Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta

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Abstract
Five different collagen chains and one smaller collagenous fragment were isolated from the collagens found in the combined cell layer and medium of rhesus monkey [Macaca mulatta] aortic smooth muscle cell cultures. The collagen chains which can be identified are .alpha.1(III), .alpha.1(I), .alpha.2, A and B. The smaller collagenous peptide exhibits an apparent MW of 45,000 and had been designated CP45. Smooth muscle cells continue to synthesize the collagens from which these components are derived for at least 8 passages in culture. At each passage the .alpha.1(III) chain consistently represents about 1/2 of the total collagen which is recovered after initial fractionation by agarose gel chromatography. Smooth muscle cells derived from rhesus monkey thoracic aorta are phenotypically stable for many generations in vitro.