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Structural Features of Cartilage Matrix Protein Deduced from CDNA

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Specialty Science
Date 1987 Jan 1
PMID 3025875
Citations 16
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Abstract

cDNAs encoding the Mr 54,000 chicken cartilage matrix protein (CMP) were selected from a cartilage cDNA expression library by immunological means. Antibodies elicited against insert-encoded protein purified from one of the clones reacted specifically with chicken CMP in immunoblots of total cartilage extract, providing positive identification of the cDNA clones isolated. The cDNAs detect a 3.4-kilobase transcript that was present in sternal cartilage and in cartilaginous but not in precartilaginous embryonic limb tissues. The cDNAs code for 416 amino acids of the chicken CMP, including its COOH terminus. There are two striking features in the deduced CMP amino acid sequence: first, it contains a region with significant homologies to repeat sequences in the precursor for epidermal growth factor; and second, it is made up of two large homologous repeat sequences. These results provide the first detailed structural information on the CMP and establish it as a developmentally regulated marker of cartilage differentiation.

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References
1.
Miller E, Matukas V . Chick cartilage collagen: a new type of alpha 1 chain not present in bone or skin of the species. Proc Natl Acad Sci U S A. 1969; 64(4):1264-8. PMC: 223278. DOI: 10.1073/pnas.64.4.1264. View

2.
Chandrasekhar S, Laurie G, Cannon F, Martin G, Kleinman H . In vitro regulation of cartilage matrix assembly by a Mr 54,000 collagen-binding protein. Proc Natl Acad Sci U S A. 1986; 83(14):5126-30. PMC: 323903. DOI: 10.1073/pnas.83.14.5126. View

3.
Hughes R . Glycoproteins as components of cellular membranes. Prog Biophys Mol Biol. 1973; 26:189-268. DOI: 10.1016/0079-6107(73)90020-5. View

4.
GOETINCK P, Pennypacker J, Royal P . Proteochondroitin sulfate synthesis and chondrogenic expression. Exp Cell Res. 1974; 87(2):241-8. DOI: 10.1016/0014-4827(74)90476-5. View

5.
Oegema Jr T, Hascall V, DZIEWIATKOWSKI D . Isolation and characterization of proteoglycans from the swarm rat chondrosarcoma. J Biol Chem. 1975; 250(15):6151-9. View