Showing papers on "Fatty acid-binding protein published in 1989"
TL;DR: The refined molecular model of holo-I-FABP suggests several potential locations for entry and exiting of the fatty acid, including the "cradle" formed by the side-chains of hydrophobic, mainly aromatic, amino acid residues.
323 citations
146 citations
TL;DR: Characteristic saturation curves for the cell metabolic responses to ASP were observed in both cell types with higher stimulation of oleate incorporation into triacylglycerol being observed in adipocytes, and the stimulation ofTriacyl glycerol synthesis was much greater with ASP than with insulin.
128 citations
TL;DR: Application of the postembedding protein A-gold labeling method with antibody against the hepatic type fatty-acid-binding protein (hFABP) to cross-sections of liver cells and a newly developed gel-chromatographic immunofluorescence assay established qualitatively that hF ABP in mitochondria was confined to outer mitochondrial membranes.
Abstract: Fatty-acid-binding proteins are known to occur in the cytosol of mammalian cells and to bind fatty acids and their CoA-esters. Application of the postembedding protein A-gold labeling method with antibody against the hepatic type fatty-acid-binding protein (hFABP) to cross-sections of liver cells and a newly developed gel-chromatographic immunofluorescence assay established qualitatively (1) that hFABP in mitochondria was confined to outer mitochondrial membranes, (2) the presence of this protein in microsomes and (3) that nuclei were also filled with hFABP. Quantitative data elaborated with a non-competitive ELISA confirmed these results. A significant difference to the distribution of cardiac FABP in heart muscle cells, where this type of protein was found in cytosol, matrix and nuclei, was observed (Borchers et al. (1989) Biochim. Biophys. Acta, in the press). hFABP-containing rat liver microsomes were incubated with long-chain acyl-CoAs in the presence of hFABP (isolated from rat liver cytosol) in a study on the acylation of sn-glycerol-3-phosphate and lysophosphatidic acid. Both acyltransferases were stimulated by addition of hFABP to the incubation medium. The morphological, immunochemical as well as kinetic data infer a direct interaction of hFABP with microsomal membranes in liver cells.
117 citations
TL;DR: In this paper, a group of similar low molecular weight proteins, including plasma membrane transport protein, fatty acid binding proteins, sterol carrier protein, and retinoid binding proteins are investigated.
Abstract: The membrane transport and cytosolic solubilization of hydrophobic ligands, including sterols, fatty acids, retinoids, and certain hydrophobic carcinogens, are facilitated by a group of similar low molecular weight proteins: plasma membrane transport protein, fatty acid binding proteins, sterol carrier protein, and retinoid binding proteins. The cellular content of these proteins, which establishes the capacity of a cell to utilize the various ligands, is determined by events regulating transcription and translation, e.g., the mRNA abundance of liver- and gut-type FABPs is increased by dietary fat, and translation of hepatic FABP appears to be stimulated by insulin. Functions attributable to these lipid binding proteins remain unclear, but data are presented that indicate physiological roles in 1) fatty acid transport, esterification, and oxidation, 2) steroidogenesis, and 3) retinoid uptake, retinaldehyde reduction, and retinol esterification. An exciting and novel prospect for cellular trafficking prote...
94 citations
TL;DR: The FABP content and the fatty acid-binding capacity of adult heart and liver were in good accordance under various physiological conditions.
89 citations
TL;DR: The need exists for studies of complexes of L- FABP with the HPETEs and HETEs in hepatocytes, especially since L-FABP has previously been associated with mitosis in normal hepatocytes and shown to be the target protein of two liver carcinogens, and these arachidonic acid metabolites have been found to be able to modulate activities related to cell growth.
82 citations
TL;DR: The newly found compartmentation of cardiac FABP in the heart cell must be considered when the true functions of the protein, yet to be defined, are studied.
82 citations
01 Jan 1989
TL;DR: functions attributable to cellular lipid binding proteins remain unclear, but data are presented that indicate physiological roles in 1) fatty acid transport, esterification, and oxidation, 2) steroidogenesis, and 3) retinoid uptake, retinaldehyde reduction, and retinol esterization.
Abstract: The membrane transport and cytosolic solubilization of hydrophobic ligands, including sterols, fatty acids, retinoids, and certain hydrophobic carcinogens, are facilitated by a group of similar low molecular weight proteins: plasma membrane transport protein, fatty acid binding proteins, sterol carrier protein, and retinoid binding proteins. The cellular content of these proteins, which establishes the capacity of a cell to utilize the various ligands, is determined by events regulating transcription and translation, e.g., the mRNA abundance of liver- and gut-type FABPs is increased by dietary fat, and translation of hepatic FABP appears to be stimulated by insulin. Functions attributable to these lipid binding proteins remain unclear, but data are presented that indicate physiological roles in 1) fatty acid transport, esterification, and oxidation, 2) steroidogenesis, and 3) retinoid uptake, retinaldehyde reduction, and retinol esterification. An exciting and novel prospect for cellular trafficking prote...
79 citations
TL;DR: Plasma FABP levels are consistent with the proposal that loss of F ABP contributes to the myocardial damage associated with ischemia and reperfusion and additional studies are needed to determine the exact role of FABp in the regulation of fatty acid metabolism in the heart.
63 citations
TL;DR: There exists a declining portal‐to‐central gradient in liver fatty acid binding protein cellular abundance in the hepatic acinus of untreated male rats, and the increased synthesis and abundance of liver fatty acids binding protein in female and clofibrate‐treated male rats results in two different alterations in the acinar expression of this protein.
TL;DR: The results indicate that the FABP-fatty acid complex may function as an intermediate in the transfer of fatty acids between membranes.
TL;DR: Large fluorescence quantum yields and long excited state life-times indicate that the FABP-binding site for ffa is highly hydrophobic, and analysis of rotational correlation times for the F ABP-bound AOffa suggest that the ffa are tightly bound to the protein.
TL;DR: H-FABP was found to modulate cardiac energy production by controlling the transfer of acyl-L-carnitine to the mitochondrial β-oxidative system and may also protect the heart against the toxic effects of high intracellular levels of fatty acid intermediates that arise during ischemia.
Abstract: Translocation of lipids inside mammalian cells is considered to be facilitated by a number of low-molecular weight lipid binding proteins. An overview of these proteins is given, with particular reference to the heart. Three distinct phospholipid transfer proteins specifically stimulate the net transfer of individual phospholipid classes between membrane structures. In rat cardiac muscle their content is 15-140 pmol/g ww. Fatty acid-binding proteins (FABP) are abundantly present in tissues actively involved in the uptake or utilization of long-chain fatty acids, such as intestine, liver and heart. The four distinct FABP types now identified show a complex tissue distribution with some tissues containing more than one type. Heart (H-) FABP comprises about 5% of the cytosolic protein mass; its content in rat heart is 100 nmol/g ww. Immunochemical evidence has been obtained for the presence of H-FABP in several other tissues, including red skeletal muscle, mammary gland and kidney. Beside long-chain fatty acids FABP binds with similar affinity also fatty acyl-CoA and acyl-L-carnitines. In heart the latter compound may be the primary ligand, since normoxic acyl-L-carnitine levels are several fold higher than those of fatty acids. In addition, H-FABP was found to modulate cardiac energy production by controlling the transfer of acyl-L-carnitine to the mitochondrial beta-oxidative system. H-FABP may also protect the heart against the toxic effects of high intracellular levels of fatty acid intermediates that arise during ischemia.
TL;DR: Chronic stimulation of rat fast‐twitch muscle increased the content of both fatty acid‐binding protein (FABP) and myoglobin and increased those in citrate synthase and 3‐hydroxyacyl‐CoA dehydrogenase activities.
TL;DR: L Liver FABPs show a much higher enhancement of fluorescence at binding of 11-dansylaminoundecanoic acid, 16-anthroyloxy-palmitic acid and 1-pyrene-dodecanoIC acid than heart FABP and additionally a blue shift in excitation and emission wavelengths with the first fatty acid.
TL;DR: The data exclude the idea that the uptake of fatty acids into cells is the result of binding proteins and/or catalyzed reactions at the water-membrane interface of the cell or within the plane of the plasma membrane.
TL;DR: The FABP content determined by ELISA was comparable in various human muscles and cultured muscle cells, but lower than that in rat muscles, and no cross-reactivity was observed with liver FABp and its antiserum.
TL;DR: Cysteine-69 is shown to react slowly, but quantitatively, with 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), indicating that the thiol group is free, but may be buried within the protein.
Abstract: 1. A new, simple and high-yield procedure is described for the purification of hepatic fatty-acid-binding protein from rat liver using naphthylaminodecyl-agarose as an affinity column. 2. Cysteine-69 is shown to react slowly, but quantitatively, with 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), indicating that the thiol group is free, but may be buried within the protein. 3. Fatty acids do not affect the DTNB reactivity of this cysteine residue; however, cysteine reactivity is enhanced in the presence of haem and oleoyl-CoA. 4. Fatty-acid-binding protein that has been modified with DTNB is still able to bind the fluorescent fatty acid 11-(dansylamino)undecanoic acid, indicating that cysteine-69 may be remote from the fatty-acid-binding site.
TL;DR: A fatty acid-binding protein (FABP) was purified from rabbit heart and characterized with respect to size, isoelectric point, and tissue distribution, and Rabbit heart FABP was shown to bind two molecules of fatty acid.
Abstract: A fatty acid-binding protein (FABP) was purified from rabbit heart and characterized with respect to size, isoelectric point, and tissue distribution. This protein was found in red muscle, diaphragm, and aorta, as well as in the heart. Amino acid composition of rabbit heart FABP differed only slightly from the human and rat proteins. Rabbit heart FABP was shown to bind two molecules of fatty acid. A monoclonal antibody was developed and used to demonstrate the feasibility of a one-step purification with affinity chromatography. Cross-reactivity was found between the human protein and the rabbit antibody, and an immunoassay was developed to human heart FABP. Levels of human heart FABP in the plasma of patients with acute myocardial infarction were significantly elevated (83 +/- 9 micrograms/ml) compared with patients with pulmonary edema (52 +/- 7 micrograms/ml) and normal volunteers (28 +/- 5 micrograms/ml; p less than 0.05, mean +/- SEM).
TL;DR: A fatty acid‐binding protein was purified from male rat kidney and identified as α2U‐globulin, which is the major male‐specific protein in rat urine, suggesting that the protein has been proteolytically processed in the kidney.
TL;DR: Cellular influx kinetics of a representative long chain fatty acid, [3H]oleate, were examined in monolayer cultures of three different human hepatoma cell lines and suggest that uptake of fatty acids by human hepat cancer cells may be mediated by a specific membrane fatty acid binding protein.
01 Jan 1989
TL;DR: The results indicate that FABP can scavenge free radicals which may be present in an ischemic/reperfused heart and, thus, may play a significant physiological role in the heart during ischemia and reperfusion.
Abstract: Recent investigations have indicated the presence of a fatty acid binding protein (FABP) in mammalian heart. This protein binds free fatty acids and their esters with high affinity, however, its physiological role remains unknown. Since FABP constitutes a significant amount of cystolic protein, it is likely that it would be a target for free radical attack. To test this hypothesis, FABP was examined for scavenging against free radicals such as the superoxide anion (O2-), hydroxyl radical (OH.) and hypochlorite radical (OCl.) which may be present in an ischemic reperfused heart. Our results suggest that FABP scavenges O2-, OH. and OCl. as indicated by the FABP inhibition of O2- -dependent reduction of cytochrome c, OH.-dependent hydroxybenzoic acid formation and OCl.-mediated chemiluminescence response. FABP was found to be a more potent scavenger of these free radicals compared to bovine serum albumin. Furthermore, FABP was more effective in scavenging OH. than O2-, and inhibited OH. mediated lipid peroxidation process. These results indicate that FABP can scavenge free radicals which may be present in an ischemic/reperfused heart and, thus, may play a significant physiological role in the heart during ischemia and reperfusion.
TL;DR: The possible property of fatty acid-binding proteins (FABPs) to transport fatty acid was investigated in various model systems with FABP preparations from liver and heart but was not detectable with a combination of oleic acid-loaded mitochondria and vesicles or liposomes due to the rapid spontaneous transfer.
Abstract: The possible property of fatty acid-binding proteins (FABPs) to transport fatty acid was investigated in various model systems with FABP preparations from liver and heart. An effect of FABP, however, was not detectable with a combination of oleic acid-loaded mitochondria and vesicles or liposomes due to the rapid spontaneous transfer. Therefore, the mitochondria were separated from the vesicles in an equilibrium dialysis cell. The spontaneous fatty acid transfer was much lower and addition of FABP resulted in an increase of fatty acid transport. Oleic acid was withdrawn from different types of monolayers by FABP with rates up to 10%/min. When two separate monolayers were used, FABP increased fatty acid transfer between these monolayers and an equilibrium was reached.
TL;DR: Fatty acid binding activity associated with a 14,000-15,000 mol.
Abstract: 1. Fatty acid binding activity associated with a 14,000-15,000 mol. wt protein was observed in the cytosolic fraction of liver, duodenum, myocardium, adipose, pectoral and gastrocnemius muscles of chickens. 2. Polyclonal antisera prepared against chicken liver fatty acid binding protein affinity for only liver FABP and a 14,000 mol. wt fatty acid binding protein in the intestine. 3. A fatty acid binding protein was not detected in chicken plasma.
TL;DR: F fetal liver FABPs play a regulatory role in critical aspects of cellular physiology during human embryogenesis and protect glucose-6-phosphate dehydrogenase from the feed-back inhibition exerted by added palmitoyl-CoA and oleate.
TL;DR: Apparent molecular weight, pI, functional activity, and hybridization of a rat hFABP cDNA probe with chicken liver mRNA suggest that chicken liver FABP is structurally related to hepatic FABPs, previously isolated and characterized in the rat.
Abstract: 1. Fatty acid binding protein (FABP) was isolated from chicken liver cytosol. 2. Apparent molecular weight, pI, functional activity, and hybridization of a rat hFABP cDNA probe with chicken liver mRNA suggest that chicken liver FABP is structurally related to hepatic FABP (hFABP) previously isolated and characterized in the rat. 3. Fatty acids bound to liver FABP affect the electrophoretic nature of FABP. 4. Levels of liver FABP mRNA isolated from chickens at various stages of development parallel developmental alterations in lipid metabolism, being highest in day old chicks and laying hens versus juvenile birds.
TL;DR: The amino acid sequence of rat heart fatty acid-binding protein was re-examined by analysing the tryptic and the chymotryptic peptides, providing evidence for the actual existence of the molecular species predicted from the cDNA.
Abstract: The amino acid sequence of rat heart fatty acid-binding protein was re-examined by analysing the tryptic and the chymotryptic peptides, since some discrepancies have been reported between the sequences determined by protein analyses and that deduced from the cDNA analyses. Our result completely agreed with the amino acid sequence predicted from the cDNA analyses, providing evidence for the actual existence of the molecular species predicted from the cDNA.
TL;DR: Defatted lung FABP reverses the inhibitory effect of palmitoyl coenzyme A (CoA) (PAL- CoA) on lung glucose-6-phosphate dehydrogenase (G6PD), a key enzyme of the hexose monophosphate (HMP) shunt pathway in vitro.
Abstract: Fatty acid-binding protein (FABP) was isolated, purified, and characterized from developing human fetal lung cytosol by gel filtration and ion-exchange chromatography. FABP exists in three immunochemically identical forms, DE-I, DE-II, and DE-III, having Mr 15,200 ± 200 each and isoelectric pH 7.8, 6.9, and 5.4, respectively. DE-I is almost lipid-free, DE-II binds mainly long-chain unsaturated fatty acids, and DE-III is an arachi-donic acid carrier. One mole of DE-II and DE-III each binds 1 mol of fatty acids noncov-alently. Concentrations of all these FABPs increase gradually from early gestation to term. Defatted lung FABP reverses the inhibitory effect of palmitoyl coenzyme A (CoA) (PAL-CoA) on lung glucose-6-phosphate dehydrogenase (G6PD), a key enzyme of the hexose monophosphate (HMP) shunt pathway. This protein when added alone activates the enzyme, suggesting that the original submaximal activity is probably due to the presence of endogenous long-chain fatty acyl CoA esters in the cytosols. As FABP...