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Effect of clofibric acid on the turnover of the fatty acid‐binding protein identified in cultured endothelial cells from bovine aorta
Author(s) -
Robers Markus,
Loddenkötter Brigitte,
Kresse Hans,
Spener Friedrich
Publication year - 1993
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536078
Subject(s) - clofibric acid , clinical chemistry , biochemistry , fatty acid , fatty acid binding protein , chemistry , clofibrate , methionine , aorta , bovine serum albumin , biology , amino acid , medicine , gene
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‐[ 35 S]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.