1994
DOI: 10.1016/0005-2760(94)90002-7
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Expression of human liver fatty acid-binding protein in Escherichia coli and comparative analysis of its binding characteristics with muscle fatty acid-binding protein

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Cited by 61 publications
(47 citation statements)
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References 45 publications
(34 reference statements)
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“…Although two earlier studies separately examined the LCFA binding profiles of rat [7;9;93] and human [94] wild-type L-FABPs, direct comparisons are difficult since different displacement assays were used in each of these studies and both differed from that presented herein. Both human and rat wild-type L-FABP bound the key ligand substrates for triglyceride synthesis: i) LCFA-CoA, consistent with earlier studies [7;9;93;94]; ii) lysophosphatidic, consistent with earlier studies [93;94]; iii) phosphatidic acid (POPA); and iv) L-FABP binding to monoacylglycerol is controversial depending on the technique used. Gel filtration chromatography of liver cytosol, solution NMR, Lipidex, and binding assay with fluorescent MG analog 12-(9-anthroyloxy)oleoyl- sn -1-glycerol (MG12AO) showed that L-FABP binds MG [95;96].…”
Section: Discussionmentioning
confidence: 99%
“…Although two earlier studies separately examined the LCFA binding profiles of rat [7;9;93] and human [94] wild-type L-FABPs, direct comparisons are difficult since different displacement assays were used in each of these studies and both differed from that presented herein. Both human and rat wild-type L-FABP bound the key ligand substrates for triglyceride synthesis: i) LCFA-CoA, consistent with earlier studies [7;9;93;94]; ii) lysophosphatidic, consistent with earlier studies [93;94]; iii) phosphatidic acid (POPA); and iv) L-FABP binding to monoacylglycerol is controversial depending on the technique used. Gel filtration chromatography of liver cytosol, solution NMR, Lipidex, and binding assay with fluorescent MG analog 12-(9-anthroyloxy)oleoyl- sn -1-glycerol (MG12AO) showed that L-FABP binds MG [95;96].…”
Section: Discussionmentioning
confidence: 99%
“…To our knowledge, no differences between oleate and palmitate binding affinities were reported in the human fatty acid binding proteins (FABPs) studied so far, including liver, muscle (40), and adipose tissue (41). Furthermore, studies that have measured fasting fractional uptake of fatty acids by heart (42), liver, or forearm (43) have failed to demonstrate any difference between palmitate and oleate.…”
Section: Discussionmentioning
confidence: 99%
“…Fatty acids are hydrophobic molecules that must be solubilized and transported within the cell by intracellular lipid chaperones known as fatty acid-binding proteins (FABP) 2 (1-4). These low molecular mass (14 -15 kDa) polypeptides are conserved from Caenorhabditis elegans to humans and are involved in fatty acid uptake, transport, and oxidation (5,6). FABPs are abundant in tissues that either require large fluxes of fatty acids or have high demand for fatty acids as an energy source.…”
mentioning
confidence: 99%