Effect of clofibric acid on the turnover of the fatty acid-binding protein identified in cultured endothelial cells from bovine aorta.

Several types of fatty acid-binding proteins are found in mammalian cells. Cultured endothelial cells from bovine aorta were shown to contain exclusively the cardiac-type fatty acid-binding protein (cFABP) with a mean concentration of 90 ng cFABP/mg extract protein. Only small variations were observed from passage to passage. In pulse-chase labeling experiments with L-[35S]methionine, a half-life of 4.0 d was measured for cFABP which is about two times longer than the average half-life of the extracted proteins. These data imply that in aortic endothelial cells cFABP is not subject to short-term regulation. However, addition of clofibric acid to the culture medium led to a shortening of the half-life of cFABP, which was compensated for by an increase in its biosynthesis. The turnover of the bulk of extract proteins remained unchanged when the cells were challenged with clofibric acid.