Abstract
In a study of human atherosclerotic plaques, the relative abundance of alpha chains in pepsin-solubilized collagens from 28 human aortas was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The ratio of alpha B, a component of the alpha chain in type V collagen, to alpha 1(I) was markedly increased in the atherosclerotic plaques compared to the nonsclerotic intact media and adventitia. It is suggested that proliferating smooth muscle cells in the sclerotic lesion were transformed to synthesize a larger amount of collagen alpha B chain during the process of human atherogenesis.