Plasmin-treated low density lipoproteins: polypeptide analyses and metabolism by cultured smooth muscle cells.

Plasmin, generated by the interaction of urokinase with plasminogen, degraded the apoprotein B moiety of human low density lipoprotein to yield distinct high moleculr weight intermediates under conditions where only a small fraction (less than 3%) of the protein was hydrolyzed to trichloroacetic acid-soluble products. The molecular weights of these intermediates were between 60 000 and 200 000 as estimated by SDS-polyacrylamide electrophoresis. Trypsin treatment yielded fragments of similar size to those obtained with plasmin. When enzyme-treated low density lipoproteins were added to bovine aortic smooth muscle cells in culture, the receptor-binding, and rates of internalization and degradation were no different from those obtained in the case of native low density lipoproteins.