title: Effects of conjugated linoleic acid isomers on lipid-metabolizing enzymes in male rats.
abstract: Male weanling Wistar rats (n = 15), weighing 200-220 g, were allocated for 6 wk to diets containing 1% (by weight) of conjugated linoleic acid (CLA), either as the 9c,11 t-isomer, the 10t,12c-isomer, or as a mixture containing 45% of each of these isomers. The five rats of the control group received 1% of oleic acid instead. Selected enzyme activities were determined in different tissues after cellular subfractionation. None of the CLA-diet induced a hepatic peroxisome-proliferation response, as evidenced by a lack of change in the activity of some characteristic enzymes [i.e., acyl-CoA oxidase, CYP4A1, but also carnitine palmitoyltransferase-I (CPT-I)] or enzyme affected by peroxisome-proliferators (glutathione S-transferase). In addition to the liver, the activity of the rate-limiting beta-oxidation enzyme in mitochondria, CPT-I, did not change either in skeletal muscle or in heart. Conversely, its activity increased more than 30% in the control value in epididymal adipose tissue of the animals fed the CLA-diets containing the 10t,12c-isomer. Conversely, the activity of phosphatidate phosphohydrolase, a rate-limiting enzyme in glycerolipid neosynthesis, remained unchanged in adipose tissue. Kinetic studies conducted on hepatic CPT-I and peroxisomal acyl-CoA oxidase with CoA derivatives predicted a different channeling of CLA isomers through the mitochondrial or the peroxisomal oxidation pathways. In conclusion, the 10t,12c-CLA isomer seems to be more efficiently utilized by the cells than its 9c,11t homolog, though the Wistar rat species appeared to be poorly responsive to CLA diets for the effects measured.
authors.affiliation: I.N.R.A, Unité de Nutrition Lipidique, Dijon, France. jean-charles.martin@ibaic.u-psud.fr
authors.forename: J C
authors.initials: JC
authors.lastname: Martin
authors.forename: S
authors.initials: S
authors.lastname: Grégoire
authors.forename: M H
authors.initials: MH
authors.lastname: Siess
authors.forename: M
authors.initials: M
authors.lastname: Genty
authors.forename: J M
authors.initials: JM
authors.lastname: Chardigny
authors.forename: O
authors.initials: O
authors.lastname: Berdeaux
authors.forename: P
authors.initials: P
authors.lastname: Juanéda
authors.forename: J L
authors.initials: JL
authors.lastname: Sébédio
mesh_terms: D042962:Acyl-CoA Oxidase; D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000378:metabolism; D042926:Cytochrome P-450 CYP4A; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D007700:Kinetics; D019787:Linoleic Acid / Q000494:pharmacology*; D050356:Lipid Metabolism; D008099:Liver / Q000201:enzymology; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D018482:Muscle, Skeletal / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
chemical_list: D004798:Enzymes; D003577:Cytochrome P-450 Enzyme System; D019787:Linoleic Acid; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D042926:Cytochrome P-450 CYP4A; D042962:Acyl-CoA Oxidase; D002334:Carnitine O-Palmitoyltransferase; D005982:Glutathione Transferase