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Research Article Free access | 10.1172/JCI113700
Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Department of Medicine, Mount Sinai School of Medicine, New York 10029.
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Published September 1, 1988 - More info
Uptake of [3H]oleate by canine or rat cardiac myocytes is saturable, displays the countertransport phenomenon, and is inhibited by phloretin and trypsin. Cardiac myocytes contain a basic (pI approximately 9.1) 40-kD plasma membrane fatty acid binding protein (FABPPM) analogous to those recently isolated from liver, adipose tissue, and gut, unrelated to the 12-14-kD cytosolic FABP in these same tissues. An antibody to rat liver FABPPM selectively inhibits specific uptake of [3H]oleate by rat heart myocytes at 37 degrees C, but has no influence on nonspecific [3H]oleate uptake at 4 degrees C or on specific uptake of [3H]glucose. Uptake of long-chain free fatty acids by cardiac muscle cells, liver, and adipose tissue and absorption by gut epithelial cells is a facilitated process mediated by identical or closely related plasma membrane FABPs.
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