Characterization of a cartilage-derived 66-kDa protein (RGD-CAP/beta ig-h3) that binds to collagen.
作者： Kazuto Hashimoto , Mitsuhide Noshiro , Shigeru Ohno , Takeshi Kawamoto , Hisashi Satakeda
DOI: 10.1016/S0167-4889(96)00147-4
关键词:
摘要: Abstract A 66-kDa collagen fiber-associated protein (RGD-CAP) was isolated from a fiber-rich fraction of pig cartilage by ultrafiltration and collagen-affinity chromatography. Amino acid sequencing cDNA cloning indicated that the RGD-CAP is identical or closely related to βig-h3 which induced in human adenocarcinoma cells transforming growth factor-β (TGF-β) (Skonier, J., Neubauer, M., Madisen, L., Bennett, K., Plowman, G.D., Purchio, A.F. (1992) DNA Cell. Biol. 11, 511–522). The RGD-CAP, as well βig-h3, has RGD sequence C-terminal region. native bound type I, II, IV collagens even presence 1 M NaCl. recombinant preparation expressed Escherichia coli also but not gelatin. mRNA chondrocytes throughout all stages, although expression level highest during prehypertrophic stage. In addition, TGF-β increased chondrocyte cultures. Since transcripts were found most tissues, this novel collagen-binding may play an important role cell-collagen interactions various tissues including developing cartilage.
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