본문 바로가기
KERD
논문KCI 등재

Shedding; towards a new paradigm of syndecan function in cancer

2

조회

0

다운로드

0

인용

0

참고문헌

키워드

주제분류화학

초록

Syndecans, cell surface heparansulfate proteoglycans, have been proposed to act as cell surface receptors and/or coreceptors to play critical roles in multiple cellular functions. However,recent reports suggest that the function of syndecans can be further extended through shedding, a cleavage of extracellular domain. Shedding constitutes an additional level for controlling the function of syndecans, providing a means to attenuate and/or regulate amplitude and duration of syndecan signals by modulating the activity of syndecans as cell surface receptors. Whether these remaining cleavage products are still capable of functioning as cell surface receptors to efficiently transduce signals inside of cells is not clear. However, shedding transforms cell surface receptor syndecans into soluble forms,which, like growth factors, may act as novel ligands to induce cellular responses by association with other cell surface receptors. It is becoming interestingly evident that shed syndecans also contribute significantly to syndecan functions in cancer biology. This review presents current knowledge about syndecan shedding and its functional significance, particularly in the context of cancer.

Abstract

Syndecans, cell surface heparansulfate proteoglycans, have been proposed to act as cell surface receptors and/or coreceptors to play critical roles in multiple cellular functions. However,recent reports suggest that the function of syndecans can be further extended through shedding, a cleavage of extracellular domain. Shedding constitutes an additional level for controlling the function of syndecans, providing a means to attenuate and/or regulate amplitude and duration of syndecan signals by modulating the activity of syndecans as cell surface receptors. Whether these remaining cleavage products are still capable of functioning as cell surface receptors to efficiently transduce signals inside of cells is not clear. However, shedding transforms cell surface receptor syndecans into soluble forms,which, like growth factors, may act as novel ligands to induce cellular responses by association with other cell surface receptors. It is becoming interestingly evident that shed syndecans also contribute significantly to syndecan functions in cancer biology. This review presents current knowledge about syndecan shedding and its functional significance, particularly in the context of cancer.

참고문헌 (54)

  1. Gee, J. M., "ADAM metalloproteases and EGFR signalling", Breast Cancer Res., 5, pp.223~224 (2003)
  2. Lee, D. C., "TACE", ADAM17 processing of EGFR ligands indicates a role as a physiological convertase, 2003, pp.995, 22~38
  3. Kveiborg, M., "Cellular roles of ADAM12 in health and disease", Int. J. Biochem. Cell Biol., 40, pp.1685~1702 (2008)
  4. Hakozaki, A., "Receptor Activator of NF-{kappa}B (RANK) Ligand Induces Ectodomain Shedding of RANK in Murine RAW264.7 Macrophages", J. Immunol., 184, pp.2442~2448 (2010)
  5. Fan, H., "Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades", EMBO J., 18, pp.6962~6972 (1999)
  6. Najy, A. J., "The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation", J. Biol. Chem., 283, pp.18393~18401 (2008)
  7. Raucci, A., "A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10)", FASEB J., 22, pp.3716~3727 (2008)
  8. Zhang, L., "Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases", J. Biol. Chem., 283, pp.35507~35516 (2008)
  9. Zhang, L., "Ectodomain shedding of the receptor for advanced glycation end products: a novel therapeutic target for Alzheimer's disease", Cell Mol. Life Sci., 66, pp.3923~3935 (2009)
  10. Kojro, E., "Regulated proteolysis of RAGE and AbetaPP as possible link between type 2 diabetes mellitus and Alzheimer's disease", J. Alzheimers Dis., 16, pp.865~878 (2009)
  11. Chandler, A. B., "Regulation of CD40L (CD154) and CD62P (p-selectin) Surface Expression upon GPIIb-IIIa Blockade of Platelets from Stable Coronary Artery Disease Patients", Thromb. Res., 125, pp.44~52 (2010)
  12. Mannello, F., "Increased shedding of soluble fragments of P-cadherin in nipple aspirate fluids from women with breast cancer", Cancer Sci., 99, pp.2160~2169 (2008)
  13. Finger, E. C., "TbetaRIII suppresses non-small cell lung cancer invasiveness and tumorigenicity", Carcinogenesis, 29, pp.528~535 (2008)
  14. Gordon, K. J., "Loss of type III transforming growth factor beta receptor expression increases motility and invasiveness associated with epithelial to mesenchymal transition during pancreatic cancer progression", Carcinogenesis, 29, pp.252~262 (2008)
  15. Koenecke, C., "Shedding of the endothelial receptor tyrosine kinase Tie2 correlates with leukemic blast burden and outcome after allogeneic hematopoietic stem cell transplantation for AML", Ann. Hematol., 89, pp.459~467 (2010)
  16. Bien, E., "Serum soluble interleukin 2 receptor alpha in human cancer of adults and children: a review", Biomarkers, 13, pp.1~26 (2008)
  17. Fears, C. Y., "Syndecan-2 is expressed in the microvasculature of gliomas and regulates angiogenic processes in microvascular endothelial cells", J. Biol. Chem., 281, pp.14533~14536 (2006)
  18. Lambaerts, K., "The signaling mechanisms of syndecan heparan sulfate proteoglycans", Curr. Opin. Cell Biol., 21, pp.662~669 (2009)
  19. Morgan, M. R., "Synergistic control of cell adhesion by integrins and syndecans", Nat. Rev. Mol. Cell Biol., 8, pp.957~969 (2007)
  20. Khotskaya, Y. B., "Syndecan- 1 Is Required for Robust Growth, Vascularization, and Metastasis of Myeloma Tumors in vivo", J. Biol. Chem., 284, pp.26085~26095 (2009)
  21. Maeda, T., "Syndecan-1 expression by stromal fibroblasts promotes breast carcinoma growth in vivo and stimulates tumor angiogenesis", Oncogene, 25, pp.1408~1412 (2006)
  22. Shimada, K., "Role of syndecan-1 (CD138) in cell survival of human urothelial carcinoma", Cancer Sci., 101, pp.155~160 (2010)
  23. Davies, E. J., "Distribution and clinical significance of heparan sulfate proteoglycans in ovarian cancer", Clin. Cancer Res., 10, pp.5178~5186 (2004)
  24. Chen, D., "Syndecan-1 expression in locally invasive and metastatic prostate cancer", Urology, 63, pp.402~407 (2004)
  25. Levy, P., "Syndecan-1 alterations during the tumorigenic progression of human colonic Caco-2 cells induced by human Ha-ras or polyoma middle T oncogenes", Br. J. Cancer, 74, pp.423~431 (1996)
  26. Oh, J. H., "Syndecan-1 enhances the endometrial cancer invasion by modulating matrix metalloproteinase-9 expression through nuclear factor kappaB", Gynecol. Oncol., 114, pp.509~515 (2009)
  27. Conejo, J. R., "Syndecan-1 expression is up-regulated in pancreatic but not in other gastrointestinal cancers", Int. J. Cancer, 88, pp.12~20 (2000)
  28. Park, H., "Syndecan-2 mediates adhesion and proliferation of colon carcinoma cells", J. Biol. Chem., 277, pp.29730~29736 (2002)
  29. Popović, A., "Expression and prognostic role of syndecan-2 in prostate cancer", Prostate Cancer Prostatic. Dis., 13, pp.78~82 (2010)
  30. Woods, A., "Syndecan-4 and focal adhesion function", Curr. Opin. Cell Biol., 13, pp.578~583 (2001)
  31. Brule, S., "The shedding of syndecan-4 and syndecan-1 from HeLa cells and human primary macrophages is accelerated by SDF-1", CXCL12 and mediated by the matrix metalloproteinase-9, 2006, pp.16, 488~501
  32. Chen, P., "MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting alpha(2)beta(1) integrin activation", PLoS One, 4, pp.e6565~ (2009)
  33. Endo, K., "Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration", J. Biol. Chem., 278, pp.40764~40770 (2003)
  34. Asundi, V. K., "Matrix metalloproteinase-dependent shedding of syndecan-3, a transmembrane heparan sulfate proteoglycan, in Schwann cells", J. Neurosci. Res., 73, pp.593~602 (2003)
  35. Rodríguez-Manzaneque, J. C., "Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion", Int. J. Biochem. Cell. Biol., 41, pp.800~810 (2009)
  36. Fitzgerald, M. L., "Shedding of Syndecan-1 and -4 Ectodomains Is Regulated by Multiple Signaling Pathways and Mediated by a Timp-3-Sensitive Metalloproteinase", J. Cell Biol., 148, pp.811~824 (2000)
  37. Pruessmeyer, J., "A disintegrin and metalloproteinase 17 (ADAM17) mediates inflammation- induced shedding of syndecan-1 and -4 by lung epithelial cells", J. Biol. Chem., 285, pp.555~564 (2010)
  38. Spencer, J., "Crystal Structure of the LasA Virulence Factor from Pseudomonas aeruginosa: Substrate Specificity and Mechanism of M23 Metallopeptidases", J. Mol. Biol., 396, pp.908~923 (2010)
  39. Park, P. W., "Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa", J. Biol. Chem., 275, pp.3057~3064 (2000)
  40. Subramanian, S. V., "Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation", J. Biol. Chem., 272, pp.14713~14720 (1997)
  41. Ding, K., "Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells", J. Cell Biol., 171, pp.729~738 (2005)
  42. Wang, F., "Matrilysin over-expression in MCF-7 cells enhances cellular invasiveness and pro-gelatinase activation", Cancer Lett., 236, pp.292~301 (2006)
  43. Wang, J. B., "Insulin increases shedding of syndecan-1 in the serum of patients with type 2 diabetes mellitus", Diabetes Res. Clin. Pract., 86, pp.83~88 (2009)
  44. Reizes, O., "Insulin promotes shedding of syndecan ectodomains from 3T3-L1 adipocytes: a proposed mechanism for stabilization of extracellular lipoprotein lipase", Biochemistry, 45, pp.5703~5711 (2006)
  45. Kliment, C. R., "Oxidative stress alters syndecan-1 distribution in lungs with pulmonary fibrosis", J. Biol. Chem., 284, pp.3537~3545 (2009)
  46. Holen, I., "Evidence of a role for a non-matrix-type metalloproteinase activity in the shedding of syndecan-1 from human myeloma cells", Br. J. Haematol., 114, pp.414~421 (2001)
  47. Maxhimer, J. B., "Heparanase-1 expression is associated with the metastatic potential of breast cancer", Surgery, 132, pp.326~333 (2002)
  48. Purushothaman, A., "Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis", Blood, 115, pp.2449~2457 (2010)
  49. Su, G., "Membrane type 1 matrix metalloproteinase-mediated stromal syndecan-1 shedding stimulates breast carcinoma cell proliferation", Cancer Res., 68, pp.9558~9565 (2008)
  50. Nikolova, V., "Differential roles for membrane-bound and soluble syndecan-1 (CD138) in breast cancer progression", Carcinogenesis, 30, pp.397~407 (2009)
  51. Yang, Y., "Heparanase enhances syndecan-1 shedding: a novel mechanism for stimulation of tumor growth and metastasis", J. Biol. Chem., 282, pp.13326~13333 (2007)
  52. Beauvais, D. M., "Syndecan-1 regulates alphavbeta3 and alphavbeta5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor", J. Exp. Med., 206, pp.691~705 (2009)
  53. Sanderson, R. D., "Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: growth regulation and the prospect of new cancer therapies", J. Cell Biochem., 96, pp.897~905 (2005)
  54. Hayashida, K., "Syndecan-1 shedding facilitates the resolution of neutrophilic inflammation by removing sequestered CXC chemokines", Blood, 114, pp.3033~3043 (2009)

관련 논문AI추천

이 간행물의 다른 논문 (11건)