 9007-28-7 (Chondroitin Sulfates)
SB  - IM
MH  - 3T3 Cells
MH  - Animal
MH  - Antineoplastic Agents/chemistry/*pharmacology
MH  - Apoptosis/drug effects
MH  - Breast Neoplasms/drug therapy
MH  - CHO Cells
MH  - Carbodiimides/chemistry/*pharmacology
MH  - Cell Division/drug effects
MH  - Cell Survival/drug effects
MH  - Chondroitin Sulfates/chemistry/pharmacology
MH  - Dogs
MH  - Drug Screening Assays, Antitumor
MH  - Female
MH  - Glycosaminoglycans/chemistry/*pharmacology
MH  - Hamsters
MH  - Heparin/chemical synthesis/pharmacology
MH  - Human
MH  - Membrane Glycoproteins/chemistry/pharmacology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Multiple Myeloma/drug therapy/pathology
MH  - Proteoglycans/chemistry/pharmacology
MH  - Support, U.S. Gov't, Non-P.H.S.
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Cells, Cultured
MH  - Xenograft Model Antitumor Assays
EDAT- 2002/07/05 10:00
MHDA- 2002/08/09 10:01
PST - ppublish
SO  - Cancer Res 2002 Jul 1;62(13):3722-8.



UI  - 22085832
PMID- 12091355
DA  - 20020701
DCOM- 20020830
IS  - 0006-4971
VI  - 100
IP  - 2
DP  - 2002 Jul 15
TI  - Soluble syndecan-1 promotes growth of myeloma tumors in vivo.
PG  - 610-7
AB  - Syndecan-1 (CD138) is a transmembrane heparan sulfate-bearing proteoglycan
      expressed by most myeloma plasma cells that regulates adhesion, migration,
      and growth factor activity. In patients with myeloma, shed syndecan-1
      accumulates in the bone marrow, and high levels of syndecan-1 in the serum
      are an indicator of poor prognosis. To test the effect of soluble
      syndecan-1 on tumor cell growth and dissemination, ARH-77 B-lymphoid cells
      were engineered to produce a soluble form of syndecan-1. Controls included
      vector only (neo)-transfected cells and cells transfected with full-length
      syndecan-1 complementary DNA that codes for the cell surface form of
      syndecan-1. Assays reveal that all 3 transfectants have similar growth
      rates in vitro, but cells expressing soluble syndecan-1 are hyperinvasive
      in collagen gels relative to controls. When injected into the marrow of
      human bones that were implanted in severe combined immunodeficient mice,
      tumors formed by cells expressing soluble syndecan-1 grow faster than
      tumors formed by neo-transfected cells or by cells expressing cell surface
      syndecan-1. In addition, cells bearing cell surface syndecan-1 exhibit a
      diminished capacity to establish tumors within the mice as compared with
      both neo- and soluble syndecan-1-transfected cells. Tumor cell
      dissemination to a contralateral human bone is detected significantly more
      often in the tumors producing soluble syndecan-1 than in controls. Thus,
      high levels of soluble syndecan-1 present in patients with myeloma may
      contribute directly to the growth and dissemination of the malignant cells
      and thus to poor prognosis.
AD  - Arkansas Cancer Research Center, Department of Pathology, and the Myeloma
      Institute for Research and Therapy, University of Arkansas for Medical
      Sciences, Little Rock, AR 72205, USA.
FAU - Yang, Yang
AU  - Yang Y
FAU - Yaccoby, Shmuel
AU  - Yaccoby S
FAU - Liu, Wei
AU  - Liu W
FAU - Langford, J Kevin
AU  - Langford JK
FAU - Pumphrey, Carla Y
AU  - Pumphrey CY
FAU - Theus, Allison
AU  - Theus A
FAU - Epstein, Joshua
AU  - Epstein J
FAU - Sanderson, Ralph D
AU  - Sanderson RD
LA  - eng
ID  - CA55819/CA/NCI
ID  - CA68494/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Bone Marrow/metabolism
MH  - Bone and Bones/pathology
MH  - Cell Division/drug effects
MH  - Cell Movement/drug effects
MH  - Human
MH  - Leukemia, Plasmacytic/etiology/metabolism/pathology
MH  - Membrane Glycoproteins/adverse effects/genetics/*physiology
MH  - Mice
MH  - Mice, Transgenic
MH  - Multiple Myeloma/etiology/metabolism/*pathology
MH  - Neoplasm Invasiveness
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/adverse effects/genetics/*physiology
MH  - Solubility
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transfection
MH  - Tumor Cells, Cultured/drug effects/metabolism
EDAT- 2002/07/02 10:00
MHDA- 2002/08/31 10:01
PST - ppublish
SO  - Blood 2002 Jul 15;100(2):610-7.



UI  - 22056914
PMID- 12061177
DA  - 20020613
DCOM- 20020712
IS  - 0042-773X
VI  - 48
IP  - 4
DP  - 2002 Apr
TI  - [Importance of selected laboratory indicators in the differential
      diagnosis and monitoring of multiple myeloma]
PG  - 290-7
AB  - Multiple myeloma is one of the most common haematologic malignancies.
      Currently there are numerous studies looking for new prognostic markers in
      multiple myeloma. The most important of them are the markers related to
      proliferative activity of neoplastic cells or to size of tumor mass. The
      subject of this paper are the results obtained from investigation of some
      such laboratory markers in a group of patients with monoclonal
      gammopathies diagnosed at our department in the last 3 years. We analyzed
      blood and bone marrow samples from 51 patients with new diagnosed
      monoclonal gammopathies, 14 of them were patients with monoclonal
      gammopathy of undetermined significance and 37 patients had multiple
      myeloma. 17 patients with multiple myeloma were treated by high-dose
      chemotherapy regimen. We assessed significance of selected laboratory
      markers for differential diagnosis of monoclonal gammopathies and for
      monitoring of activity of multiple myeloma. Among the investigated
      parameters, we verified the significance of cell cycle analysis of bone
      marrow plasmatic population and of the determination of the number of
      circulating myeloma cells in differential diagnosis of monoclonal
      gammopathies. In our opinion, the determination of soluble CD138, beta
      2-microglobulin and neopterin serum levels can be also recommended as
      helpful markers for a solution of this problem. Except of beta
      2-microglobulin serum level we did not find statistically significant
      correlation with activity of multiple myeloma in any of the investigated
      parameters.
AD  - Oddeleni klinicke hematologie FN, Hradec Kralove.
FAU - Maisnar, V
AU  - Maisnar V
FAU - Touskova, M
AU  - Touskova M
FAU - Maly, J
AU  - Maly J
FAU - Krejsek, J
AU  - Krejsek J
FAU - Kmonicek, M
AU  - Kmonicek M
FAU - Kopecky, O
AU  - Kopecky O
LA  - cze
PT  - Journal Article
TT  - Vyznam vybranych laboratornich ukazatelu pro diferencialni diagnostiku a
      sledovani aktivity mnohocetneho myelomu.
CY  - Czech Republic
TA  - Vnitr Lek
JID - 0413602
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (beta 2-Microglobulin)
RN  - 0 (syndecan)
RN  - 670-65-5 (Neopterin)
SB  - IM
MH  - Bone Marrow/*pathology
MH  - Diagnosis, Differential
MH  - English Abstract
MH  - Female
MH  - Human
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Middle Age
MH  - Multiple Myeloma/*diagnosis/drug therapy/pathology
MH  - Neopterin/analysis
MH  - Paraproteinemias/diagnosis
MH  - Proteoglycans/analysis
MH  - Support, Non-U.S. Gov't
MH  - Tumor Markers, Biological/*analysis
MH  - beta 2-Microglobulin/analysis
EDAT- 2002/06/14 10:00
MHDA- 2002/07/13 10:01
PST - ppublish
SO  - Vnitr Lek 2002 Apr;48(4):290-7.



UI  - 22054787
PMID- 12060120
DA  - 20020612
DCOM- 20020910
IS  - 0007-1048
VI  - 117
IP  - 4
DP  - 2002 Jun
TI  - Chromosomal aberrations are shared by malignant plasma cells and a small
      fraction of circulating CD19+ cells in patients with myeloma and
      monoclonal gammopathy of undetermined significance.
PG  - 852-9
AB  - In the present study, we aimed to identify distinct structural and
      numerical chromosomal aberrations in peripheral blood B cells of patients
      with myeloma and monoclonal gammopathy of undetermined significance
      (MGUS), which reflect changes thought to occur at different stages of the
      disease process. Peripheral blood from 12 patients with multiple myeloma
      and three patients with MGUS was investigated for the occurrence of
      retinoblastoma-1 gene deletions, p53 gene deletions and numerical
      aberrations demonstrated previously to be present in the patients' bone
      marrow CD138+ cells. By combining immunocytochemical staining for light
      chains and interphase fluorescence in situ hybridization (FISH), aberrant
      light-chain +ve cells were detected in the circulating CD19+ cell
      fraction. Each kind of chromosomal change present in the myeloma tumour
      cells was found to be shared by a small fraction of CD19+ cells (0.1-1.8%;
      median 0.36%, n = 6). In one MGUS patient, aberrant cells could be
      identified with a frequency of 0.34% within the CD19-sorted cell fraction.
      Clonotypic cells were detected with a frequency of 0.01-0.07% of
      peripheral blood nucleated cells by m-RNA in situ hybridization with
      patient-specific probes in three investigated patients. These results
      provide evidence that the circulating clonotypic B cells are closely
      related to the malignant plasma cells in myeloma and MGUS.
AD  - First Department of Internal Medicine and Medical Oncology,
      Wilhelminenspital, University of Vienna, Montleartstrasse 37, 1160 Vienna,
      Austria.
FAU - Zojer, Niklas
AU  - Zojer N
FAU - Schuster-Kolbe, Judith
AU  - Schuster-Kolbe J
FAU - Assmann, Irene
AU  - Assmann I
FAU - Ackermann, Jutta
AU  - Ackermann J
FAU - Strasser, Kathrin
AU  - Strasser K
FAU - Hubl, Wolfgang
AU  - Hubl W
FAU - Drach, Johannes
AU  - Drach J
FAU - Ludwig, Heinz
AU  - Ludwig H
LA  - eng
PT  - Journal Article
CY  - England
TA  - Br J Haematol
JID - 0372544
RN  - 0 (Antigens, CD19)
RN  - 0 (Disulfides)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulins, Light-Chain)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
RN  - 135949-60-9 (RB 101)
RN  - 63-91-2 (Phenylalanine)
SB  - IM
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, CD19/*immunology
MH  - Bone Marrow Examination
MH  - *Chromosome Aberrations
MH  - Chromosomes, Human, Pair 11
MH  - Chromosomes, Human, Pair 17
MH  - Clone Cells
MH  - Disease Progression
MH  - Disulfides
MH  - Gene Deletion
MH  - Genes, Immunoglobulin
MH  - Genes, Retinoblastoma
MH  - Genes, p53
MH  - Human
MH  - Immunoglobulin G
MH  - Immunoglobulins, Light-Chain
MH  - Immunohistochemistry/methods
MH  - In Situ Hybridization, Fluorescence
MH  - Membrane Glycoproteins
MH  - Middle Age
MH  - Multiple Myeloma/*genetics/immunology
MH  - Paraproteinemias/*genetics/immunology
MH  - Phenylalanine/*analogs & derivatives
MH  - Plasma Cells/*physiology
MH  - Polymerase Chain Reaction/methods
MH  - Proteoglycans
MH  - RNA, Messenger/analysis
MH  - Support, Non-U.S. Gov't
MH  - T-Lymphocytes/immunology/*physiology
EDAT- 2002/06/13 10:00
MHDA- 2002/09/11 10:01
AID - 3529 [pii]
PST - ppublish
SO  - Br J Haematol 2002 Jun;117(4):852-9.



UI  - 22162522
PMID- 12055189
DA  - 20020812
DCOM- 20020920
IS  - 0021-9258
VI  - 277
IP  - 33
DP  - 2002 Aug 16
TI  - Syndecan-2 mediates adhesion and proliferation of colon carcinoma cells.
PG  - 29730-6
AB  - Syndecan-2 is a transmembrane heparan sulfate proteoglycan whose function
      at the cell surface is unclear. In this study, we examined the function of
      syndecan-2 in colon cancer cell lines. In several colon cancer cell lines,
      syndecan-2 was highly expressed compared with normal cell lines. In
      contrast, syndecan-1 and -4 were decreased. Cell biological studies using
      the extracellular domain of recombinant syndecan-2 (2E) or spreading assay
      with syndecan-2 antibody-coated plates showed that syndecan-2 mediated
      adhesion and cytoskeletal organization of colon cancer cells. This
      interaction was critical for the proliferation of colon carcinoma cells.
      Blocking with 2E or antisense syndecan-2 cDNA induced G(0)/G(1) cell cycle
      arrest with concomitantly increased expression of p21, p27, and p53.
      Furthermore, blocking of syndecan-2 through antisense syndecan-2 cDNA
      significantly reduced tumorigenic activity in colon carcinoma cells.
      Therefore, increased syndecan-2 expression appears to be a critical for
      colon carcinoma cell behavior, and syndecan-2 regulates tumorigenic
      activity through regulation of adhesion and proliferation in colon
      carcinoma cells.
AD  - Department of Life Sciences, Division of Molecular Life Sciences and
      Center for Cell Signaling Research, Ewha Medical School, Ewha Women's
      University, Seoul 120-750 Korea.
FAU - Park, Haein
AU  - Park H
FAU - Kim, Yeonhee
AU  - Kim Y
FAU - Lim, Yangmi
AU  - Lim Y
FAU - Han, Innoc
AU  - Han I
FAU - Oh, Eok-Soo
AU  - Oh ES
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 149769-25-5 (fibroglycan)
SB  - IM
MH  - Adenocarcinoma/pathology
MH  - Base Sequence
MH  - Carcinoma/pathology
MH  - Cell Adhesion/*physiology
MH  - Cell Cycle
MH  - Cell Division/*physiology
MH  - Colonic Neoplasms/*pathology
MH  - DNA Primers
MH  - Flow Cytometry
MH  - Human
MH  - Membrane Glycoproteins/*physiology
MH  - Proteoglycans/*physiology
MH  - Support, Non-U.S. Gov't
EDAT- 2002/06/11 10:00
MHDA- 2002/09/21 10:01
PHST- 2002/Jun/07 [aheadofprint]
AID - 10.1074/jbc.M202435200 [doi]
AID - M202435200 [pii]
PST - ppublish
SO  - J Biol Chem 2002 Aug 16;277(33):29730-6.



UI  - 22018140
PMID- 12023357
DA  - 20020522
DCOM- 20020612
IS  - 0022-1767
VI  - 168
IP  - 11
DP  - 2002 Jun 1
TI  - CD9 is a unique marker for marginal zone B cells, B1 cells, and plasma
      cells in mice.
PG  - 5605-11
AB  - Marginal zone (MZ), follicular (FO), and B1 B cells form the long-lived
      naive B cell compartment. To identify surface markers that define MZ B
      cells in mice, we generated a panel of mAbs reactive with MZ but not FO B
      cells. One of these mAbs, MZ3, was found to recognize the tetraspanin CD9.
      CD9 expression not only distinguishes MZ B cells from FO B cells but also
      divided peritoneal cavity B1 cells into smaller subsets. After short-term
      in vitro stimulation with various mitogens, FO B cells failed to induce
      CD9 protein, while MZ B cells up-regulated the level of CD9 protein.
      However, after prolonged culture of FO B cells with LPS, surface CD9 was
      induced, together with syndecan 1, indicative of plasma cell
      differentiation. Following immunization with a T-independent-2 Ag, R36A,
      or a T-dependent Ag, SRBC, we found that CD9 is not expressed by germinal
      center B cells but is eventually expressed on plasma cells in response to
      both T-independent-2 and T-dependent Ags. Collectively, these results
      suggest that MZ B cells and B1 cell subsets are the immediate precursors
      of plasma cells in the primary response and that CD9 is acquired by
      T-dependent plasma cells.
AD  - Division of Developmental and Clinical Immunology and Department of
      Microbiology, University of Alabama, Birmingham, AL 35294, USA.
FAU - Won, Woong-Jai
AU  - Won WJ
FAU - Kearney, John F
AU  - Kearney JF
LA  - eng
ID  - AI14782/AI/NIAID
ID  - CA13148/CA/NCI
PT  - Journal Article
CY  - United States
TA  - J Immunol
JID - 2985117R
RN  - 0 (Antigens, CD)
RN  - 0 (Biological Markers)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (RNA, Messenger)
RN  - 147785-22-6 (CD9 antigen)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Antigens, CD/*analysis/genetics
MH  - B-Lymphocytes/*chemistry/physiology
MH  - Biological Markers
MH  - Cell Differentiation
MH  - Cells, Cultured
MH  - Lipopolysaccharides/pharmacology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred CBA
MH  - Plasma Cells/*chemistry/physiology
MH  - RNA, Messenger/analysis
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2002/05/23 10:00
MHDA- 2002/06/13 10:01
PST - ppublish
SO  - J Immunol 2002 Jun 1;168(11):5605-11.



UI  - 21997958
PMID- 12003262
DA  - 20020510
IS  - 0937-4477
VI  - 259
IP  - 3
DP  - 2002 Mar
TI  - Syndecan-1 expression in laryngeal cancer.
PG  - 115-8
AB  - Syndecan-1 is a member of the syndecan family of cell surface heparan
      sulphate proteoglycans. The aim of this study was the evaluation of
      syndecan-1 expression in laryngeal cancer. The findings were correlated
      both with the clinico-pathological parameters of the tumours and with
      patient survival. Paraffin-embedded samples from 48 patients with
      laryngeal cancer selected from the files of the ENT Department of the
      Medical Academy in Lublin were immunostained with anti-syndecan-1
      monoclonal antibody. The patients' mean age was 56 years, and 69% survived
      for over 3 years. Syndecan-1 immunoreactivity was observed in 48 (100%) of
      carcinomas. In our study, statistically significant correlations were
      observed both between syndecan-1 expression and patient survival
      (Chi-square = 4.364; P<0.05) and between syndecan-1 expression and
      clinical stage of disease (Chi-square = 4.363; P<0.05). Significant
      differences in syndecan-1 expression were also observed with various
      stages of histological differentiation of the carcinomas (Chi-square =
      6.588; P<0.05), and also according to the presence or absence of
      metastatic changes in the regional lymph nodes (Chi-square = 6.289;
      P<0.05). Our results indicate that syndecan-1 could be used as a
      prognostic marker in laryngeal cancer.
AD  - Otolaryngology Department, Medical Academy, Lublin, Poland.
FAU - Klatka, Janusz
AU  - Klatka J
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Eur Arch Otorhinolaryngol
JID - 9002937
SB  - IM
EDAT- 2002/05/11 10:00
MHDA- 2002/05/11 10:00
PST - ppublish
SO  - Eur Arch Otorhinolaryngol 2002 Mar;259(3):115-8.



UI  - 21976173
PMID- 11979781
DA  - 20020430
DCOM- 20020703
LR  - 20020723
IS  - 0047-1852
VI  - 60 Suppl 2
DP  - 2002 Feb
TI  - [Induction of syndecan-1 expression in parietal cells during gastric
      mucosal injury by NSAIDs]
PG  - 217-21
AD  - Third Department of Internal Medicine, Asahikawa Medical College.
FAU - Yokota, Kinichi
AU  - Yokota K
FAU - Satoh, Tomonobu
AU  - Satoh T
LA  - jpn
PT  - Journal Article
CY  - Japan
TA  - Nippon Rinsho
JID - 0420546
RN  - 0 (Anti-Inflammatory Agents, Non-Steroidal)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 50-78-2 (Aspirin)
SB  - IM
MH  - Animal
MH  - Anti-Inflammatory Agents, Non-Steroidal/*adverse effects
MH  - Apoptosis
MH  - Aspirin/adverse effects
MH  - Membrane Glycoproteins/*metabolism/physiology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Parietal Cells, Gastric/*metabolism/physiology
MH  - Proteoglycans/*metabolism/physiology
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Stomach Ulcer/chemically induced/metabolism
EDAT- 2002/05/01 10:00
MHDA- 2002/07/04 10:01
PST - ppublish
SO  - Nippon Rinsho 2002 Feb;60 Suppl 2:217-21.



UI  - 22075154
PMID- 11967265
DA  - 20020624
DCOM- 20020806
IS  - 0021-9258
VI  - 277
IP  - 26
DP  - 2002 Jun 28
TI  - ADAM13 disintegrin and cysteine-rich domains bind to the second
      heparin-binding domain of fibronectin.
PG  - 23336-44
AB  - ADAM13 is a member of the disintegrin and metalloprotease protein family
      that is expressed on cranial neural crest cells surface and is essential
      for their migration. ADAM13 is an active protease that can cleave
      fibronectin in vitro and remodel a fibronectin substrate in vivo. Using a
      recombinant secreted protein containing both disintegrin and cysteine-rich
      domains of ADAM13, we show that this "adhesive" region of the protein
      binds directly to fibronectin. Fibronectin fusion proteins corresponding
      to the various functional domains were used to define the second
      heparin-binding domain as the ADAM13 binding site. Mutation of the
      syndecan-binding site (PPRR --> PPTM) within this domain abolishes binding
      of the recombinant disintegrin and cysteine-rich domains of ADAM13. We
      further show that the adhesive disintegrin and cysteine-rich domain of
      ADAM13 can promote cell adhesion via beta(1) integrins. This adhesion
      requires integrin activation and can be prevented by antibodies to the
      cysteine-rich domain of ADAM13 and beta(1) integrin. Finally, wild type,
      but not the E/A mutant of ADAM13 metalloprotease domain, can be shed from
      the cell surface, releasing the metalloprotease domain associated with the
      disintegrin and cysteine-rich domains. This suggests that ADAM13 shedding
      may involve its own metalloprotease activity and that the released
      protease may interact with both integrins and extracellular matrix
      proteins.
AD  - Department of Cell Biology, University of Virginia School of Medicine,
      Charlottesville, Virginia 22908, USA.
FAU - Gaultier, Alban
AU  - Gaultier A
FAU - Cousin, Helene
AU  - Cousin H
FAU - Darribere, Thierry
AU  - Darribere T
FAU - Alfandari, Dominique
AU  - Alfandari D
LA  - eng
ID  - DE14365/DE/NIDCR
ID  - HD26402/HD/NICHD
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Antigens, CD29)
RN  - 0 (Disintegrins)
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 52-90-4 (Cysteine)
RN  - 9005-49-6 (Heparin)
RN  - EC 3.4.24 (Metalloendopeptidases)
SB  - IM
MH  - Animal
MH  - Antigens, CD29/metabolism
MH  - Binding Sites
MH  - Cell Line
MH  - Cell Movement
MH  - Cysteine
MH  - Disintegrins/*metabolism
MH  - Fibronectins/chemistry/*metabolism
MH  - Heparin/*metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Metalloendopeptidases/*metabolism
MH  - Proteoglycans/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2002/04/23 10:00
MHDA- 2002/08/07 10:01
PHST- 2002/Apr/19 [aheadofprint]
AID - 10.1074/jbc.M201792200 [doi]
AID - M201792200 [pii]
PST - ppublish
SO  - J Biol Chem 2002 Jun 28;277(26):23336-44.



UI  - 21931411
PMID- 11933459
DA  - 20020405
DCOM- 20020418
IS  - 1210-7875
VI  - 38
IP  - 1
DP  - 2002 Jan
TI  - [Syndecan-1 (CD138): an immunohistochemical marker of plasma cell tumors]
PG  - 33-6
AB  - The immunohistochemical detection of syndecan-1 (belonging to the cluster
      CD138) is a sensitive and reliable method for identifying normal and
      neoplastic plasma cells. It may be used in paraffin-embedded bone marrow
      specimens, as well as in extramedullary tumours of unknown origin. The
      three anaplastic tumours reported by us in the lymph node, the gingiva,
      and pleura were negative for other markers, but the syndecan-1 positivity
      elucidated their plasmocytic histogenesis.
AD  - Sikluv patologicko-anatomicky ustav Lekarske fakulty UK a Fakultni
      nemocnice, Plzen.
FAU - Fakan, F
AU  - Fakan F
FAU - Boudova, L
AU  - Boudova L
FAU - Hejda, C
AU  - Hejda C
LA  - cze
PT  - Journal Article
TT  - Syndecan-1 (CD138): imunohistochemicky marker nadoru z plazmatickych
      bunek.
CY  - Czech Republic
TA  - Cesk Patol
JID - 0050734
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - IM
MH  - Aged
MH  - Case Report
MH  - English Abstract
MH  - Female
MH  - Human
MH  - Immunohistochemistry
MH  - Male
MH  - Membrane Glycoproteins/*analysis
MH  - Middle Age
MH  - Multiple Myeloma/chemistry/diagnosis
MH  - Plasmacytoma/chemistry/*diagnosis
MH  - Proteoglycans/*analysis
MH  - Support, Non-U.S. Gov't
MH  - Tumor Markers, Biological/*analysis
EDAT- 2002/04/06 10:00
MHDA- 2002/04/19 10:01
PST - ppublish
SO  - Cesk Patol 2002 Jan;38(1):33-6.



UI  - 21920769
PMID- 11923257
DA  - 20020329
DCOM- 20020429
IS  - 0146-0404
VI  - 43
IP  - 4
DP  - 2002 Apr
TI  - Role of syndecan-1 in leukocyte-endothelial interactions in the ocular
      vasculature.
PG  - 1135-41
AB  - PURPOSE: Leukocyte endothelial interactions are a key feature of ocular
      angiogenesis but also play a role in nonproliferative vascular alterations
      as are found in early diabetes or uveitis. The adhesion of leukocytes to
      endothelial cells during inflammation is a multistep process that involves
      leukocyte rolling, adhesion, and extravasation mediated by selectins, cell
      adhesion molecules (CAMs), integrins, and chemokines. Heparan sulfate (HS)
      is known to bind to and modify the function of these molecules under
      physiological conditions. In this study, the role of the HS proteoglycan
      syndecan-1 in mediating leukocyte-endothelial interactions in the ocular
      vasculature was investigated. METHODS: Mice carrying a deletion in the
      gene encoding the cell surface HS proteoglycan syndecan-1 (sdc1) were used
      to study the interactions of leukocytes and endothelial cells in vivo,
      using a perfusion technique with FITC-coupled ConA and intravital
      microscopy. RESULTS: In a retina perfusion model, Sdc1(-/-) mice showed
      increased leukocyte adhesion that was largely attributable to the
      leukocytes. Intravital microscopy studies revealed a dramatic increase in
      adhesion after tumor necrosis factor (TNF)-alpha treatment of sdc1(-/-)
      mice compared with similarly treated wild-type mice. The higher degree of
      leukocyte adhesion may account for the increase in inflammation-mediated
      corneal angiogenesis observed in sdc1(-/-) mice. CONCLUSIONS: The results
      indicate a role for syndecan-1 as a negative regulator of
      leukocyte-mediated inflammatory responses. Thus, syndecan-1 could have use
      as a target for prevention of pathologic leukocyte-endothelial
      interactions in angiogenesis and inflammation.
AD  - Division of Newborn Medicine, Children's Hospital, Boston, Massachusetts
      02115, USA.
FAU - Gotte, Martin
AU  - Gotte M
FAU - Joussen, Antonia M
AU  - Joussen AM
FAU - Klein, Christoph
AU  - Klein C
FAU - Andre, Patrick
AU  - Andre P
FAU - Wagner, Denisa D
AU  - Wagner DD
FAU - Hinkes, Michael T
AU  - Hinkes MT
FAU - Kirchhof, Bernd
AU  - Kirchhof B
FAU - Adamis, Anthony P
AU  - Adamis AP
FAU - Bernfield, Merton
AU  - Bernfield M
LA  - eng
ID  - R01-CA-28735/CA/NCI
ID  - R01-EY-12611-01/EY/NEI
ID  - R01-HL-53756/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - Invest Ophthalmol Vis Sci
JID - 7703701
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Necrosis Factor)
RN  - 0 (fluorescein isothiocyanate-concanavalin A)
RN  - 0 (syndecan)
RN  - 11028-71-0 (Concanavalin A)
RN  - 3326-32-7 (Fluorescein-5-isothiocyanate)
SB  - IM
MH  - Animal
MH  - Bone Marrow Transplantation
MH  - Cell Adhesion/physiology
MH  - Concanavalin A
MH  - Cornea/blood supply/pathology
MH  - Corneal Neovascularization/*metabolism/pathology
MH  - Endothelium, Vascular/*metabolism
MH  - Fluorescein-5-isothiocyanate/*analogs & derivatives
MH  - Leukocytes/*metabolism
MH  - Membrane Glycoproteins/*physiology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Mice, Knockout
MH  - Proteoglycans/*physiology
MH  - Retinal Vessels/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Necrosis Factor/pharmacology
EDAT- 2002/03/30 10:00
MHDA- 2002/05/01 10:01
PST - ppublish
SO  - Invest Ophthalmol Vis Sci 2002 Apr;43(4):1135-41.



UI  - 21918085
PMID- 11918721
DA  - 20020328
DCOM- 20020508
IS  - 0022-202X
VI  - 118
IP  - 4
DP  - 2002 Apr
TI  - Inhibition of hair follicle growth by a laminin-1 G-domain peptide,
      RKRLQVQLSIRT, in an organ culture of isolated vibrissa rudiment.
PG  - 712-8
AB  - We established a serum-free organ culture system of isolated single
      vibrissa rudiments taken from embryonic day 13 mice. This system allowed
      us to test more than 30 laminin-derived cell adhesive peptides to
      determine their roles on the growth and differentiation of vibrissa hair
      follicles. We found that the RKRLQVQLSIRT sequence (designated AG-73),
      which mapped to the LG-4 module of the laminin-alpha1 chain
      carboxyl-terminal G domain, perturbed the growth of hair follicles in
      vitro. AG-73 is one of the cell-binding peptides identified from more than
      600 systematically synthesized 12 amino acid peptides covering the whole
      amino acid sequence of the laminin-alpha1, -beta1, and -gamma1 chains, by
      cell adhesion assay. Other cell-adhesive laminin peptides and a control
      scrambled peptide, LQQRRSVLRTKI, however, failed to show any significant
      effects on the growth of hair follicles. The AG-73 peptide binds to
      syndecan-1, a transmembrane heparan-sulfate proteoglycan. Syndecan-1 was
      expressed in both the mesenchymal condensation and the epithelial hair peg
      of developing vibrissa, suggesting that AG-73 binding to the cell surface
      syndecan-1 perturbed the epithelial-mesenchymal interactions of developing
      vibrissa. The formation of hair bulbs was aberrant in the explants treated
      with AG-73. In addition, impaired basement membrane formation, an abnormal
      cytoplasmic bleb formation, and an unusual basal formation of actin
      bundles were noted in the AG-73-treated-hair matrix epithelium, indicating
      that AG-73 binding perturbs various steps of epithelial morphogenesis,
      including the basement membrane remodeling. We also found a
      region-specific loss of the laminin-alpha1 chain in the basement membrane
      at the distal region of the invading hair follicle epithelium, indicating
      that laminins play a part in hair morphogenesis.
AD  - Department of Plastic and Reconstructive Surgery, Kitasato University
      School of Medicine, Kitasato, Sagamihara, Japan.
FAU - Hayashi, Kazuhiro
AU  - Hayashi K
FAU - Mochizuki, Mayumi
AU  - Mochizuki M
FAU - Nomizu, Motoyoshi
AU  - Nomizu M
FAU - Uchinuma, Eijyu
AU  - Uchinuma E
FAU - Yamashina, Shohei
AU  - Yamashina S
FAU - Kadoya, Yuichi
AU  - Kadoya Y
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Invest Dermatol
JID - 0426720
RN  - 0 (AG 73)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (laminin 1)
RN  - 0 (syndecan)
RN  - 151186-83-3 (laminin A)
SB  - IM
MH  - Animal
MH  - Epithelial Cells/chemistry/metabolism/ultrastructure
MH  - Female
MH  - Fetus/drug effects
MH  - Hair Follicle/cytology/*drug effects/*growth & development
MH  - Immunohistochemistry
MH  - In Vitro
MH  - Laminin/analysis/biosynthesis/metabolism/*pharmacology
MH  - Membrane Glycoproteins/analysis/biosynthesis
MH  - Mice
MH  - Mice, Inbred ICR
MH  - Microscopy, Immunoelectron
MH  - Organ Culture
MH  - Peptide Fragments/metabolism/*pharmacology
MH  - Pregnancy
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/analysis/biosynthesis
MH  - Support, Non-U.S. Gov't
MH  - Vibrissae/cytology/*drug effects/*growth & development
EDAT- 2002/03/29 10:00
MHDA- 2002/05/09 10:01
AID - 1730 [pii]
PST - ppublish
SO  - J Invest Dermatol 2002 Apr;118(4):712-8.



UI  - 21916527
PMID- 11918567
DA  - 20020328
DCOM- 20020531
LR  - 20020703
IS  - 0007-1048
VI  - 117
IP  - 1
DP  - 2002 Apr
TI  - Phenotyping primitive plasma cells.
PG  - 252-3
FAU - Joshua, Douglas
AU  - Joshua D
FAU - Pope, Belinda
AU  - Pope B
FAU - Brown, Ross
AU  - Brown R
FAU - Brown, Lisa
AU  - Brown L
FAU - Murray, Alan
AU  - Murray A
FAU - Gibson, John
AU  - Gibson J
LA  - eng
PT  - Comment
PT  - Letter
CY  - England
TA  - Br J Haematol
JID - 0372544
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Biological Markers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - EC 3.2.2.- (T10 antigen)
RN  - EC 3.2.2.5 (NAD+ Nucleosidase)
SB  - IM
CON - Br J Haematol. 1996 Jul;94(1):76-81. PMID: 8757512
CON - Br J Haematol. 1999 Sep;106(3):669-81. PMID: 10468855
CON - Br J Haematol. 2001 Jun;113(3):794-802. PMID: 11380472
MH  - Antigens, Differentiation/*analysis
MH  - Biological Markers/analysis
MH  - Flow Cytometry
MH  - Human
MH  - Immunophenotyping
MH  - Membrane Glycoproteins/*analysis
MH  - NAD+ Nucleosidase/*analysis
MH  - Plasma Cells/*immunology
MH  - Proteoglycans/*analysis
EDAT- 2002/03/29 10:00
MHDA- 2002/06/01 10:01
AID - 3406_5 [pii]
PST - ppublish
SO  - Br J Haematol 2002 Apr;117(1):252-3.



UI  - 21900367
PMID- 11904737
DA  - 20020320
DCOM- 20020606
IS  - 0939-5555
VI  - 81
IP  - 3
DP  - 2002 Mar
TI  - Syndecan-1 in B lymphoid malignancies.
PG  - 125-35
AB  - Syndecans are heparan sulfate-bearing proteoglycans that are found on the
      surface of most cells. Syndecan-1 is expressed predominantly on epithelia,
      but is also present on pre-B cells and plasma cells. The syndecans act to
      bind various effector molecules via their heparan sulfate chains,
      including both soluble and insoluble molecules within the extracellular
      milieu. These interactions promote cell adhesion to extracellular matrix
      and to adjacent cells. In addition, the syndecans can bind to and affect
      the biological activity of a number of heparin-binding growth factors.
      Thus, syndecan-1 can play a dramatic role in regulating cell behavior. In
      this review we discuss the expression of syndecan-1 on malignant B
      lymphoid cells as well as specific structure-function relationships of the
      molecule. Emphasis is placed on the important role that syndecan-1 has in
      regulating the growth of B lymphoid malignancies, particularly multiple
      myeloma.
AD  - Arkansas Cancer Research Center, Department of Pathology, Slot 517,
      University of Arkansas for Medical Sciences, 4301 West Markham, Little
      Rock, AR 72205, USA. sandersonralphd@uams.edu
FAU - Sanderson, R D
AU  - Sanderson RD
FAU - Borset, M
AU  - Borset M
LA  - eng
ID  - CA55819/CA/NCI
ID  - CA68494/CA/NCI
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
CY  - Germany
TA  - Ann Hematol
JID - 9107334
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Animal
MH  - B-Lymphocytes/*metabolism/*pathology
MH  - Human
MH  - Lymphoma/*metabolism/*pathology
MH  - Membrane Glycoproteins/*metabolism/physiology
MH  - Multiple Myeloma/*metabolism/*pathology
MH  - Proteoglycans/*metabolism/physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
RF  - 117
EDAT- 2002/03/21 10:00
MHDA- 2002/06/12 10:01
PHST- 2001/Dec/10 [received]
PHST- 2002/Jan/21 [accepted]
PHST- 2002/Mar/01 [aheadofprint]
AID - 10.1007/s00277-002-0437-8 [doi]
PST - ppublish
SO  - Ann Hematol 2002 Mar;81(3):125-35.



UI  - 21898286
PMID- 11900484
DA  - 20020319
DCOM- 20020503
IS  - 0014-4827
VI  - 274
IP  - 2
DP  - 2002 Apr 1
TI  - Immunoreactivity to cell surface syndecans in cytoplasm and nucleus:
      tubulin-dependent rearrangements.
PG  - 235-45
AB  - Syndecans are transmembrane proteoglycans implicated in the regulation of
      cell growth and differentiation, by interacting with growth factors.
      Although syndecans play a major role in regulating cell morphology, little
      is known about their subcellular distribution and in vivo association with
      the cytoskeleton. To address this question, we investigated the
      subcellular distribution and dynamic rearrangement of syndecans-1, -2, and
      -4, using confocal laser microscopy. Furthermore, we monitored the spatial
      relation of syndecans to tubulin in both mitotic and interphase cells.
      Initially, the reactivity to syndecans was confined to the cytoplasm,
      staining of the cell membranes appearing later. Syndecan-1 also seems to
      translocate to the nucleus in a time-dependent manner. The mitotic spindle
      shows unexpectedly more syndecans than that found in interphase cells.
      After vinblastine treatment, both syndecan-1 and tubulin were recovered as
      paracrystalline occlusion bodies, and the nuclear reactivity to syndecan-1
      disappeared, suggesting tubulin-mediated nuclear transport of this
      proteoglycan. Plasma membrane staining reappeared in the postmitotic
      cells. Nuclear translocation predominantly affected syndecan-1, whereas
      syndecan-2 and -4 remained in cytoplasm and cell membrane. This is the
      first report on regulated nuclear translocation and the presence of
      syndecan-1 in the mitotic spindle, where it may stabilize the mitotic
      machinery. The syndecan-1/tubulin complex may also act as a vehicle for
      the transport of protein growth factors to the cell nucleus.
CI  - Copyright 2002 Elsevier Science (USA).
AD  - Department of IMPI, Karolinska Institutet, Huddinge, S-14186, Sweden.
FAU - Brockstedt, Ulrika
AU  - Brockstedt U
FAU - Dobra, Katalin
AU  - Dobra K
FAU - Nurminen, Mervi
AU  - Nurminen M
FAU - Hjerpe, Anders
AU  - Hjerpe A
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Exp Cell Res
JID - 0373226
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tubulin)
RN  - 0 (syndecan)
SB  - IM
MH  - Active Transport, Cell Nucleus/*physiology
MH  - Animal
MH  - Cell Compartmentation/physiology
MH  - Cell Division/*physiology
MH  - Cell Membrane/*metabolism/ultrastructure
MH  - Cell Nucleus/*metabolism/ultrastructure
MH  - Human
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Mitotic Spindle Apparatus/*metabolism/ultrastructure
MH  - Protein Transport/physiology
MH  - Proteoglycans/*metabolism
MH  - Tubulin/*metabolism
MH  - Tumor Cells, Cultured
EDAT- 2002/03/20 10:00
MHDA- 2002/05/04 10:01
AID - 10.1006/excr.2002.5477 [doi]
AID - S0014482702954777 [pii]
PST - ppublish
SO  - Exp Cell Res 2002 Apr 1;274(2):235-45.



UI  - 21876674
PMID- 11882495
DA  - 20020307
DCOM- 20020408
LR  - 20020712
IS  - 0193-1849
VI  - 282
IP  - 4
DP  - 2002 Apr
TI  - Proteolysis-inducing factor differentially influences transcriptional
      regulation in endothelial subtypes.
PG  - E763-9
AB  - Proteolysis-inducing factor (PIF) is a novel sulfated glycoprotein
      initially identified as a protein capable of triggering muscle proteolysis
      during the process of cancer cachexia. Only skeletal muscle and liver
      exhibit substantial binding of PIF in adult tissue. Here, we demonstrate
      that PIF induces transcriptional regulation in both the liver endothelial
      cell line SK-HEP-1 and in human umbilical vein endothelial cells (HUVECs)
      but not in pulmonary artery endothelial cells. PIF differentially induces
      activation of nuclear factor-kappaB, resulting in the induction of
      proinflammatory cytokines [interleukin (IL)-8 and IL-6] and increased
      expression of the cell surface proteins intercellular adhesion molecule-1
      and vascular cell adhesion molecule in SK-HEP-1 and HUVECs only. In
      addition, PIF induces the shedding of syndecans from the cell surface.
      Syndecans are involved in wound repair, metastasis of cancers, and
      embryonic development. These results suggest that PIF may play additional
      roles in the proinflammatory response observed in cancer cachexia but may
      also have a role without the cachectic process.
AD  - Molecular Immunology Group, Department of Clinical and Surgical Sciences,
      University of Edinburgh, Edinburgh EH3 9YW, United Kingdom.
FAU - Watchorn, T M
AU  - Watchorn TM
FAU - Waddell, I
AU  - Waddell I
FAU - Ross, J A
AU  - Ross JA
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Am J Physiol Endocrinol Metab
JID - 100901226
RN  - 0 (Blood Proteins)
RN  - 0 (Interleukin-6)
RN  - 0 (Interleukin-8)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NF-kappa B)
RN  - 0 (Proteoglycans)
RN  - 0 (Ubiquitin)
RN  - 0 (Vascular Cell Adhesion Molecule-1)
RN  - 0 (proteolysis-inducing peptide)
RN  - 0 (syndecan)
RN  - 126547-89-5 (Intercellular Adhesion Molecule-1)
RN  - 149769-25-5 (fibroglycan)
SB  - IM
MH  - Blood Proteins/*pharmacology
MH  - Cell Line
MH  - Cells, Cultured
MH  - Endothelium/chemistry/drug effects/metabolism
MH  - Endothelium, Vascular/chemistry/drug effects/*metabolism
MH  - Gene Expression Regulation/*drug effects
MH  - Human
MH  - Intercellular Adhesion Molecule-1/analysis
MH  - Interleukin-6/secretion
MH  - Interleukin-8/secretion
MH  - Liver/metabolism
MH  - Membrane Glycoproteins/analysis
MH  - NF-kappa B/metabolism
MH  - Phosphorylation
MH  - Proteoglycans/analysis
MH  - Pulmonary Artery
MH  - Support, Non-U.S. Gov't
MH  - Transcription, Genetic/drug effects
MH  - Ubiquitin/metabolism
MH  - Umbilical Veins
MH  - Vascular Cell Adhesion Molecule-1/analysis
EDAT- 2002/03/08 10:00
MHDA- 2002/04/09 10:01
AID - 10.1152/ajpendo.00408.2001 [doi]
PST - ppublish
SO  - Am J Physiol Endocrinol Metab 2002 Apr;282(4):E763-9.



UI  - 21876994
PMID- 11882359
DA  - 20020307
DCOM- 20020503
IS  - 0301-472X
VI  - 30
IP  - 3
DP  - 2002 Mar
TI  - Leukemic B cells clonally identical to myeloma plasma cells are
      myelomagenic in NOD/SCID mice.
PG  - 221-8
AB  - OBJECTIVE: In multiple myeloma (MM), the immunoglobulin gene rearrangement
      characterizing malignant plasma cells is unique. For a patient with
      multiple myeloma who underwent a B-cell leukemic blast transformation,
      using the immunoglobulin molecular signature, we characterized the clonal
      relationship to autologous plasma cells and the impact on normal
      polyclonal B-lymphocyte populations. METHODS: Single-cell reverse
      transcriptase polymerase chain reaction (RT-PCR)/PCR was used to determine
      the clonal relationship between autologous MM plasma cells and leukemic B
      cells. A murine xenograft model was used to determine the myelomagenic
      potential of the leukemic B cells. RESULTS: Single-cell analysis showed
      that circulating leukemic-phase cells were clonotypic, with an IgH VDJ
      sequence identical to that of diagnosis plasma cells. Analysis of IgH
      transcripts indicates MM clonal dominance over normal B-cell components of
      the immune system at diagnosis and during leukemic disease. Leukemic B
      cells were xenografted to irradiated NOD/SCID mice, leading to lytic bone
      lesions and clonotypic cells in murine BM. Although human cells in murine
      BM expressed CD138, a marker largely absent from ex vivo leukemic cells,
      the expression of CD45, CD19, and CD20 confirmed that engrafting cells
      were mature, probably late-stage B cells rather than plasma cells.
      CONCLUSIONS: Leukemic B cells are able to exert strong clonal dominance
      over normal components of the immune system, colonize the murine BM in a
      xenograft model, and disrupt normal bone metabolism leading to lytic bone
      lesions. This supports the hypothesis that clonotypic MM B cells are
      reservoirs of disease that persist throughout therapy and give rise to
      relapse.
AD  - Department of Oncology, University of Alberta and Cross Cancer Institute,
      Edmonton, Alberta, Canada. lpilarski@gpu.srv.ualberta.ca
FAU - Pilarski, Linda M
AU  - Pilarski LM
FAU - Seeberger, Karen
AU  - Seeberger K
FAU - Coupland, Robert W
AU  - Coupland RW
FAU - Eshpeter, Alana
AU  - Eshpeter A
FAU - Keats, Jonathan J
AU  - Keats JJ
FAU - Taylor, Brian J
AU  - Taylor BJ
FAU - Belch, Andrew R
AU  - Belch AR
LA  - eng
ID  - CA80963/CA/NCI
PT  - Journal Article
CY  - Netherlands
TA  - Exp Hematol
JID - 0402313
RN  - 0 (Antigens, CD19)
RN  - 0 (Antigens, CD20)
RN  - 0 (Antigens, CD45)
RN  - 0 (Immunoglobulins, Heavy-Chain)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
SB  - IM
MH  - Animal
MH  - Antigens, CD19/analysis
MH  - Antigens, CD20/analysis
MH  - Antigens, CD45/analysis
MH  - B-Lymphocytes/immunology/pathology
MH  - Bone Marrow/*pathology
MH  - Clone Cells/*pathology
MH  - Comparative Study
MH  - Gene Rearrangement, B-Lymphocyte, Heavy Chain
MH  - Human
MH  - Immunoglobulins, Heavy-Chain/genetics
MH  - Leukemia, B-Cell/*genetics/immunology/pathology
MH  - Lymphocyte Transformation
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Mice
MH  - Mice, Inbred NOD
MH  - Mice, SCID
MH  - Multiple Myeloma/*genetics/immunology/pathology
MH  - Neoplasm Transplantation
MH  - Plasma Cells/pathology
MH  - Proteoglycans/analysis
MH  - RNA, Messenger/analysis
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transplantation, Heterologous
EDAT- 2002/03/08 10:00
MHDA- 2002/05/04 10:01
AID - S0301472X01007883 [pii]
PST - ppublish
SO  - Exp Hematol 2002 Mar;30(3):221-8.



UI  - 21866203
PMID- 11877746
DA  - 20020305
DCOM- 20020308
IS  - 0008-543X
VI  - 94
IP  - 4 Suppl
DP  - 2002 Feb 15
TI  - Comparison of the biologic effects of MA5 and B-B4 monoclonal antibody
      labeled with iodine-131 and bismuth-213 on multiple myeloma.
PG  - 1202-9
AB  - BACKGROUND: Using a specific monoclonal antibody (MAb), B-B4, coupled to
      bismuth-213 ((213)Bi) by a chelating agent (CITC-DTPA), the feasibility of
      alpha-radioimmunotherapy (RIT) for multiple myeloma (MM) has been
      demonstrated previously. METHODS: In this study, the two MAbs tested, MA5
      and B-B4, target the epithelial antigens Muc-1 and syndecan-1,
      respectively, which are both expressed by MM cell lines. Antibody
      characterization was evaluated by flow cytometric analysis of normal and
      tumoral hematopoeitic cells of MM patients as well as immunohistochemical
      tests of normal, nonhematopoetic tissues. Radiobiologic effects were
      evaluated for (213)Bi- and iodine-131 ((131)I)--labeled antibodies. We
      assessed in vitro mortality (thymidine incorporation, MTT, and clonogenic
      assays) and cell cycle modifications with propidium iodide staining. These
      tests were performed on MM cell lines until 120 hours postirradiation at
      several time points, using radiolabeled antibody concentrations ranging
      from 0.5 to 20 nM and specific activities ranging from 240 to 1200 MBq/mg
      of MAb. RESULTS: MA5 stained all MM cells in only 50% of patients, whereas
      B-B4 recognized all MM cells in all patients. B-B4 principally showed
      hepatic, pulmonary, and duodenal staining, whereas MA5 marked renal and
      pulmonary tissues. RIT with (213)Bi-B-B4 induced specific mortality and
      G(2)/M phase cell cycle arrest, which depended on the concentrations and
      specific activity. For (213)Bi-MA5, this arrest appeared at concentrations
      above 10 nM, an amount fivefold higher than that required with B-B4. This
      difference was also found in thymidine incorporation assays. Furthermore,
      with (213)Bi-B-B4, the arrest at the G(2)/M phase appeared quickly, within
      24 hours after irradiation, and affected up to 60% of the cells (for 20 nM
      of (213)Bi-B-B4 at 1,200 MBq/mg). Conversly, (131)I-B-B4 had a very
      limited effect on cell mortality and did not induce any cell cycle arrest.
      CONCLUSIONS: The results of this study show that B-B4 might be the more
      effective therapeutic antibody and suggest that alpha-RIT might be more
      suitable than beta-RIT for treating single-cell tumor models. Thus, these
      findings set the stage for the beginning of clinical trials using
      alpha-emitter--radiolabeled B-B4, with special attention paid to hepatic,
      pulmonary, and intestinal side effects.
CI  - Copyright 2002 American Cancer Society.
AD  - INSERM U463, Institut de Biologie, Nantes, France.
FAU - Supiot, Stephane
AU  - Supiot S
FAU - Faivre-Chauvet, Alain
AU  - Faivre-Chauvet A
FAU - Couturier, Olivier
AU  - Couturier O
FAU - Heymann, Marie Francoise
AU  - Heymann MF
FAU - Robillard, Nelly
AU  - Robillard N
FAU - Kraeber-Bodere, Francoise
AU  - Kraeber-Bodere F
FAU - Morandeau, Laurence
AU  - Morandeau L
FAU - Mahe, Marc Andre
AU  - Mahe MA
FAU - Cherel, Michel
AU  - Cherel M
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antineoplastic Agents)
RN  - 0 (Iodine Radioisotopes)
RN  - 0 (Radioisotopes)
RN  - 7440-69-9 (Bismuth)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/chemistry/*pharmacokinetics
MH  - Antineoplastic Agents/chemistry/*pharmacokinetics
MH  - Bismuth/chemistry/*pharmacokinetics
MH  - Cell Survival/drug effects
MH  - Cells, Cultured
MH  - Drug Delivery Systems/methods
MH  - G2 Phase/drug effects
MH  - Human
MH  - Iodine Radioisotopes/chemistry/*pharmacokinetics
MH  - Mitosis/drug effects
MH  - Multiple Myeloma/*metabolism/pathology
MH  - Radioimmunotherapy/methods
MH  - Radioisotopes
MH  - Radiotherapy
MH  - Tumor Cells, Cultured
EDAT- 2002/03/06 10:00
MHDA- 2002/03/09 10:01
AID - 10.1002/cncr.10286 [pii]
PST - ppublish
SO  - Cancer 2002 Feb 15;94(4 Suppl):1202-9.



UI  - 21858722
PMID- 11869291
DA  - 20020228
DCOM- 20020709
IS  - 0012-1592
VI  - 44
IP  - 1
DP  - 2002 Feb
TI  - Role of syndecan in the elongation of postoral arms in sea urchin larvae.
PG  - 45-53
AB  - Ac-SYN is the core protein of a cell surface proteoglycan of the sea
      urchin Anthocidaris crassispina. To examine the functions of Ac-SYN,
      embryos were cultured in the presence of affinity-purified antibody
      against Ac-SYN. At the late pluteus stage, severe inhibition of elongation
      of the postoral arms was seen in treated embryos compared with control
      embryos. Blastocoeleic microinjection of the antibody did not affect
      morphogenesis. The relationship between the number of cells in the
      postoral arms and the length of the postoral rods was investigated in
      normal embryos. This showed that postoral arm elongation has two phases:
      the first phase accompanies the increase in cell numbers while the second
      does not. The syndecan antibody inhibited the increase in cell numbers in
      the postoral arms. Furthermore, in the treated embryos, cell numbers
      continued to increase normally until 31 h post fertilization (hpf), while
      cell division stopped after 31 hpf. These results suggest that Ac-SYN
      participates in postoral arm formation via cell division in sea urchin
      embryos.
AD  - Department of Regulation Biology, Faculty of Science, Saitama University,
      Saitama, Saitama 338-8570, Japan.
FAU - Tomita, Kazuo
AU  - Tomita K
FAU - Yamasu, Kyo
AU  - Yamasu K
FAU - Suyemitsu, Takashi
AU  - Suyemitsu T
LA  - eng
PT  - Journal Article
CY  - Japan
TA  - Dev Growth Differ
JID - 0356504
RN  - 0 (Antibodies)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Animal
MH  - Antibodies/immunology
MH  - Blastocyst/physiology
MH  - Larva/growth & development/physiology
MH  - Membrane Glycoproteins/immunology/*physiology
MH  - Proteoglycans/immunology/*physiology
MH  - Sea Urchins/*embryology
EDAT- 2002/03/01 10:00
MHDA- 2002/07/10 10:01
AID - 617 [pii]
PST - ppublish
SO  - Dev Growth Differ 2002 Feb;44(1):45-53.



UI  - 21848230
PMID- 11859103
DA  - 20020222
DCOM- 20020315
IS  - 0022-1767
VI  - 168
IP  - 5
DP  - 2002 Mar 1
TI  - Correlation of tissue distribution, developmental phenotype, and
      intestinal homing receptor expression of antigen-specific B cells during
      the murine anti-rotavirus immune response.
PG  - 2173-81
AB  - The intestinal homing receptor, alpha(4)beta(7), helps target lymphocytes
      to Peyer's patches (PP) and intestinal lamina propria (ILP). We have
      previously shown that protective immunity to rotavirus (RV), an intestinal
      pathogen, resides in memory B cells expressing alpha(4)beta(7). In this
      study, using a novel FACS assay, we have directly studied the phenotype of
      B cells that express surface RV-specific Ig during the in vivo RV immune
      response. During primary infection, RV-specific B cells first appear as
      large IgD(-)B220(low)alpha(4)beta(7)(-)and alpha(4)beta(7)(+) cells
      (presumptive extrafollicular, Ab-secreting B cells), and then as large and
      small IgD(-)B220(high)alpha(4)beta(7)(-)cells (presumptive germinal center
      B cells). The appearance of B cells with the phenotype of large
      IgD(-)B220(low)alpha(4)beta(7)(+) cells in PP and most notably in
      mesenteric lymph nodes coincides with the emergence of RV-specific
      Ab-secreting cells (ASC) in the ILP. Thus, these B lymphocytes are good
      candidates for the migratory population giving rise to the RV-specific ASC
      in the ILP. RV-specific long-term memory B cells preferentially accumulate
      in PP and express alpha(4)beta(7). Nine months after infection most
      RV-specific IgA ASC are found in PP and ILP and at lower frequency in bone
      marrow and spleen. This study is the first to follow changes in
      tissue-specific homing receptor expression during Ag-specific B cell
      development in response to a natural host, tissue-specific pathogen. These
      results show that alpha(4)beta(7) is tightly regulated during the
      Ag-specific B cell response to RV and is expressed concurrently with the
      specific migration of memory and effector B cells to intestinal tissues.
AD  - Laboratory of Immunology and Vascular Biology, Department of Pathology,
      Stanford University School of Medicine, Stanford, CA 94305, USA.
      kry@stanford.edu
FAU - Youngman, Kenneth R
AU  - Youngman KR
FAU - Franco, Manuel A
AU  - Franco MA
FAU - Kuklin, Nelly A
AU  - Kuklin NA
FAU - Rott, Lusijah S
AU  - Rott LS
FAU - Butcher, Eugene C
AU  - Butcher EC
FAU - Greenberg, Harry B
AU  - Greenberg HB
LA  - eng
ID  - AI 3783/AI/NIAID
ID  - AI 47822/AI/NIAID
ID  - DK 10022/DK/NIDDK
ID  - DK 56339/DK/NIDDK
ID  - GM 37734/GM/NIGMS
ID  - R37 AI 21632/AI/NIAID
PT  - Journal Article
CY  - United States
TA  - J Immunol
JID - 2985117R
RN  - 0 (Antibodies, Viral)
RN  - 0 (Antigens, CD45)
RN  - 0 (Antigens, Viral)
RN  - 0 (Immunoglobulin D)
RN  - 0 (Integrins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (integrin alpha4beta7)
RN  - 0 (syndecan)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Antibodies, Viral/biosynthesis
MH  - Antigens, CD45/analysis
MH  - Antigens, Viral/immunology
MH  - B-Lymphocyte Subsets/classification/*immunology
MH  - Cell Movement
MH  - Flow Cytometry
MH  - Immunoglobulin D/analysis
MH  - Immunophenotyping
MH  - Integrins/analysis/*metabolism
MH  - Intestines/*immunology
MH  - Kinetics
MH  - Lymphoid Tissue/immunology
MH  - Membrane Glycoproteins/analysis
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Models, Immunological
MH  - Proteoglycans/analysis
MH  - Rotavirus/*immunology
MH  - Rotavirus Infections/*immunology
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.
MH  - Tissue Distribution
EDAT- 2002/02/23 10:00
MHDA- 2002/03/16 10:01
PST - ppublish
SO  - J Immunol 2002 Mar 1;168(5):2173-81.



UI  - 21845924
PMID- 11856308
DA  - 20020221
DCOM- 20020319
IS  - 0014-2956
VI  - 269
IP  - 2
DP  - 2002 Jan
TI  - Cell surface heparan sulfate proteoglycans: target and partners of the
      basic fibroblast growth factor in rat Sertoli cells.
PG  - 502-11
AB  - Basic fibroblast growth factor (bFGF) regulates diversified biological
      functions in rat Sertoli cells. This report demonstrates that bFGF
      inhibits steroidogenesis in developing rat Sertoli cells. Follicle
      stimulating hormone (FSH)-stimulated estradiol production was reduced by
      bFGF. Moreover, the amount of cytochrome P450 aromatase, responsible for
      the irreversible transformation of androgens into estrogens, is decreased
      by bFGF at the transcriptional level. The bFGF inhibitory effect was also
      observed in the presence of dibutyryl-cAMP, cholera toxin or RO-20-1724,
      all inducing high levels of cAMP, the second messenger of FSH. Heparan
      sulfate proteoglycans (HSPGs) were shown to be required as cofactors for
      bFGF signaling. Indeed, sodium chlorate, described to drastically decrease
      proteoglycan sulfation, abolishes the bFGF downregulation of
      FSH-stimulated estradiol synthesis previously observed. Glypican-1,
      syndecan-1 and -4, potential bFGF coreceptors, are mainly regulated at the
      transcriptional level. This report shows that the bFGF regulation of their
      expression specifically depends on the nature of HSPG and of the Sertoli
      cell developmental stage. In conclusion, HSPG are partners and the target
      of bFGF in rat Sertoli cells.
AD  - Laboratoire de Biochimie, IRBA, Universite de Caen, France.
      s_brucato@yahoo.fr
FAU - Brucato, Sylvie
AU  - Brucato S
FAU - Bocquet, Jean
AU  - Bocquet J
FAU - Villers, Corinne
AU  - Villers C
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Eur J Biochem
JID - 0107600
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 50-28-2 (Estradiol)
RN  - 9002-68-0 (Follicle Stimulating Hormone)
RN  - EC 1.14.13.- (Aromatase)
SB  - IM
MH  - Animal
MH  - Aromatase/genetics
MH  - Cell Adhesion/physiology
MH  - Cell Membrane/metabolism
MH  - Cells, Cultured
MH  - Estradiol/biosynthesis
MH  - Fibroblast Growth Factor 2/*metabolism/physiology
MH  - Follicle Stimulating Hormone/pharmacology
MH  - Gene Expression Regulation/physiology
MH  - Heparan Sulfate Proteoglycan/chemistry/genetics/*metabolism
MH  - Male
MH  - Membrane Glycoproteins/genetics
MH  - Proteoglycans/genetics
MH  - RNA, Messenger/genetics
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sertoli Cells/cytology/metabolism
EDAT- 2002/02/22 10:00
MHDA- 2002/03/20 10:01
AID - 2672 [pii]
PST - ppublish
SO  - Eur J Biochem 2002 Jan;269(2):502-11.



UI  - 21839829
PMID- 11850808
DA  - 20020218
DCOM- 20020227
IS  - 0950-9232
VI  - 21
IP  - 5
DP  - 2002 Jan 24
TI  - HOXD3 enhances motility and invasiveness through the TGF-beta-dependent
      and -independent pathways in A549 cells.
PG  - 798-808
AB  - Homeobox genes regulate sets of genes that determine cellular fates in
      embryonic morphogenesis and maintenance of adult tissue architecture by
      regulating cellular motility and cell-cell interactions. Our previous
      studies showed that a specific member, HOXD3, when overexpressed,
      upregulates integrin beta3 expression in human erythroleukemia HEL cells
      and lung cancer A549 cells, and enhances their motility and invasiveness.
      We performed a microarray study of over 7075 genes to determine the
      mechanisms underlying the HOXD3-enhanced motility and invasiveness in A549
      cells. RT-PCR-based tracking gene analyses highlighted a set of
      TGF-beta-upregulated genes, which included matrix metalloproteinase-2,
      syndecan-1, CD44, and TGF-beta-induced 68 kDa protein. Exogenous TGF-beta
      also caused this pattern of upregulation in A549 cells and enhanced their
      migratory and invasive activity, confirming the involvement of TGF-beta
      signaling. However, HOXD3 reduced the expression of TGF-beta-independent
      genes coding for desmosomal components such as desmoglein, desmoplakin and
      plakoglobin which are known to suppress tumor invasion and metastasis.
      These results suggest that HOXD3 enhances the invasive and metastatic
      potential of cancer cells through the TGF-beta-dependent and -independent
      pathways.
AD  - Division of Cancer-Related Genes, Institute for Genetic Medicine, Hokkaido
      University, Kita-15, Nishi-7, Kita-ku, Sapporo 060-0815, Japan.
FAU - Miyazaki, Yasumasa J
AU  - Miyazaki YJ
FAU - Hamada, Jun-ichi
AU  - Hamada J
FAU - Tada, Mitsuhiro
AU  - Tada M
FAU - Furuuchi, Keiji
AU  - Furuuchi K
FAU - Takahashi, Yoko
AU  - Takahashi Y
FAU - Kondo, Satoshi
AU  - Kondo S
FAU - Katoh, Hiroyuki
AU  - Katoh H
FAU - Moriuchi, Tetsuya
AU  - Moriuchi T
LA  - eng
PT  - Journal Article
CY  - England
TA  - Oncogene
JID - 8711562
RN  - 0 (Homeodomain Proteins)
RN  - 0 (Hoxd-3 protein)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (Transforming Growth Factor beta)
SB  - IM
MH  - *Cell Movement
MH  - Down-Regulation
MH  - Gene Expression Profiling
MH  - Homeodomain Proteins/genetics/*physiology
MH  - Neoplasm Invasiveness
MH  - Neoplasms/genetics/*metabolism/pathology
MH  - Oligonucleotide Array Sequence Analysis
MH  - RNA, Neoplasm/biosynthesis
MH  - *Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Transforming Growth Factor beta/biosynthesis/*pharmacology
MH  - Tumor Cells, Cultured
MH  - Up-Regulation
EDAT- 2002/02/19 10:00
MHDA- 2002/03/19 10:01
PHST- 2001/Apr/30 [received]
PHST- 2001/Oct/02 [revised]
PHST- 2001/Oct/29 [accepted]
AID - 10.1038/sj/onc/1205126 [doi]
PST - ppublish
SO  - Oncogene 2002 Jan 24;21(5):798-808.



UI  - 21831457
PMID- 11842937
DA  - 20020214
DCOM- 20020604
IS  - 0022-3484
VI  - 37
IP  - 1
DP  - 2002 Feb
TI  - Effects of interleukin-4 on proteoglycan accumulation in human gingival
      fibroblasts.
PG  - 42-9
AB  - In inflammatory gingival diseases, cytokines have been demonstrated to
      play critical roles by coordinating the stimulation of immunological and
      connective tissue cells. The activities of these cells, degrading and
      remodeling extracellular matrices, constitute the major pathological and
      repair processes. Thus, elucidating cellular and molecular events
      occurring in inflamed connective tissues is crucial for the understanding
      and treatment of inflammation. In order to test a hypothesis that
      proinflammatory cytokines affect metabolism of major extracellular matrix
      molecules, we studied metabolism of proteoglycans (PGs) by human gingival
      fibroblasts (HGF) under the influence of interleukin-4 (IL-4) as a model
      of gingivitis. HGF in cell culture were metabolically radiolabeled using
      [3H]glucosamine and [35S]sulfate in the presence or absence of IL-4, and
      the labeled PGs were analyzed by chromatographic techniques. The
      incorporation of 35S into PGs increased with IL-4 both in media and cell
      layer. At 100 ng/ml of IL-4, the increment of 35S incorporation over
      control culture was 16-39% (p<0.001) in media and 12-35% (p=0.01) in cell
      layer. The 35S-labeled macromolecules were PGs containing heparan sulfate
      (HS) and chondroitin sulfate (CS) chains. From the molecular weight and
      glycosaminoglycan composition analyses, versican and perlecan-type and
      biglycan and decorin-type were very likely to be the major PG constituents
      both in media and cell layer. IL-4 stimulated synthesis of versican and
      perlecan-type more potently than biglycan and decorin-type. With IL-4
      treatment, the ratio of CSPG/HSPG decreased in media and increased in cell
      layer. This ratio suggested that syndecan family HSPGs were also present
      in HGF. In conclusion, IL-4 stimulated accumulation of CS/HSPGs in human
      gingival fibroblasts.
AD  - Department of Hard Tissue Engineering, Periodontology, Graduate School,
      Tokyo Medical and Dental University, Japan.
FAU - Hashimoto-Uoshima, M
AU  - Hashimoto-Uoshima M
FAU - Noguchi, K
AU  - Noguchi K
FAU - Suzuki, M
AU  - Suzuki M
FAU - Murata, A
AU  - Murata A
FAU - Yanagishita, M
AU  - Yanagishita M
FAU - Ishikawa, I
AU  - Ishikawa I
LA  - eng
PT  - Journal Article
CY  - Denmark
TA  - J Periodontal Res
JID - 0055107
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Lectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteochondroitin Sulfates)
RN  - 0 (Proteoglycans)
RN  - 0 (Radiopharmaceuticals)
RN  - 0 (Sulfur Radioisotopes)
RN  - 0 (Transforming Growth Factor beta)
RN  - 0 (decorin)
RN  - 0 (syndecan)
RN  - 10028-17-8 (Tritium)
RN  - 123939-84-4 (biglycan)
RN  - 126968-45-4 (versican)
RN  - 143972-95-6 (perlecan)
RN  - 207137-56-2 (Interleukin-4)
RN  - 3416-24-8 (Glucosamine)
RN  - 9007-28-7 (Chondroitin Sulfates)
SB  - D
SB  - IM
MH  - Adult
MH  - Cell Culture
MH  - Chondroitin Sulfates/analysis
MH  - Chromatography, Agarose
MH  - Chromatography, Ion Exchange
MH  - Extracellular Matrix Proteins/analysis/*metabolism
MH  - Female
MH  - Fibroblasts/*metabolism
MH  - Gingiva/cytology/*metabolism
MH  - Gingivitis/metabolism
MH  - Glucosamine/diagnostic use
MH  - Glycosaminoglycans/analysis
MH  - Heparan Sulfate Proteoglycan/analysis
MH  - Human
MH  - Interleukin-4/*pharmacology
MH  - Lectins
MH  - Membrane Glycoproteins/analysis
MH  - Molecular Weight
MH  - Proteochondroitin Sulfates/analysis
MH  - Proteoglycans/analysis/*metabolism
MH  - Radiopharmaceuticals/diagnostic use
MH  - Sulfur Radioisotopes/diagnostic use
MH  - Support, Non-U.S. Gov't
MH  - Transforming Growth Factor beta/antagonists & inhibitors
MH  - Tritium/diagnostic use
EDAT- 2002/02/15 10:00
MHDA- 2002/06/05 10:01
PST - ppublish
SO  - J Periodontal Res 2002 Feb;37(1):42-9.



UI  - 21818538
PMID- 11830493
DA  - 20020206
DCOM- 20020425
IS  - 0006-4971
VI  - 99
IP  - 4
DP  - 2002 Feb 15
TI  - Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor
      binding and promotes Met signaling in multiple myeloma.
PG  - 1405-10
AB  - Heparan sulfate proteoglycans (HSPGs) play a crucial role in growth
      regulation by assembling signaling complexes and presenting growth factors
      to their cognate receptors. Within the immune system, expression of the
      HSPG syndecan-1 (CD138) is characteristic of terminally differentiated B
      cells, ie, plasma cells, and their malignant counterpart, multiple myeloma
      (MM). This study explored the hypothesis that syndecan-1 might promote
      growth factor signaling and tumor growth in MM. For this purpose, the
      interaction was studied between syndecan-1 and hepatocyte growth factor
      (HGF), a putative paracrine and autocrine regulator of MM growth. The
      study demonstrates that syndecan-1 is capable of binding HGF and that this
      growth factor is indeed a potent stimulator of MM survival and
      proliferation. Importantly, the interaction of HGF with heparan sulfate
      moieties on syndecan-1 strongly promotes HGF-mediated signaling, resulting
      in enhanced activation of Met, the receptor tyrosine kinase for HGF.
      Moreover, HGF binding to syndecan-1 promotes activation of the
      phosphatidylinositol 3-kinase/protein kinase B and RAS/mitogen-activated
      protein kinase pathways, signaling routes that have been implicated in the
      regulation of cell survival and proliferation, respectively. These results
      identify syndecan-1 as a functional coreceptor for HGF that promotes
      HGF/Met signaling in MM cells, thus suggesting a novel function for
      syndecan-1 in MM tumorigenesis.
AD  - Department of Pathology, Academic Medical Center, University of Amsterdam,
      The Netherlands.
FAU - Derksen, Patrick W B
AU  - Derksen PW
FAU - Keehnen, Robert M J
AU  - Keehnen RM
FAU - Evers, Ludo M
AU  - Evers LM
FAU - van Oers, Marinus H J
AU  - van Oers MH
FAU - Spaargaren, Marcel
AU  - Spaargaren M
FAU - Pals, Steven T
AU  - Pals ST
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Blood
JID - 7603509
RN  - 0 (MAP Kinase Signaling System)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (proto-oncogene protein akt)
RN  - 0 (syndecan)
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - EC 2.7.1.137 (1-Phosphatidylinositol 3-Kinase)
RN  - EC 2.7.11.- (Proto-Oncogene Protein c-met)
RN  - EC 3.6.1.- (ras Proteins)
SB  - AIM
SB  - IM
MH  - 1-Phosphatidylinositol 3-Kinase/metabolism
MH  - Cell Division/drug effects
MH  - Enzyme Activation
MH  - Hepatocyte Growth Factor/*metabolism
MH  - Human
MH  - MAP Kinase Signaling System
MH  - Membrane Glycoproteins/metabolism/*pharmacology/physiology
MH  - Multiple Myeloma/etiology/*metabolism/pathology
MH  - Protein Binding
MH  - Proteoglycans/metabolism/*pharmacology/physiology
MH  - Proto-Oncogene Protein c-met/genetics/metabolism/*physiology
MH  - Proto-Oncogene Proteins/metabolism
MH  - Signal Transduction/*drug effects
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - ras Proteins/metabolism
EDAT- 2002/02/07 10:00
MHDA- 2002/04/26 10:01
PST - ppublish
SO  - Blood 2002 Feb 15;99(4):1405-10.



UI  - 21666312
PMID- 11807222
DA  - 20020124
DCOM- 20020307
IS  - 0022-1317
VI  - 83
IP  - Pt 2
DP  - 2002 Feb
TI  - Characterization of pseudorabies virus glycoprotein C attachment to
      heparan sulfate proteoglycans.
PG  - 301-9
AB  - Pseudorabies virus first attaches to cells through an interaction between
      the envelope glycoprotein C (gC) and the cell surface heparan sulfate (HS)
      that is linked to proteoglycans (HSPGs). The HS-binding domain of gC is
      composed of three discrete heparin-binding domains (HBDs), designated
      HBD1, -2 and -3 for their proximity to the amino terminus of gC. Each HBD
      can independently mediate virus attachment to HS, yet each also exhibits a
      distinct binding preference for differentially sulfated derivatives of
      heparin. To demonstrate this, affinity columns composed of wild-type gC or
      mutant gC retaining a single HBD to capture several HSPGs from cultured
      pig and bovine kidney cells were used. The wild-type gC column bound all
      of the HSPGs well and, overall, bound more than 90% of the total sample
      applied to the column. Columns composed of either HBD2 or -3 bound
      intermediate amounts (40%) of the total sample applied, while the HBD1
      column bound low amounts of HSPGs. HBD2 and -3 columns did not uniformly
      bind all of the HSPGs from bovine kidney cells, but the same HSPGs were
      bound with equal efficiency on each column. Thus, despite their different
      preferences for sulfation patterns on HS side-chains, HBD2 and -3 appear
      to bind the same proteoglycan cores. These results established a hierarchy
      of HBD2=HBD3>HBD1 in importance for HSPG binding. These in vitro-binding
      results correlated with the attachment phenotype of virus strains
      expressing gC with a single HBD in their envelopes.
AD  - Department of Molecular Sciences, University of Tennessee Health Science
      Center, 858 Madison Avenue, Room 201, Memphis, TN 38163, USA.
FAU - Rue, Cary A
AU  - Rue CA
FAU - Ryan, Patrick
AU  - Ryan P
LA  - eng
PT  - Journal Article
CY  - England
TA  - J Gen Virol
JID - 0077340
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (pseudorabies virus glycoproteins)
RN  - 0 (syndecan)
RN  - 9004-34-6 (Cellulose)
SB  - IM
MH  - Animal
MH  - Cattle
MH  - Cell Line
MH  - Cellulose/metabolism
MH  - Heparan Sulfate Proteoglycan/chemistry/genetics/*metabolism
MH  - Herpesvirus 1, Suid/*pathogenicity/physiology
MH  - Kidney/cytology
MH  - L Cells (Cell Line)
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Proteoglycans/metabolism
MH  - Pseudorabies/*virology
MH  - Recombinant Fusion Proteins/chemistry/genetics/metabolism
MH  - Swine
MH  - Viral Envelope Proteins/chemistry/genetics/*metabolism
EDAT- 2002/01/25 10:00
MHDA- 2002/03/08 10:01
PST - ppublish
SO  - J Gen Virol 2002 Feb;83(Pt 2):301-9.



UI  - 21655489
PMID- 11796840
DA  - 20020117
DCOM- 20020228
IS  - 0893-3952
VI  - 15
IP  - 1
DP  - 2002 Jan
TI  - The level of syndecan-1 expression is a distinguishing feature in behavior
      between keratoacanthoma and invasive cutaneous squamous cell carcinoma.
PG  - 45-9
AB  - Keratoacanthoma (KA) resolves spontaneously but is regarded by some as a
      variant of squamous cell carcinoma (SCC). However, others consider KA a
      totally benign entity. Syndecan-1 is one of the heparan sulfate
      proteoglycans that mediates intercellular and cell to matrix adhesion. Its
      expression appears to be inversely correlated with tumor aggressiveness
      and invasiveness. Previous studies have shown decreased levels of
      syndecan-1 expression in invasive cutaneous SCC, correlating with tumor
      de-differentiation. However, a similar study has never been done on KA. To
      investigate syndecan-1 expression in classic KA and compare the results
      with those of classic invasive SCC, 24 KAs were immunostained for
      syndecan-1 (CD 138) using the monoclonal antibody B-B4 on formalin-fixed
      paraffin-embedded tissue. Results were semi-quantitatively scored as
      either negative or positive (mild, moderate, or strong) and compared with
      those previously obtained on 23 invasive SCC and in situ lesions. All 24
      KAs were positive for syndecan-1 expression. Staining intensity of 18
      cases was comparable with that of SCC in situ or adjacent normal
      epidermis. By comparison, invasive SCC showed significantly diminished
      staining. Reduced staining in focal areas of cytologic atypia at the base
      was present in three KAs. Syndecan-1 expression in KA mirrors that of SCC
      in situ and normal epidermis, providing a molecular basis that
      biologically KA may be closely related to SCC in situ but distinctively
      different from invasive SCC.
AD  - Department of Pathology, University of Arkansas for Medical Sciences, 4301
      W. Markham, Little Rock, AR 72205, USA. mukunyadziperkins@uams.edu
FAU - Mukunyadzi, Perkins
AU  - Mukunyadzi P
FAU - Sanderson, Ralph D
AU  - Sanderson RD
FAU - Fan, Chun-Yang
AU  - Fan CY
FAU - Smoller, Bruce R
AU  - Smoller BR
LA  - eng
ID  - CA 68494/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JID - 8806605
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Carcinoma in Situ/*metabolism/pathology
MH  - Carcinoma, Squamous Cell/*metabolism/pathology
MH  - Diagnosis, Differential
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Keratoacanthoma/*metabolism/pathology
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Neoplasm Invasiveness
MH  - Proteoglycans/*biosynthesis
MH  - Skin Neoplasms/*metabolism/pathology
MH  - Stromal Cells/metabolism/pathology
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2002/01/18 10:00
MHDA- 2002/03/01 10:01
PST - ppublish
SO  - Mod Pathol 2002 Jan;15(1):45-9.



UI  - 21645767
PMID- 11786412
DA  - 20020111
DCOM- 20020705
IS  - 0002-9440
VI  - 160
IP  - 1
DP  - 2002 Jan
TI  - Heparan sulfate proteoglycans as regulators of fibroblast growth factor-2
      receptor binding in breast carcinomas.
PG  - 185-94
AB  - Binding of fibroblast growth factors (FGFs) to their tyrosine
      kinase-signaling receptors (FGFRs) requires heparan sulfate (HS). HS
      proteoglycans (HSPGs) determine mitogenic responses of breast carcinoma
      cells to FGF-2 in vitro. For this study, we examined the role of HSPGs as
      modulators of FGF-2 binding to FGFR-1 in situ and in vitro. During
      stepwise reconstitution of the FGF-2/HSPG/FGFR-1 complex in situ, we
      identified an elevated ability of breast carcinoma cell HSPGs to promote
      receptor complex formation compared to normal breast epithelium. HSPGs
      isolated from the MCF-7 breast-carcinoma cell line were then fractionated
      according to their ability to assemble the FGF-2 receptor complex. All
      MCF-7 HSPGs are decorated with HS chains similarly capable of promoting
      FGF-2 receptor complex formation. In this in vitro model, syndecan-1 and
      syndecan-4 are the cell surface HSPGs contributing most to the complex
      formation. Relative expression levels of these syndecans in human breast
      carcinoma tissues correlate well with receptor complex formation in situ,
      indicating that in breast carcinomas, core protein levels determine FGF-2
      receptor complex formation. However, variances in syndecan expression
      levels do not explain the difference in FGF-2 receptor complex formation
      between normal and malignant epithelial cells, suggesting that alterations
      in HS structure occur during malignant transformation.
AD  - Department of Pathology and Laboratory Medicine, University of
      Wisconsin-Madison, Madison, Wisconsin 52792-8550, USA.
FAU - Mundhenke, Christoph
AU  - Mundhenke C
FAU - Meyer, Kristy
AU  - Meyer K
FAU - Drew, Sally
AU  - Drew S
FAU - Friedl, Andreas
AU  - Friedl A
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Am J Pathol
JID - 0370502
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - EC 2.7.1.- (fibroblast growth factor receptor 2)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - AIM
SB  - IM
MH  - Breast Neoplasms/*metabolism
MH  - Carcinoma/*metabolism
MH  - Female
MH  - Fibroblast Growth Factor 2/metabolism
MH  - Heparan Sulfate Proteoglycan/*physiology
MH  - Human
MH  - Membrane Glycoproteins/metabolism
MH  - Protein Processing, Post-Translational
MH  - Proteoglycans/metabolism
MH  - Receptor Protein-Tyrosine Kinases/*metabolism
MH  - Receptors, Fibroblast Growth Factor/*metabolism
MH  - Tissue Distribution
EDAT- 2002/01/12 10:00
MHDA- 2002/07/06 10:01
PST - ppublish
SO  - Am J Pathol 2002 Jan;160(1):185-94.



UI  - 21640541
PMID- 11781374
DA  - 20020108
DCOM- 20020131
IS  - 0022-1007
VI  - 195
IP  - 1
DP  - 2002 Jan 7
TI  - Fc gamma receptors and cross-presentation in dendritic cells.
PG  - F1-3
AD  - INSERM U520, Institut Curie, 75005 Paris, France. sebas@curie.fr
FAU - Amigorena, Sebastian
AU  - Amigorena S
LA  - eng
PT  - Comment
PT  - Journal Article
CY  - United States
TA  - J Exp Med
JID - 2985109R
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (MAGE-3 antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NY-ESO-1 protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, IgG)
RN  - 0 (syndecan)
SB  - IM
CON - J Exp Med. 2002 Jan 7;195(1):125-33. PMID: 11781371
MH  - Antibodies, Neoplasm/*immunology
MH  - *Antigen Presentation
MH  - Antigens, Neoplasm/*immunology
MH  - Autoimmunity
MH  - Dendritic Cells/*immunology
MH  - Immune Tolerance
MH  - Membrane Glycoproteins/immunology
MH  - Neoplasm Proteins/immunology
MH  - Proteins/immunology
MH  - Proteoglycans/immunology
MH  - Receptors, IgG/*metabolism
MH  - T-Lymphocytes, Cytotoxic/immunology
EDAT- 2002/01/10 10:00
MHDA- 2002/02/01 10:01
PST - ppublish
SO  - J Exp Med 2002 Jan 7;195(1):F1-3.



UI  - 21640538
PMID- 11781371
DA  - 20020108
DCOM- 20020131
IS  - 0022-1007
VI  - 195
IP  - 1
DP  - 2002 Jan 7
TI  - Antitumor monoclonal antibodies enhance cross-presentation ofcCellular
      antigens and the generation of myeloma-specific killer T cells by
      dendritic cells.
PG  - 125-33
AB  - The mechanism of antitumor effect of monoclonal antibodies (mAbs) is not
      fully understood. Here we show that coating myeloma cells with
      anti-syndecan-1 antibody promotes cross-presentation of cellular antigens
      by dendritic cells (DCs) to autologous T cells from healthy donors. The
      tumor cells treated with anti-syndecan-1 or isotype-matched control
      antibody were fed to HLA-mismatched monocyte-derived immature DCs. Tumor
      cell-loaded mature DCs induced a strong CD8(+) T cell response that was
      specific for the cancer-testis (C-T) antigens expressed in the tumor. The
      CD8(+) T cells killed peptide-pulsed targets, as well as myeloma tumor
      cells. Importantly, mAbs-coated tumor-loaded DCs were consistently
      superior to DCs loaded with peptides or dying cells for eliciting
      tumor-specific killer T cells. This enhanced cross-presentation was not
      due to enhanced tumor cell uptake or to DC maturation. When mixtures of
      NY-Eso-1-positive and -negative myeloma cells were captured by DCs, the
      anti-syndecan-1 antibody had to be on the NY-Eso-1-positive cells to
      elicit NY-Eso-1-specific response. Cross-presentation was inhibited by
      pretreatment of DCs with Fc gamma receptor blocking antibodies. Targeting
      of mAb-coated tumors to DCs may contribute to the efficacy of
      tumor-reactive mAb and offers a new strategy for immunotherapy.
AD  - Laboratory of Tumor Immunology and Immunotherapy, The Rockefeller
      University, New York, NY 10021, USA.
FAU - Dhodapkar, Kavita M
AU  - Dhodapkar KM
FAU - Krasovsky, Joseph
AU  - Krasovsky J
FAU - Williamson, Barbara
AU  - Williamson B
FAU - Dhodapkar, Madhav V
AU  - Dhodapkar MV
LA  - eng
ID  - CA81138/CA/NCI
ID  - M0-RR00102/RR/NCRR
PT  - Journal Article
CY  - United States
TA  - J Exp Med
JID - 2985109R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (MAGE-3 antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NY-ESO-1 protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, IgG)
RN  - 0 (syndecan)
RN  - 82115-62-6 (Interferon Type II)
SB  - IM
CIN - J Exp Med. 2002 Jan 7;195(1):F1-3. PMID: 11781374
MH  - Antibodies, Monoclonal/immunology/pharmacology
MH  - Antibodies, Neoplasm/*immunology/pharmacology
MH  - *Antigen Presentation
MH  - Antigens, Neoplasm/*immunology
MH  - Apoptosis
MH  - Dendritic Cells/*immunology
MH  - Human
MH  - Immunotherapy
MH  - Interferon Type II/secretion
MH  - Killer Cells/*immunology
MH  - Male
MH  - Membrane Glycoproteins/immunology
MH  - Multiple Myeloma/*therapy
MH  - Neoplasm Proteins/immunology
MH  - Proteins/immunology
MH  - Proteoglycans/immunology
MH  - Receptors, IgG/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - T-Lymphocytes/*immunology
MH  - Testicular Neoplasms/immunology
EDAT- 2002/01/10 10:00
MHDA- 2002/02/01 10:01
PST - ppublish
SO  - J Exp Med 2002 Jan 7;195(1):125-33.



UI  - 21637968
PMID- 11779146
DA  - 20020107
DCOM- 20020225
IS  - 0006-291X
VI  - 290
IP  - 1
DP  - 2002 Jan 11
TI  - Expression and characterization of minican, a recombinant syndecan-1 with
      extensively truncated core protein.
PG  - 146-52
AB  - Syndecan-1 is an integral membrane heparan sulfate/chondroitin sulfate
      proteoglycan, involved in the control of cell growth and differentiation.
      The biological activities of syndecan-1 involve interactions with a
      variety of extracellular ligands, such as growth factors and matrix
      components, that are mainly mediated by the heparan sulfate moieties. The
      expression of syndecan-1 is downregulated in various malignant tumors, and
      low levels of expression appear to correlate with poor prognosis of some
      cancer types. On the other hand, the extracellular portion of syndecan-1
      (ectodomain) has been demonstrated to inhibit the proliferation of various
      cancer cells in culture, suggesting that proteoglycan-like molecules
      should be studied further with regard to their antitumor activities. We
      have expressed, in CHO cells, a truncated syndecan-1 ectodomain
      ("minican") harboring domains for glycosaminoglycan attachment and
      antibody recognition. Analysis of recombinant minican indicates that it
      shares some of the biochemical and biological characteristics attributed
      to syndecan-1 ectodomain. Minican was thus substituted with heparan
      sulfate chains and bound to extracellular matrix proteins as well as
      fibroblast growth factors. Notably, minican inhibited the proliferation of
      S115 mouse mammary carcinoma cells and the effect seemed to involve
      inhibition of the Ras/Erk signaling pathway. Our data suggest that
      recombinant syndecan-1 with a minimal protein component is biologically
      active. This information may provide useful in further design of
      proteoglycan-like antitumor molecules.
CI  - (c)2002 Elsevier Science.
AD  - Turku Centre for Biotechnology, University of Turku and Abo Akademi
      University, Tykistokatu 6, BioCity, FIN-20520, Turku, Finland.
FAU - Viklund, Leif
AU  - Viklund L
FAU - Loo, Britt-Marie
AU  - Loo BM
FAU - Hermonen, Jorma
AU  - Hermonen J
FAU - El-Darwish, Kamel
AU  - El-Darwish K
FAU - Jalkanen, Markku
AU  - Jalkanen M
FAU - Salmivirta, Markku
AU  - Salmivirta M
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Biochem Biophys Res Commun
JID - 0372516
RN  - 0 (Culture Media, Serum-Free)
RN  - 0 (DNA, Complementary)
RN  - 0 (Disaccharides)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (minican)
RN  - 0 (syndecan)
RN  - 57-85-2 (Testosterone)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 2.7.1.- (Mitogen-Activated Protein Kinases)
RN  - EC 3.6.1.- (ras Proteins)
RN  - EC 4.2.2. (Polysaccharide-Lyases)
RN  - EC 4.2.2.4 (Chondroitin ABC Lyase)
RN  - EC 4.2.2.8 (heparitinsulfate lyase)
SB  - IM
MH  - Animal
MH  - Blotting, Northern
MH  - Blotting, Western
MH  - CHO Cells
MH  - Cell Division/drug effects
MH  - Chondroitin ABC Lyase/metabolism
MH  - Cloning, Molecular
MH  - Culture Media, Serum-Free/pharmacology
MH  - DNA, Complementary/metabolism
MH  - Disaccharides/chemistry
MH  - Dose-Response Relationship, Drug
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Extracellular Matrix/metabolism
MH  - Fibroblast Growth Factors/metabolism
MH  - Glycosaminoglycans/chemistry
MH  - Hamsters
MH  - Heparitin Sulfate/chemistry
MH  - Membrane Glycoproteins/*biosynthesis/*chemistry
MH  - Mice
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Peptide Fragments/*biosynthesis/*chemistry
MH  - Phosphorylation
MH  - Polysaccharide-Lyases/metabolism
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/*biosynthesis/*chemistry
MH  - Recombinant Proteins/*biosynthesis/*chemistry
MH  - Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Testosterone/pharmacology
MH  - Time Factors
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - ras Proteins/metabolism
EDAT- 2002/01/10 10:00
MHDA- 2002/02/28 10:01
AID - 10.1006/bbrc.2001.6187 [doi]
AID - S0006291X0196187X [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun 2002 Jan 11;290(1):146-52.



UI  - 21607909
PMID- 11743640
DA  - 20011214
DCOM- 20020213
IS  - 1019-6439
VI  - 20
IP  - 1
DP  - 2002 Jan
TI  - Syndecan-1 expression in cancer of the uterine cervix: association with
      lymph node metastasis.
PG  - 39-43
AB  - The development of carcinoma is associated with alterations in the
      expression of many cell adhesion molecules. Syndecan-1 is a cell surface
      proteoglycan that binds cells to the extracellular matrix and changes its
      expression following malignant transformation in some tumors. Our purpose
      was to examine the pattern of syndecan-1 expression in cancer of the
      uterine cervix and assess the clinicopathological significance of
      syndecan-1 expression. A total of 106 tissue specimens (6 normal, 19
      cervical intraepithelial neoplasia (CIN) and 81 invasive cancer) were
      analyzed immunohistochemically. In addition, the corresponding expression
      of mRNA in tumor tissues was evaluated by reverse transcription-polymerase
      chain reaction (RT/PCR) in comparison with normal counterparts. Syndecan-1
      was positive in normal squamous cells except the basal cell layer. The
      intensity of syndecan-1 staining was the strongest in normal epithelium,
      followed by CIN, and invasive squamous cell carcinoma. Syndecan-1
      expression in cancer tissue tended to be higher in keratinizing type than
      non-keratinizing type and not found in adenocarcinoma. Syndecan-1
      expression was markedly decreased at the mRNA level in invasive squamous
      cell carcinoma as compared with that of normal uterine cervix.
      Interestingy, there was an inverse correlation between the expression of
      syndecan-1 in the primary site and lymph node metastasis, although there
      was no significant correlation between syndecan-1 expression and the
      prognosis. The results of the present study suggest that syndecan-1
      expression is associated with squamous tissues and plays a key role in the
      progression of the cancer of the uterine cervix especially in the
      metastatic process.
AD  - Department of Obstetrics and Gynecology, Yamaguchi University School of
      Medicine, Yamaguchi 755-8505, Japan. fnuma@po.cc.yamaguchi-u.ac.jp
FAU - Numa, Fumitaka
AU  - Numa F
FAU - Hirabayashi, Kei
AU  - Hirabayashi K
FAU - Kawasaki, Keiko
AU  - Kawasaki K
FAU - Sakaguchi, Yuko
AU  - Sakaguchi Y
FAU - Sugino, Norihiro
AU  - Sugino N
FAU - Suehiro, Yutaka
AU  - Suehiro Y
FAU - Suminami, Yoshinori
AU  - Suminami Y
FAU - Hirakawa, Hiroshi
AU  - Hirakawa H
FAU - Umayahara, Kenji
AU  - Umayahara K
FAU - Nawata, Shugo
AU  - Nawata S
FAU - Ogata, Hidenobu
AU  - Ogata H
FAU - Kato, Hiroshi
AU  - Kato H
LA  - eng
PT  - Journal Article
CY  - Greece
TA  - Int J Oncol
JID - 9306042
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Carcinoma, Adenosquamous/*metabolism/secondary
MH  - Cervical Intraepithelial Neoplasia/*metabolism/secondary
MH  - Cervix Neoplasms/*metabolism/secondary
MH  - Cervix Uteri/metabolism
MH  - DNA Primers/chemistry
MH  - Female
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Leiomyoma/metabolism
MH  - Lymphatic Metastasis
MH  - Membrane Glycoproteins/*biosynthesis/genetics
MH  - Middle Age
MH  - Neoplasm Proteins/*biosynthesis/genetics
MH  - Proteoglycans/*biosynthesis/genetics
MH  - RNA, Messenger/biosynthesis
MH  - Reverse Transcriptase Polymerase Chain Reaction
EDAT- 2001/12/18 10:00
MHDA- 2002/02/14 10:01
PST - ppublish
SO  - Int J Oncol 2002 Jan;20(1):39-43.



