scholarly journals Malonyl coenzyme A and the regulation of functional carnitine palmitoyltransferase-1 activity and fat oxidation in human skeletal muscle

2002 ◽  
Vol 110 (11) ◽  
pp. 1687-1693 ◽  
Author(s):  
Blake B. Rasmussen ◽  
Ulf C. Holmbäck ◽  
Elena Volpi ◽  
Beatrice Morio-Liondore ◽  
Douglas Paddon-Jones ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Coenzyme A ◽  
Fat Oxidation ◽  
Carnitine Palmitoyltransferase ◽  
Carnitine Palmitoyltransferase 1

FAT OXIDATION AND ACYL-COENZYME A BINDING PROTEIN CONTENT IN HUMAN SKELETAL MUSCLE

2003 ◽  
Vol 35 (Supplement 1) ◽  
pp. S255
Author(s):  
J Franch ◽  
K Levin ◽  
J R. Daugaard ◽  
J Jensen ◽  
P K. Pedersen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Content ◽  
Human Skeletal Muscle ◽  
Coenzyme A ◽  
Binding Protein ◽  
Fat Oxidation ◽  
Acyl Coenzyme A

Fatty Acid Oxidation in Mitochondria from Needle Biopsy Samples of Human Skeletal Muscle

1984 ◽  
Vol 66 (2) ◽  
pp. 173-178 ◽  
Author(s):  
K. Gohil ◽  
D. A. Jones ◽  
R. H. T. Edwards
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Needle Biopsy ◽  
Human Skeletal Muscle ◽  
Normal Subjects ◽  
Normal Activity ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Palmitoyl Carnitine ◽  
Mitochondrial Abnormality

1. Activities for the oxidation of palmitoyl-carnitine, of palmitoyl-CoA and of carnitine palmitoyltransferase were measured in mitochondria prepared from needle biopsy samples of human skeletal muscle. Results are presented for nine normal subjects and 18 patients in whom there was evidence of mitochondrial abnormality. 2. Palmitoylcarnitine and palmitoyl-CoA oxidation were measured spectrophotometrically by following the reduction of added cytochrome c in the presence of cyanide. 3. Because of large variations in the activities between subjects it was essential to express the three activities per unit of cytochrome c oxidase activity to demonstrate unambiguous specific alterations in the activities. 4. In most of the patients the order of the three activities was similar to that in the normal subjects. However, in five cases the activity for palmitoylcarnitine oxidation was less than 4% of the mean normal value. In two of these patients, the low activity could be accounted for by very low (<10% normal) activity of carnitine palmitoyltransferase (CPT). In another two patients the activity of CPT was normal but that of palmitoyl-CoA dehydrogenase (a measure of β-oxidation) was very low.

scholarly journals A case of carnitine palmitoyltransferase II deficiency in human skeletal muscle

FEBS Letters ◽  
1988 ◽  
Vol 241 (1-2) ◽  
pp. 126-130 ◽  
Author(s):  
Rajinder Singh ◽  
Isobel.M. Shepherd ◽  
Jerry P. Derrick ◽  
Rona R. Ramsay ◽  
H.Stanley A. Sherratt ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Carnitine Palmitoyltransferase ◽  
Carnitine Palmitoyltransferase Ii

scholarly journals Differential epigenetic and transcriptional response of the skeletal muscle carnitine palmitoyltransferase 1B (CPT1B) gene to lipid exposure with obesity

2015 ◽  
Vol 309 (4) ◽  
pp. E345-E356 ◽  
Author(s):  
Jill M. Maples ◽  
Jeffrey J. Brault ◽  
Carol A. Witczak ◽  
Sanghee Park ◽  
Monica J. Hubal ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Dna Methylation ◽  
Transcription Factor ◽  
Fatty Acid ◽  
Histone Acetylation ◽  
Human Skeletal Muscle ◽  
Epigenetic Modifications ◽  
Carnitine Palmitoyltransferase ◽  
Severely Obese ◽  
Metabolic Inflexibility

The ability to increase fatty acid oxidation (FAO) in response to dietary lipid is impaired in the skeletal muscle of obese individuals, which is associated with a failure to coordinately upregulate genes involved with FAO. While the molecular mechanisms contributing to this metabolic inflexibility are not evident, a possible candidate is carnitine palmitoyltransferase-1B (CPT1B), which is a rate-limiting step in FAO. The present study was undertaken to determine if the differential response of skeletal muscle CPT1B gene transcription to lipid between lean and severely obese subjects is linked to epigenetic modifications (DNA methylation and histone acetylation) that impact transcriptional activation. In primary human skeletal muscle cultures the expression of CPT1B was blunted in severely obese women compared with their lean counterparts in response to lipid, which was accompanied by changes in CpG methylation, H3/H4 histone acetylation, and peroxisome proliferator-activated receptor-δ and hepatocyte nuclear factor 4α transcription factor occupancy at the CPT1B promoter. Methylation of specific CpG sites in the CPT1B promoter that correlated with CPT1B transcript level blocked the binding of the transcription factor upstream stimulatory factor, suggesting a potential causal mechanism. These findings indicate that epigenetic modifications may play important roles in the regulation of CPT1B in response to a physiologically relevant lipid mixture in human skeletal muscle, a major site of fatty acid catabolism, and that differential DNA methylation may underlie the depressed expression of CPT1B in response to lipid, contributing to the metabolic inflexibility associated with severe obesity.

Factors regulating fat oxidation in human skeletal muscle

2011 ◽  
Vol 12 (10) ◽  
pp. 852-858 ◽  
Author(s):  
B. Kiens ◽  
T. J. Alsted ◽  
J. Jeppesen
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Fat Oxidation

Malonyl-CoA and carnitine in regulation of fat oxidation in human skeletal muscle during exercise

2005 ◽  
Vol 288 (1) ◽  
pp. E133-E142 ◽  
Author(s):  
Carsten Roepstorff ◽  
Nils Halberg ◽  
Thore Hillig ◽  
Asish K. Saha ◽  
Neil B. Ruderman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Human Skeletal Muscle ◽  
Fat Oxidation ◽  
Free Carnitine ◽  
Carbohydrate Diet ◽  
Acetyl Coa ◽  
Low Carbohydrate Diet ◽  
Malonyl Coa ◽  
Amp Activated Protein Kinase

Intracellular mechanisms regulating fat oxidation were investigated in human skeletal muscle during exercise. Eight young, healthy, moderately trained men performed bicycle exercise (60 min, 65% peak O2 consumption) on two occasions, where they ingested either 1) a high-carbohydrate diet (H-CHO) or 2) a low-carbohydrate diet (L-CHO) before exercise to alter muscle glycogen content as well as to induce, respectively, low and high rates of fat oxidation. Leg fat oxidation was 122% higher during exercise in L-CHO than in H-CHO ( P < 0.001). In keeping with this, the activity of α2-AMP-activated protein kinase (α2-AMPK) was increased twice as much in L-CHO as in H-CHO ( P < 0.01) at 60 min of exercise. However, acetyl-CoA carboxylase (ACC)β Ser221 phosphorylation was increased to the same extent (6-fold) under the two conditions. The concentration of malonyl-CoA was reduced 13% by exercise in both conditions ( P < 0.05). Pyruvate dehydrogenase activity was higher during exercise in H-CHO than in L-CHO ( P < 0.01). In H-CHO only, the concentrations of acetyl-CoA and acetylcarnitine were increased ( P < 0.001), and the concentration of free carnitine was decreased ( P < 0.01), by exercise. The data suggest that a decrease in the concentration of malonyl-CoA, secondary to α2-AMPK activation and ACC inhibition (by phosphorylation), contributes to the increase in fat oxidation observed at the onset of exercise regardless of muscle glycogen levels. They also suggest that, with high muscle glycogen, the availability of free carnitine may limit fat oxidation during exercise, due to its increased use for acetylcarnitine formation.

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