title: Characterization of a cartilage-derived 66-kDa protein (RGD-CAP/beta ig-h3) that binds to collagen.
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 and cDNA cloning indicated that the RGD-CAP is identical or closely related to beta ig-h3 protein which is induced in human adenocarcinoma cells by transforming growth factor-beta (TGF-beta) (Skonier, J., Neubauer, M., Madisen, L., Bennett, K., Plowman, G.D., and Purchio, A.F. (1992) DNA Cell. Biol. 11, 511-522). The RGD-CAP, as well as beta ig-h3, has the RGD sequence in the C-terminal region. The native RGD-CAP bound to type I, II, and IV collagens even in the presence of 1 M NaCl. A recombinant preparation of RGD-CAP expressed in Escherichia coli cells also bound to collagen but not to gelatin. The RGD-CAP mRNA was expressed in chondrocytes throughout all stages, although the expression level was highest during the prehypertrophic stage. In addition, TGF-beta increased the RGD-CAP mRNA level in chondrocyte cultures. Since RGD-CAP transcripts were found in most tissues, this novel collagen-binding protein may play an important role in cell-collagen interactions in various tissues including developing cartilage.
authors.affiliation: Department of Removal Prosthodontics, School of Dentistry, Hiroshima University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hashimoto
authors.forename: M
authors.initials: M
authors.lastname: Noshiro
authors.forename: S
authors.initials: S
authors.lastname: Ohno
authors.forename: T
authors.initials: T
authors.lastname: Kawamoto
authors.forename: H
authors.initials: H
authors.lastname: Satakeda
authors.forename: Y
authors.initials: Y
authors.lastname: Akagawa
authors.forename: K
authors.initials: K
authors.lastname: Nakashima
authors.forename: A
authors.initials: A
authors.lastname: Okimura
authors.forename: H
authors.initials: H
authors.lastname: Ishida
authors.forename: T
authors.initials: T
authors.lastname: Okamoto
authors.forename: H
authors.initials: H
authors.lastname: Pan
authors.forename: M
authors.initials: M
authors.lastname: Shen
authors.forename: W
authors.initials: W
authors.lastname: Yan
authors.forename: Y
authors.initials: Y
authors.lastname: Kato
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D015139:Blotting, Southern; D002356:Cartilage / Q000737:chemistry / Q000166:cytology / Q000378:metabolism*; D002454:Cell Differentiation / Q000502:physiology; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D003094:Collagen / Q000378:metabolism*; D018076:DNA, Complementary / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D016326:Extracellular Matrix Proteins; D018507:Gene Expression Regulation, Developmental; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D015183:Restriction Mapping; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013552:Swine; D016212:Transforming Growth Factor beta; D000099222:betaIG-H3 Protein
chemical_list: D003094:Collagen; D018076:DNA, Complementary; D016326:Extracellular Matrix Proteins; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; D016212:Transforming Growth Factor beta; D000099222:betaIG-H3 Protein