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Gene Review

SDC1  -  syndecan 1

Homo sapiens

Synonyms: CD138, SDC, SYND1, Syndecan-1, syndecan
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Disease relevance of SDC1

  • Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma [1].
  • In comparison with bile ductular cells of normal liver, reactive ductules in chronic cholestasis were marked by an elevated expression of syndecan-1, surrounded by an increased perlecan expression [2].
  • These data reveal changes in the expression of syndecan-1, syndecan-3, and perlecan in human chronic cholestatic liver disease, that may be important in the deposition of matrix components and activation of growth factors that support ductular reaction and accompanying fibrogenesis [2].
  • These data reinforce the role of the tumor stroma in ovarian adenocarcinoma and suggest that stromal induction of syndecan-1 contributes to the pathogenesis of this malignancy [3].
  • For HPV11 infectivity assays, a high virion inoculum was required to infect K562 cells, whereas ectopic expression of syndecan-1 increased permissiveness eightfold and expression of syndecan-4 or glypican-1 fourfold [4].

High impact information on SDC1

  • Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2 [5].
  • We find that this control can be imposed by the soluble syndecan-1 ectodomain, a heparan sulfate proteoglycan shed from cell surfaces into wound fluids [5].
  • The syndecan family of cell-surface heparan sulfate proteoglycans participate in multiple cell behaviors ranging from growth factor signaling to cell adhesion [6].
  • Syndecan captures, protects, and transmits HIV to T lymphocytes [7].
  • The B lymphocyte-induced maturation protein (Blimp-1) upregulates the expression of syndecan-1 and J chain and represses that of c-myc [8].

Chemical compound and disease context of SDC1


Biological context of SDC1


Anatomical context of SDC1


Associations of SDC1 with chemical compounds

  • Increased expression of SDC1 may account in part for the hypotriglyceridemic effect that can result from the administration of chenodeoxycholic acid to humans [14].
  • Specific glycosaminoglycan lyase digestions, followed by product analyses using fluorescence-assisted carbohydrate electrophoresis and immunoprecipitation experiments, showed that the p53 form is associated with syndecan-1 through both chondroitin sulfate and heparan sulfate [19].
  • We conclude that ADAMTS-4 activation in this cell system involves the coordinated activity of both glycosylphosphatidyl inositol-anchored MT4-MMP and the proteoglycan form of syndecan-1 on the cell surface [19].
  • These results indicate that several HSPGs can serve as HPV receptors and support a putative role for syndecan-1, rather than alpha6 integrin, as a primary receptor protein in natural HPV infection of keratinocytes [4].
  • Although the proteolytic cleavage of IGFBP-rP1 decreased its heparin-binding activity, the cleaved form could bind syndecan-1 efficiently [20].
  • We propose that tyrosine dephosphorylation of syndecan-1 may regulate its association with cytoskeleton components [21].

Physical interactions of SDC1


Enzymatic interactions of SDC1


Regulatory relationships of SDC1

  • These results suggest that the shedding of syndecan-1 promoted by MT1-MMP through the preferential cleavage of Gly245-Leu246 peptide bond stimulates cell migration [15].
  • Thus, current studies demonstrate that hepatic SDC1 is induced in an FXR isoform-specific manner [14].
  • In contrast, syndecan-1 shedding induced by 12-O-tetradecanoylphorbol-13-acetate treatment was inhibited by BB-94 but not by either TIMP-1 or TIMP-2 [15].
  • CCR5 is therefore involved in the RANTES-induced accelerated shedding of SD-1 and SD-4 ectodomains [22].
  • Shedding of syndecan-1 was also induced by MT3-MMP but not by other MT-MMPs [15].

Other interactions of SDC1

  • These results support a specific role for shed syndecan-1 or MMP7-syndecan-1 complexes in tumor progression and add to accumulating evidence that syndecans and glypicans have nonequivalent functions in vivo [27].
  • Treatment of cells with MMP inhibitor BB-94 or tissue inhibitor of MMP (TIMP)-2 but not TIMP-1 interfered with the syndecan-1 shedding promoted by MT1-MMP expression [15].
  • Stromal expression of syndecan-1 and glypican-1 were poor prognostic factors for survival in univariate analysis [3].
  • The detection of a variant form of syndecan-3 as a major stromal HSPG suggests a specific role for this syndecan in haemopoiesis [28].
  • Furthermore, the close correlation between syndecan expression and negative ER status raises the possibility of hormonal regulation or more likely an association with an aggressive, ER-negative carcinoma phenotype [29].

Analytical, diagnostic and therapeutic context of SDC1


  1. Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma. Derksen, P.W., Keehnen, R.M., Evers, L.M., van Oers, M.H., Spaargaren, M., Pals, S.T. Blood (2002) [Pubmed]
  2. Heparan sulfate proteoglycan expression in chronic cholestatic human liver diseases. Roskams, T., Rosenbaum, J., De Vos, R., David, G., Desmet, V. Hepatology (1996) [Pubmed]
  3. Distribution and clinical significance of heparan sulfate proteoglycans in ovarian cancer. Davies, E.J., Blackhall, F.H., Shanks, J.H., David, G., McGown, A.T., Swindell, R., Slade, R.J., Martin-Hirsch, P., Gallagher, J.T., Jayson, G.C. Clin. Cancer Res. (2004) [Pubmed]
  4. Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses. Shafti-Keramat, S., Handisurya, A., Kriehuber, E., Meneguzzi, G., Slupetzky, K., Kirnbauer, R. J. Virol. (2003) [Pubmed]
  5. Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. Kato, M., Wang, H., Kainulainen, V., Fitzgerald, M.L., Ledbetter, S., Ornitz, D.M., Bernfield, M. Nat. Med. (1998) [Pubmed]
  6. Molecular interactions of the syndecan core proteins. Rapraeger, A.C., Ott, V.L. Curr. Opin. Cell Biol. (1998) [Pubmed]
  7. Syndecan captures, protects, and transmits HIV to T lymphocytes. Bobardt, M.D., Saphire, A.C., Hung, H.C., Yu, X., Van der Schueren, B., Zhang, Z., David, G., Gallay, P.A. Immunity (2003) [Pubmed]
  8. Differential effect of B lymphocyte-induced maturation protein (Blimp-1) expression on cell fate during B cell development. Messika, E.J., Lu, P.S., Sung, Y.J., Yao, T., Chi, J.T., Chien, Y.H., Davis, M.M. J. Exp. Med. (1998) [Pubmed]
  9. Porphyromonas gingivalis lipopolysaccharide induces shedding of syndecan-1 expressed by gingival epithelial cells. Andrian, E., Grenier, D., Rouabhia, M. J. Cell. Physiol. (2005) [Pubmed]
  10. The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells. Beauvais, D.M., Burbach, B.J., Rapraeger, A.C. J. Cell Biol. (2004) [Pubmed]
  11. Epithelial syndecan-1 expression is associated with stage and grade in colorectal cancer. Lundin, M., Nordling, S., Lundin, J., Isola, J., Wiksten, J.P., Haglund, C. Oncology (2005) [Pubmed]
  12. Reduced syndecan-1 expression stimulates heparin-binding growth factor-mediated invasion in ovarian cancer cells in a urokinase-independent mechanism. Matsuzaki, H., Kobayashi, H., Yagyu, T., Wakahara, K., Kondo, T., Kurita, N., Sekino, H., Inagaki, K., Suzuki, M., Kanayama, N., Terao, T. Oncol. Rep. (2005) [Pubmed]
  13. Role of heparan sulfate proteoglycan (syndecan-1) on the renal epithelial cells during calcium oxalate monohydrate crystal attachment. Chikama, S., Iida, S., Inoue, M., Kawagoe, N., Tomiyasu, K., Matsuoka, K., Noda, S., Takazono, I. The Kurume medical journal. (2002) [Pubmed]
  14. Syndecan-1 expression is regulated in an isoform-specific manner by the farnesoid-X receptor. Anisfeld, A.M., Kast-Woelbern, H.R., Meyer, M.E., Jones, S.A., Zhang, Y., Williams, K.J., Willson, T., Edwards, P.A. J. Biol. Chem. (2003) [Pubmed]
  15. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. Endo, K., Takino, T., Miyamori, H., Kinsen, H., Yoshizaki, T., Furukawa, M., Sato, H. J. Biol. Chem. (2003) [Pubmed]
  16. The role of syndecan cytoplasmic domain in basic fibroblast growth factor-dependent signal transduction. Volk, R., Schwartz, J.J., Li, J., Rosenberg, R.D., Simons, M. J. Biol. Chem. (1999) [Pubmed]
  17. Induced expression of syndecan-1 in the stroma of head and neck squamous cell carcinoma. Mukunyadzi, P., Liu, K., Hanna, E.Y., Suen, J.Y., Fan, C.Y. Mod. Pathol. (2003) [Pubmed]
  18. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. Cohen, A.R., Woods, D.F., Marfatia, S.M., Walther, Z., Chishti, A.H., Anderson, J.M., Wood, D.F. J. Cell Biol. (1998) [Pubmed]
  19. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. Gao, G., Plaas, A., Thompson, V.P., Jin, S., Zuo, F., Sandy, J.D. J. Biol. Chem. (2004) [Pubmed]
  20. Proteolytic processing of IGFBP-related protein-1 (TAF/angiomodulin/mac25) modulates its biological activity. Ahmed, S., Yamamoto, K., Sato, Y., Ogawa, T., Herrmann, A., Higashi, S., Miyazaki, K. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  21. Tyrosine dephosphorylation of the syndecan-1 PDZ binding domain regulates syntenin-1 recruitment. Sulka, B., Lortat-Jacob, H., Terreux, R., Letourneur, F., Rousselle, P. J. Biol. Chem. (2009) [Pubmed]
  22. RANTES (CCL5) induces a CCR5-dependent accelerated shedding of syndecan-1 (CD138) and syndecan-4 from HeLa cells and forms complexes with the shed ectodomains of these proteoglycans as well as with those of CD44. Charnaux, N., Brule, S., Chaigneau, T., Saffar, L., Sutton, A., Hamon, M., Prost, C., Lievre, N., Vita, C., Gattegno, L. Glycobiology (2005) [Pubmed]
  23. Plasminogen activator inhibitor-1 supports IL-8-mediated neutrophil transendothelial migration by inhibition of the constitutive shedding of endothelial IL-8/heparan sulfate/syndecan-1 complexes. Marshall, L.J., Ramdin, L.S., Brooks, T., DPhil, P.C., Shute, J.K. J. Immunol. (2003) [Pubmed]
  24. Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling. Utani, A., Momota, Y., Endo, H., Kasuya, Y., Beck, K., Suzuki, N., Nomizu, M., Shinkai, H. J. Biol. Chem. (2003) [Pubmed]
  25. Laminin alpha3 LG4 module induces keratinocyte migration: involvement of matrix metalloproteinase-9. Momota, Y., Suzuki, N., Kasuya, Y., Kobayashi, T., Mizoguchi, M., Yokoyama, F., Nomizu, M., Shinkai, H., Iwasaki, T., Utani, A. J. Recept. Signal Transduct. Res. (2005) [Pubmed]
  26. Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin. Grootjans, J.J., Reekmans, G., Ceulemans, H., David, G. J. Biol. Chem. (2000) [Pubmed]
  27. Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells. Ding, K., Lopez-Burks, M., Sánchez-Duran, J.A., Korc, M., Lander, A.D. J. Cell Biol. (2005) [Pubmed]
  28. Expression of proteoglycan core proteins in human bone marrow stroma. Schofield, K.P., Gallagher, J.T., David, G. Biochem. J. (1999) [Pubmed]
  29. Syndecan-1 and syndecan-4 are overexpressed in an estrogen receptor-negative, highly proliferative breast carcinoma subtype. Baba, F., Swartz, K., van Buren, R., Eickhoff, J., Zhang, Y., Wolberg, W., Friedl, A. Breast Cancer Res. Treat. (2006) [Pubmed]
  30. Soluble syndecan-1 and serum basic fibroblast growth factor are new prognostic factors in lung cancer. Joensuu, H., Anttonen, A., Eriksson, M., Mäkitaro, R., Alfthan, H., Kinnula, V., Leppä, S. Cancer Res. (2002) [Pubmed]
  31. Cell-surface proteoglycan expression by lymphocytes from peripheral blood and gingiva in health and periodontal disease. Manakil, J.F., Sugerman, P.B., Li, H., Seymour, G.J., Bartold, P.M. J. Dent. Res. (2001) [Pubmed]
  32. The mapping and visual ordering of the human syndecan-1 and N-myc genes near the telomeric region of chromosome 2p. Kaukonen, J., Alanen-Kurki, L., Jalkanen, M., Palotie, A. Hum. Genet. (1997) [Pubmed]
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