title: Concomitant increase by peroxisome proliferators of fatty acid-binding protein, peroxisomal beta-oxidation and cytosolic acyl-CoA hydrolase in liver.
abstract: Inductions of FABP in hepatic cytosol by administration of tiadenol and clofibric acid were studied in rats, mice and guinea-pigs. In rats and mice, [1-14C]oleic acid-binding capacity of hepatic cytosol was increased, in association with induction of peroxisomal beta-oxidation, by the administration of either the two peroxisome proliferators. The increase in [1-14C]oleic acid binding capacity was responsible for the increase in the content of FABP in livers. The peroxisome proliferators caused an induction of acyl-CoA hydrolase of lower-molecular-weight form alone in hepatic cytosol of mice, although inductions of two long-chain acyl-CoA hydrolases (higher- and lower-molecular-weight form) were brought about in hepatic cytosol of rats. Guinea-pigs lacked the peroxisome proliferator-caused inductions of FABP, peroxisomal beta-oxidation and acyl-CoA hydrolase. There was no essential difference in the inductions of FABP, acyl-CoA hydrolases and peroxisomal beta-oxidation between tiadenol and clofibric acid, despite a marked difference in their chemical structures. These results suggest that the induction of FABP is correlated with the inductions of both peroxisomal beta-oxidation and cytosolic long-chain acyl-CoA hydrolase of lower-molecular-weight form.
authors.forename: H
authors.initials: H
authors.lastname: Katoh
authors.forename: Y
authors.initials: Y
authors.lastname: Kawashima
authors.forename: M
authors.initials: M
authors.lastname: Takegishi
authors.forename: H
authors.initials: H
authors.lastname: Watanuki
authors.forename: A
authors.initials: A
authors.lastname: Hirose
authors.forename: H
authors.initials: H
authors.lastname: Kozuka
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D002455:Cell Division / Q000187:drug effects; D002994:Clofibrate / Q000031:analogs & derivatives*; D002995:Clofibric Acid / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005233:Fatty Alcohols / Q000494:pharmacology*; D006168:Guinea Pigs; D008099:Liver / Q000378:metabolism*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008830:Microbodies / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010084:Oxidation-Reduction; D010170:Palmitoyl-CoA Hydrolase / Q000096:biosynthesis*; D051381:Rats; D011919:Rats, Inbred Strains; D013869:Thiolester Hydrolases / Q000096:biosynthesis*
chemical_list: D002352:Carrier Proteins; C082667:Fabp5 protein, mouse; C086936:Fabp7 protein, mouse; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005233:Fatty Alcohols; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; C004568:tiadenol; D002995:Clofibric Acid; D013869:Thiolester Hydrolases; D010170:Palmitoyl-CoA Hydrolase; D002994:Clofibrate