In vitro studies on origin and site of action of enzyme activity responsible for conversion of human proapoprotein A-I into apoprotein A-I

AbstractHuman hepatocellular carcinoma cells (Hep G2) were shown to secrete apo A-I as a proprotein. No apo A-I synthesis could be detected with endothelial cells from human umbilical cord veins. Conversion of proapo A-I into apo A-I is a slow (of the order of hours) process, mediated by a Ca2+/Mg2+-dependent enzyme which is present on the surface of plasma lipoprotein particles, endothelial cells and Hep G2 cells, and is probably synthesized by Hep G2 cells