title: Effect of fatty acid-binding proteins on intermembrane fatty acid transport studies on different types and mutant proteins.
abstract: Liposomes of different charge fixed to nitrocellulose filters were used to study the transfer of fatty acids to rat heart or liver mitochondria in the presence of fatty acid-binding protein (FABP) or albumin. [14C]Palmitate oxidation was used as a parameter. Different FABP types and heart FABP mutants were tested. The charge of the liposomes did not influence the solubilization and mitochondrial oxidation of palmitate without FABP and the amount of solubilized palmitate in the presence of FABP. Mitochondria did not show a preference for oxidation of FABP-bound palmitate over their tissue-specific FABP type. All FABP types increased palmitate oxidation by heart and liver mitochondria with neutral, positive and negative liposomes by 2.5-fold, 3.2-fold and twofold, respectively. Ileal lipid-binding protein and H-FABP mutants that do not bind fatty acid had no effect. Other H-FABP mutants had different effects, dependent on the site of mutation. The effect of albumin was similar to, but not dependent on, liposome charge. The ionic strength had only a slight effect. In conclusion, the transfer of palmitate from liposomal membranes to mitochondria was increased by all FABP types to a similar extent. The membrane charge had a large effect in contrast to the origin of the mitochondria.
authors.affiliation: Department of Biochemistry, University of Nijmegen, The Netherlands. J.Veerkamp@bioch.kun.nl
authors.forename: J H
authors.initials: JH
authors.lastname: Veerkamp
authors.forename: H T
authors.initials: HT
authors.lastname: Van Moerkerk And
authors.forename: A W
authors.initials: AW
authors.lastname: Zimmerman
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D003066:Coenzyme A Ligases / Q000378:metabolism; D004058:Diffusion; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D008081:Liposomes / Q000378:metabolism; D008297:Male; D008564:Membrane Potentials; D008929:Mitochondria, Heart / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D009928:Organ Specificity; D010084:Oxidation-Reduction; D010168:Palmitates / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D011994:Recombinant Proteins / Q000378:metabolism; D025521:Tumor Suppressor Proteins
chemical_list: D002352:Carrier Proteins; C107608:FABP7 protein, human; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D008081:Liposomes; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010168:Palmitates; D011994:Recombinant Proteins; D025521:Tumor Suppressor Proteins; D003066:Coenzyme A Ligases