Effects of conjugated linoleic acid isomers on lipid-metabolizing enzymes in male rats
Autor: | Jean-Louis Sébédio, Pierre Juanéda, Olivier Berdeaux, Martine Genty, Stéphane Grégoire, Jean-Michel Chardigny, Jean-Charles Martin, Marie-Hélène Siess |
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Rok vydání: | 2000 |
Předmět: |
Male
Linoleic acid Conjugated linoleic acid Adipose tissue Biochemistry Mixed Function Oxygenases Linoleic Acid chemistry.chemical_compound Cytochrome P-450 Enzyme System medicine Animals Acyl-CoA oxidase Carnitine Rats Wistar Muscle Skeletal Glutathione Transferase Oxidase test Carnitine O-Palmitoyltransferase biology Myocardium Organic Chemistry Cell Biology Peroxisome Lipid Metabolism Enzyme assay Enzymes Mitochondria Rats Kinetics Adipose Tissue Liver chemistry biology.protein lipids (amino acids peptides and proteins) Acyl-CoA Oxidase Cytochrome P-450 CYP4A Oxidoreductases medicine.drug |
Zdroj: | Lipids. 35:91-98 |
ISSN: | 1558-9307 0024-4201 |
Popis: | 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. |
Databáze: | OpenAIRE |
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