Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

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Abstract
Hyaline cartilage contains a unique set of collagenous proteins. Type II collagen is the most abundant, constituting about 85% of the total cartilage collagen. Several minor collagenous components were described. To study the structure and developmental regulation of chondrocyte-specific collagens, a c[complementary]DNA library was constructed from embryonic chicken sternal cartilage mRNA. The isolation and characterization of a 3200 base-pair-long cDNA that codes for a collagenous polypeptide of unusual structure in that the total length of the molecule is only about half of pro.alpha.1(II) collagen chains is reported. The mRNA for this polypeptide is considerably smaller than mRNA encoding the pro.alpha. chains of interstitial collagens. The peptide encoded by the cDNA appears to contain at least 3 domains with triple-helical potential separated by short, noncollagenous peptides. Between the 3 collagenous domains are several cysteinyl residues.