Biosynthesis of type I and III collagens by cultured smooth muscle cells from human aorta.

Abstract

The synthesis of collagen by human aortic smooth muscle cells was studied after incubating the cells with [3H]proline and [3H]glycine for 48 h. The culture medium and cells were lyophilized and then digested with cyanogen bromide (CNBr) in 70% (wt/vol) formic acid. The resultant peptides were subjected to ion exchange chromatography on carboxymethyl-cellulose and gel filtration on agarose. On the basis of the molar ratios of the .alpha.1(I)-CB8 and .alpha.1(III)-CB8 peptides of the .alpha.1(I) and .alpha.1(III) chains, approximately 1/4 of the collagen synthesized by these cells was identified as type III and 3/4 as type I. The smooth muscle can synthesize at least 2 types of collagen found in the arterial wall.