Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta.
Five different collagen chains and one smaller collagenous fragment have been isolated from the collagens found in the combined cell layer and medium of rhesus monkey aortic smooth muscle cell cultures. The collagen chains which can be identified are alpha1 (III), alpha1(I), alpha2, A and B. The smaller collagenous peptide exhibits an apparent molecular weight of 45 000 and has been designated CP45 (Mayne, R., et al. (1977), Arch. Biochem. Biophys. 181, 462). Smooth muscle cells continue to synthesize the collagens from which these components are derived for at least eight passages in culture. At each passage the alpha1 (III) chain consistently represents about one-half of the total collagen which is recovered after initial fractionation by agarose gel chromatography. The results show that smooth muscle cells derived from rhesus monkey thoracic aorta are phenotypically stable for many generations in vitro.
D000818:Animals; D001013:Aorta, Thoracic / Q000378:metabolism*; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis / Q000302:isolation & purification; D005347:Fibroblasts / Q000032:analysis; D000882:Haplorhini; D006801:Humans; D008253:Macaca mulatta; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D012867:Skin / Q000032:analysis
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen