title: Role of fatty acid-binding protein in lipid metabolism of insect flight muscle.
abstract: Since insect flight muscles are among the most active muscles in nature, their extremely high rates of fuel supply and oxidation pose interesting physiological problems. Long-distance flights of species like locusts and hawkmoths are fueled through fatty acid oxidation. The lipid substrate is transported as diacylglycerol in the blood, employing a unique and efficient lipoprotein shuttle system. Following diacyglycerol hydrolysis by a flight muscle lipoprotein lipase, the liberated fatty acids are ultimately oxidized in the mitochondria. Locusta flight muscle cytoplasm contains an abundant fatty acid-binding protein (FABP). The flight muscle FABP of Locusta migratoria is a 15 kDa protein with an isoelectric point of 5.8, binding fatty acids in a 1:1 molar stoichiometric ratio. Binding affinity of the FABP for long-chain fatty acids (apparent dissociation constant Kd = 5.21 +/- 0.16 microM) is however markedly lower than that of mammalian FABPs. The NH2-terminal amino acid sequence shares structural homologies with two insect FABPs recently purified from hawkmoth midgut, as well as with mammalian FABPs. In contrast to all other isolated FABPs, the NH2 terminus of locust flight muscle FABP appeared not to be acetylated. During development of the insect, a marked increase in fatty acid binding capacity of flight muscle homogenate was measured, along with similar increases in both fatty acid oxidation capacity and citrate synthase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Experimental Zoology, University of Utrecht, The Netherlands.
authors.forename: D J
authors.initials: DJ
authors.lastname: van der Horst
authors.forename: J M
authors.initials: JM
authors.lastname: van Doorn
authors.forename: P C
authors.initials: PC
authors.lastname: Passier
authors.forename: M M
authors.initials: MM
authors.lastname: Vork
authors.forename: J F
authors.initials: JF
authors.lastname: Glatz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D006110:Grasshoppers; D006801:Humans; D050356:Lipid Metabolism; D008297:Male; D008969:Molecular Sequence Data; D009036:Moths; D009132:Muscles / Q000378:metabolism*; D009363:Neoplasm Proteins; D017386:Sequence Homology, Amino Acid; D025521:Tumor Suppressor Proteins
chemical_list: D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D025521:Tumor Suppressor Proteins