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Gene Review

VCAN  -  versican

Gallus gallus

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Disease relevance of VCAN

  • In contrast, total collagen synthesis showed a greater than 10-fold increase until day 18, a result suggesting that collagen synthesis was replacing proteoglycan synthesis during cellular hypertrophy [1].
  • Cellular transformation and differentiation. Effect of Rous sarcoma virus transformation on sulfated proteoglycan synthesis by chicken chondrocytes [2].
  • The 1/20/5-D-4 monoclonal antibody did not recognize antigenic determinants on proteoglycan isolated from Swarm rat chondrosarcoma [3].
  • A genomic DNA fragment (gCORE-1), encoding a portion of the cartilage proteoglycan core protein, has been isolated from a phage library using cDNA as a probe [4].
  • In combination with basal lamina proteins, collagen type IX proteoglycan slightly inhibited neurite outgrowth and led to a stronger fasciculation of retinal axons [5].

High impact information on VCAN

  • The synthetic program of these cells was also dramatically modified: the cultures no longer synthesized the chondroblast-unique type IV sulfated proteoglycan and began synthesizing alpha 2 collagen chains typical of fibroblastic or early limb bud cells [6].
  • Although this adhesion involves a homophilic binding mechanism, the binding of the cell surface proteoglycan heparan sulphate to the glycoprotein is also required [7].
  • I report here the presence, in some human cartilages, of a proteoglycan population that initially will not aggregate with the hyaluronic acid but subsequently can be chased into aggregate [8].
  • Delayed formation of proteoglycan aggregate structures in human articular cartilage disease states [8].
  • However, Heinegärd and Hascall have characterized the small proportion of nonaggregating proteoglycan present in bovine nasal septum cartilage and found that it contained more peptide than the aggregating proteoglycan [8].

Chemical compound and disease context of VCAN


Biological context of VCAN

  • A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo [11].
  • When the immobilization of added PG-M to available plastic surfaces of coated dishes was blocked by pretreating the dishes with serum albumin, the inhibitory effect of PG-M was abolished, suggesting that the immobilized fraction of PG-M can act as a cell adhesion inhibitor [12].
  • In contrast, heparan sulfate proteoglycan form LD and heparan sulfate-derivatized serum albumin had far lower inhibitory activities, indicating that the active site for the interaction between cells and PG-M is on the chondroitin sulfate chains [12].
  • It is likely, therefore, that multiforms of the PG-M core protein may be generated by alternative usage of either or both of the two different chondroitin sulfate attachment domains (alpha and beta) and that molecular forms of PG-M may vary from tissue to tissue by such an alternative splicing [13].
  • Immunofluorescent staining with these antibodies allowed us to demonstrate that distribution of HSPG at the epithelial-mesenchymal interface varied with the stages of intestinal development, suggesting that remodeling of this proteoglycan is essential for regulating cell behavior during morphogenesis [14].

Anatomical context of VCAN

  • We have isolated cDNA clones encoding the core protein of PG-M, a large chondroitin sulfate proteoglycan that has been shown to be expressed in the prechondrogenic condensation area of the developing chick limb buds (Shinomura T., Jensen, K. L., Yamagata, M., Kimata, K., and Solursh, M. (1990) Anat. Embryol. 181, 227-233) [15].
  • These domains show an extremely high homology to corresponding domains of a human fibroblast large chondroitin sulfate proteoglycan, versican [15].
  • Immunofluorescent localization of PG-M showed that the intensity of PG-M staining progressively became higher in the core mesenchyme region than in the peripheral loose mesenchyme, closely following the condensation of mesenchymal cells [11].
  • PG-M was found in some developmentally active areas, such as the perinotochordal mesenchyme between notochord and neural tube, the basement membranes facing neuroepithelial cells, and condensing mesenchymal cells in limb buds, suggesting some functions distinctive of the developing tissues [16].
  • Molecules reactive to a monoclonal antibody to the PG-M core protein (designated MY-174) were distributed in various tissues, including aorta, lung, cornea, brain, skeletal muscle and dermis [16].

Associations of VCAN with chemical compounds


Physical interactions of VCAN


Regulatory relationships of VCAN

  • Pretreatment of collagen gels with the proteoglycan monomer from bovine nasal cartilage had no effect of the adhesion of crest cells, but the proteoglycan almost completely inhibited adhesion to adsorbed fibronectin, but only when absorbed collagen was also present [22].
  • CT also stimulated the proteoglycan synthesis only in the diaphysis but the stimulation was less potent (133% of control) than PTH (650% of control) or dibutyryl cyclic AMP (625% of control) [23].
  • Monensin, which is known to cause dilatation of the Golgi apparatus and to inhibit sulfation of proteoglycan, was found to affect the release of the sulfotransferases [24].

Other interactions of VCAN


Analytical, diagnostic and therapeutic context of VCAN


  1. Gene expression and extracellular matrix ultrastructure of a mineralizing chondrocyte cell culture system. Gerstenfeld, L.C., Landis, W.J. J. Cell Biol. (1991) [Pubmed]
  2. Cellular transformation and differentiation. Effect of Rous sarcoma virus transformation on sulfated proteoglycan synthesis by chicken chondrocytes. Muto, M., Yoshimura, M., Okayama, M., Kaji, A. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  3. Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan. Caterson, B., Christner, J.E., Baker, J.R. J. Biol. Chem. (1983) [Pubmed]
  4. Partial structure of the gene for chicken cartilage proteoglycan core protein. Tanaka, T., Har-el, R., Tanzer, M.L. J. Biol. Chem. (1988) [Pubmed]
  5. Two chondroitin sulfate proteoglycans differentially expressed in the developing chick visual system. Ring, C., Lemmon, V., Halfter, W. Dev. Biol. (1995) [Pubmed]
  6. Fibronectin alters the phenotypic properties of cultured chick embryo chondroblasts. West, C.M., Lanza, R., Rosenbloom, J., Lowe, M., Holtzer, H., Avdalovic, N. Cell (1979) [Pubmed]
  7. Neuronal cell-cell adhesion depends on interactions of N-CAM with heparin-like molecules. Cole, G.J., Loewy, A., Glaser, L. Nature (1986) [Pubmed]
  8. Delayed formation of proteoglycan aggregate structures in human articular cartilage disease states. Oegema, T.R. Nature (1980) [Pubmed]
  9. Partial cDNA sequence encoding a globular domain at the C terminus of the rat cartilage proteoglycan. Doege, K., Fernandez, P., Hassell, J.R., Sasaki, M., Yamada, Y. J. Biol. Chem. (1986) [Pubmed]
  10. Monoclonal antibodies to different protein-related epitopes of human articular cartilage proteoglycans. Glant, T.T., Mikecz, K., Poole, A.R. Biochem. J. (1986) [Pubmed]
  11. A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo. Kimata, K., Oike, Y., Tani, K., Shinomura, T., Yamagata, M., Uritani, M., Suzuki, S. J. Biol. Chem. (1986) [Pubmed]
  12. Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates. Yamagata, M., Suzuki, S., Akiyama, S.K., Yamada, K.M., Kimata, K. J. Biol. Chem. (1989) [Pubmed]
  13. Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing. Ito, K., Shinomura, T., Zako, M., Ujita, M., Kimata, K. J. Biol. Chem. (1995) [Pubmed]
  14. Origin and deposition of basement membrane heparan sulfate proteoglycan in the developing intestine. Simon-Assmann, P., Bouziges, F., Vigny, M., Kedinger, M. J. Cell Biol. (1989) [Pubmed]
  15. cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed during chondrogenesis in chick limb buds. Alternative spliced multiforms of PG-M and their relationships to versican. Shinomura, T., Nishida, Y., Ito, K., Kimata, K. J. Biol. Chem. (1993) [Pubmed]
  16. Tissue variation of two large chondroitin sulfate proteoglycans (PG-M/versican and PG-H/aggrecan) in chick embryos. Yamagata, M., Shinomura, T., Kimata, K. Anat. Embryol. (1993) [Pubmed]
  17. Tandem repeats are involved in G1 domain inhibition of versican expression and secretion and the G3 domain enhances glycosaminoglycan modification and product secretion via the complement-binding protein-like motif. Yang, B.L., Cao, L., Kiani, C., Lee, V., Zhang, Y., Adams, M.E., Yang, B.B. J. Biol. Chem. (2000) [Pubmed]
  18. Hyaluronic acid-dependent change in the extracellular matrix of mouse dermal fibroblasts that is conducive to cell proliferation. Yoneda, M., Shimizu, S., Nishi, Y., Yamagata, M., Suzuki, S., Kimata, K. J. Cell. Sci. (1988) [Pubmed]
  19. Vitronectin and thrombospondin promote retinal neurite outgrowth: developmental regulation and role of integrins. Neugebauer, K.M., Emmett, C.J., Venstrom, K.A., Reichardt, L.F. Neuron (1991) [Pubmed]
  20. Chondroitin sulfate proteoglycan (PG-M-like proteoglycan) is involved in the binding of hyaluronic acid to cellular fibronectin. Yamagata, M., Yamada, K.M., Yoneda, M., Suzuki, S., Kimata, K. J. Biol. Chem. (1986) [Pubmed]
  21. Distribution and expression of two interactive extracellular matrix proteins, cytotactin and cytotactin-binding proteoglycan, during development of Xenopus laevis. I. Embryonic development. Williamson, D.A., Parrish, E.P., Edelman, G.M. J. Morphol. (1991) [Pubmed]
  22. Adhesion to extracellular materials by neural crest cells at the stage of initial migration. Newgreen, D.F. Cell Tissue Res. (1982) [Pubmed]
  23. Selective activation of diaphyseal chondrocytes by parathyroid hormone, calcitonin and N6,O2-dibutyryl adenosine 3',5'-cyclic monophosphoric acid in proteoglycan synthesis of chick embryonic femur cultivated in vitro. Kawashima, K., Iwata, S., Endo, H. Endocrinol. Jpn. (1980) [Pubmed]
  24. Secretion of chondroitin 6-sulfotransferase and chondroitin 4-sulfotransferase from cultured chick embryo chondrocytes. Habuchi, O., Tsuzuki, M., Takeuchi, I., Hara, M., Matsui, Y., Ashikari, S. Biochim. Biophys. Acta (1991) [Pubmed]
  25. Proteoglycan-Lb, a small dermatan sulfate proteoglycan expressed in embryonic chick epiphyseal cartilage, is structurally related to osteoinductive factor. Shinomura, T., Kimata, K. J. Biol. Chem. (1992) [Pubmed]
  26. Molecular cloning and ultrastructural localization of the core protein of an eggshell matrix proteoglycan, ovocleidin-116. Hincke, M.T., Gautron, J., Tsang, C.P., McKee, M.D., Nys, Y. J. Biol. Chem. (1999) [Pubmed]
  27. cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals homology to the small interstitial proteoglycan gene family and expression in muscle and intestine. Blochberger, T.C., Vergnes, J.P., Hempel, J., Hassell, J.R. J. Biol. Chem. (1992) [Pubmed]
  28. cDNA clone to chick corneal chondroitin/dermatan sulfate proteoglycan reveals identity to decorin. Li, W., Vergnes, J.P., Cornuet, P.K., Hassell, J.R. Arch. Biochem. Biophys. (1992) [Pubmed]
  29. Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules. Hoffman, S., Crossin, K.L., Edelman, G.M. J. Cell Biol. (1988) [Pubmed]
  30. Electron microscopic characterization of chick embryonic skeletal muscle proteoglycans. Pechak, D.G., Carrino, D.A., Caplan, A.I. J. Cell Biol. (1985) [Pubmed]
  31. Immunological characterization of the major chick cartilage proteoglycan and its intracellular localization in cultured chondroblasts: a comparison with Type II procollagen. Pacifici, M., Soltesz, R., Thal, G., Shanley, D.J., Boettiger, D., Holtzer, H. J. Cell Biol. (1983) [Pubmed]
  32. Cloning and sequence analysis of a partial cDNA for chicken cartilage proteoglycan core protein. Sai, S., Tanaka, T., Kosher, R.A., Tanzer, M.L. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  33. A heparan sulfate proteoglycan in developing avian axonal tracts. Halfter, W. J. Neurosci. (1993) [Pubmed]
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