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Showing papers on "Fatty acid-binding protein published in 1984"


Journal ArticleDOI
TL;DR: It is concluded that permeation of the plasma membrane of the adipocyte by long-chain FAs at physiological concentrations is mediated by a protein transporter with distinct specificity requirements.

274 citations


Journal ArticleDOI
TL;DR: Cholestyramine feeding increased the FABP content of liver cytosol from rats sacrificed at the mid-light phase, but not in those sacrificed atThe mid-dark phase, in such a way that the diurnal variation of the F ABP content virtually disappeared.

120 citations


Journal ArticleDOI
TL;DR: It appears that fatty acids and their CoA esters are the foremost binding partners of FABPs in vivo.
Abstract: Fatty-acid-binding proteins (FABPs) are known as cytosolic binding sites for fatty acids and their CoA esters. Radioactively labeled and fluorescent fatty acids were used to locate and identify these proteins in bovine liver cytosol. The occurrence of two species of FABPs was demonstrated and these were designated pI6.0-FABP and pI7.0-FABP according to their isoelectric points in the delipidated state. Oleic acid/FABP binding ratios were 1 with pI6.0-FABP and 2 with pI7.0-FABP. Upon binding of oleic acid the isoelectric points of liganded FABPs shifted to pH 5.0-5.1 in each case. Both proteins were purified by removing nonbinding proteins by acid and heat denaturation and subsequent gel filtration. By making use of the pI shifts observed upon lipidation and delipidation of the binding proteins with ligand fatty acids, final purification was achieved in two fractionations by isoelectric focusing. The binding proteins (Mr 11 800 +/- 1 000) had similar amino-acid compositions (no Trp) and were not covalently modified by carbohydrate and fatty acid. Fatty acids and their CoA esters were complexed by either FABP, cholesterol only by pI-7.0-FABP, though non-stoichiometrically. 16-(9-Anthroyloxy)palmitic acid was bound by pI-7.0-FABP in a 1:1 ratio and precluded the additional binding of a straight-chain fatty acid. Electrophoretic titration curves indicated dissociation of the oleic acid/pI7.0-FABP complex below pH 5.0. It appears that fatty acids and their CoA esters are the foremost binding partners of FABPs in vivo. The results are discussed in terms of a single binding site for fatty acids per molecule FABP.

118 citations


Journal ArticleDOI
TL;DR: A simple experimental system was developed for studying the movement of long-chain fatty acids between multilamellar liposomes and soluble proteins capable of binding fatty acids, and it was found that the fatty acid transferred from the liposome to either protein rapidly and selectively under conditions where phospholipid and cholesterol transfer did not occur.

84 citations


Journal ArticleDOI
TL;DR: Observations lead to the conclusion that the low molecular weight fatty acid binding proteins from rat liver and heart are different proteins.

70 citations


Journal ArticleDOI
TL;DR: The hypothesis that Mr 12 000 soluble FABPs intrinsic to brain may act as regulators of synaptosomal Na+-dependent amino acid uptake by sequestering free fatty acids which inhibit this process is consistent with the hypothesis that it might be served by fatty acid binding proteins intrinsic tobrain.
Abstract: High-affinity, Na+-dependent synaptosomal amino acid uptake systems are strongly stimulated by proteins which are known to bind fatty acids, including the Mr 12 000 fatty acid binding protein (FABP) from liver. To explore the possibility that such a function might be served by fatty acid binding proteins intrinsic to brain, we examined the 105000g supernatant of brain for fatty acid binding. Observed binding was accounted for mainly by components excluded by Sephadex G-50, and to a small degree by the Mr 12 000 protein fraction (brain FABP fraction). The partially purified brain FABP fraction contained a protein immunologically identical with liver FABP as well as a FABP electrophoretically distinct from liver FABP. Brain FABP fraction markedly stimulated synaptosomal Na+-dependent, but not Na+-independent, amino acid uptake, and also completely reversed the inhibition of synaptosomal Na+-dependent amino acid uptake induced by oleic acid. Palmitic, stearic, and oleic acids were endogenously associated with the brain FABP fraction. These data are consistent with the hypothesis that Mr 12 000 soluble FABPs intrinsic to brain may act as regulators of synaptosomal Na+-dependent amino acid uptake by sequestering free fatty acids which inhibit this process.

63 citations


Journal ArticleDOI
TL;DR: Amo acid sequence rearrangements in the COOH-terminal region of rat liver FABP had a significant effect on its ability to bind fatty acids as well as on its stability in bacteria.

45 citations


Journal ArticleDOI
TL;DR: The results revealed characteristic differences between cardiac and hepatic FABPs with regard to binding a fatty acid.

43 citations


Journal ArticleDOI
TL;DR: A fatty acid binding protein has been purified from etiolated Avena sativa seedlings and is capable of binding long-chain fatty acids and their CoA-esters.

36 citations


Journal ArticleDOI
01 Jul 1984-Lipids
TL;DR: Electrophoretic studies revealed that FABP from hepatic cytosol of rat, mouse and guinea pig, purified with affinity chromatography, are distinct from one another in terms of their charge.
Abstract: Binding properties of liver cytosolic protein for oleic acid, palmitoyl-CoA and bromosulphophthalein (BSP) were compared for rat, mouse and guinea pig. Hepatic cytosol of rat, mouse and guinea pig contained proteins with a molecular weight of ca. 12,000 and had an affinity for [1-14C]-oleic acid. The concentration of fatty acid-binding protein (FABP) was almost the same in livers of the animals of the 3 species and was ca. 50 μg/mg cytosolic protein. Electrophoretic studies revealed that FABP from hepatic cytosol of rat, mouse and guinea pig, purified with affinity chromatography, are distinct from one another in terms of their charge. FABP of rat liver was capable of binding any 3 ligands-oleic acid, palmitoyl-CoA and BSP—at relatively high binding capacity. FABP of mouse liver also bound oleic acid and palmitoyl-CoA to a great extent, but its binding capacity for BSP was only one-third that of rat liver. FABP of guinea pig liver bound less oleic acid and palmitoyl-CoA than rat liver, whereas it had almost the same binding capacity for BSP as rat liver.

23 citations