Proliferation of mitochondria and gene expression of carnitine palmitoyltransferase and fatty acyl-CoA oxidase in rat skeletal muscle, heart and liver by hypolipidemic fatty acids

2000 ◽  
Vol 92 (5) ◽  
pp. 317-329 ◽  
Author(s):  
Geir K. Totland ◽  
Lise Madsen ◽  
Beate Klementsen ◽  
Hege Vaagenes ◽  
Harald Kryvi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Fatty Acids ◽  
Fatty Acyl ◽  
Carnitine Palmitoyltransferase ◽  
Rat Skeletal Muscle ◽  
Acyl Coa Oxidase

Increased muscle carnitine palmitoyltransferase II mRNA after increased contractile activity

1995 ◽  
Vol 268 (2) ◽  
pp. E277-E281 ◽  
Author(s):  
Z. Yan ◽  
S. Salmons ◽  
J. Jarvis ◽  
F. W. Booth
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acids ◽  
Contractile Activity ◽  
Fatty Acyl ◽  
Carnitine Palmitoyltransferase ◽  
The Matrix ◽  
Wet Weight ◽  
Matrix Compartment ◽  
Dependent Transport ◽  
Carnitine Palmitoyltransferase Ii

The capacity of skeletal muscle to oxidize fatty acids increases with endurance training. The oxidation of long-chain fatty acids occurs in mitochondria and is initiated by a carnitine-dependent transport step in which three enzymes help fatty acyl groups enter the matrix compartment. The purpose of this study was to determine whether pretranslational regulation of one of these three enzymes, carnitine palmitoyltransferase II (CPT II), as estimated from the level of CPT II mRNA, plays a role in the doubling of CPT activity in skeletal muscle of rats subjected to daily 2-h bouts of running on treadmills (P. A. Mole, L. B. Oscai, and J. O. Holloszy. J. Clin. Invest. 50: 2323-2330, 1971). After 100 min/day of running on motor-driven treadmills for 2 wk, CPT II mRNA in the plantaris muscle was unchanged when normalized per unit of extracted RNA but was 50% higher (P < 0.05) over sedentary controls when normalized per unit of muscle wet weight. To test whether additional contractile activity would make CPT II mRNA even higher, continuous indirect electrical stimulation was imposed on the tibialis anterior muscles. After 9 days of chronic stimulation, CPT II mRNA was 63, 221, and 137% greater than control (P < 0.001) when normalized to extracted RNA, muscle wet weight, and whole muscle, respectively, compared with the muscle in the control rats. These data indicate that pretranslational regulation of CPT II occurs in response to increased contractile activity in skeletal muscle.

The influence of biocomposites containing genetically modified flax fibers on gene expression in rat skeletal muscle

2010 ◽  
Vol 55 (6) ◽  
pp. 323-329 ◽  
Author(s):  
Tomasz Gredes ◽  
Christiane Kunert-Keil ◽  
Marzena Dominiak ◽  
Tomasz Gedrange ◽  
Magdalena Wróbel-Kwiatkowska ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Genetically Modified ◽  
Rat Skeletal Muscle ◽  
Flax Fibers

scholarly journals Chlorpromazine and carnitine-dependency of rat liver peroxisomal β-oxidation of long-chain fatty acids

1987 ◽  
Vol 241 (3) ◽  
pp. 783-791 ◽  
Author(s):  
J Vamecq
Keyword(s):  
Fatty Acids ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Rat Liver ◽  
Fatty Acyl ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Synthetase Activity ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Mitochondrial Fatty Acid

The enzyme targets for chlorpromazine inhibition of rat liver peroxisomal and mitochondrial oxidations of fatty acids were studied. Effects of chlorpromazine on total fatty acyl-CoA synthetase activity, on both the first and the third steps of peroxisomal beta-oxidation, on the entry of fatty acyl-CoA esters into the peroxisome and on catalase activity, which allows breakdown of the H2O2 generated during the acyl-CoA oxidase step, were analysed. On all these metabolic processes, chlorpromazine was found to have no inhibitory action. Conversely, peroxisomal carnitine octanoyltransferase activity was depressed by 0.2-1 mM-chlorpromazine, which also inhibits mitochondrial carnitine palmitoyltransferase activity in all conditions in which these enzyme reactions are assayed. Different patterns of inhibition by the drug were, however, demonstrated for both these enzyme activities. Inhibitory effects of chlorpromazine on mitochondrial cytochrome c oxidase activity were also described. Inhibitions of both cytochrome c oxidase and carnitine palmitoyltransferase are proposed to explain the decreased mitochondrial fatty acid oxidation with 0.4-1.0 mM-chlorpromazine reported by Leighton, Persico & Necochea [(1984) Biochem. Biophys. Res. Commun. 120, 505-511], whereas depression by the drug of carnitine octanoyltransferase activity is presented as the factor responsible for the decreased peroxisomal beta-oxidizing activity described by the above workers.

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