Inhibition of carnitine palmitoyltransferase in normal human skeletal muscle and in muscle of patients with carnitine palmitoyltransferase deficiency by long- and short-chain acylcarnitine and acyl-coenzyme A

1993 ◽  
Vol 71 (10) ◽  
Author(s):  
S. Zierz ◽  
S. Neumann-Schmidt ◽  
F. Jerusalem
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Coenzyme A ◽  
Carnitine Palmitoyltransferase ◽  
Short Chain ◽  
Normal Human ◽  
Carnitine Palmitoyltransferase Deficiency ◽  
Acyl Coenzyme A

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

scholarly journals THE DISTRIBUTION OF LACTATE DEHYDROGENASE ISOZYMES IN HUMAN SKELETAL MUSCLE FIBERS

1964 ◽  
Vol 12 (8) ◽  
pp. 608-614 ◽  
Author(s):  
M. VAN WIJHE ◽  
M. C. BLANCHAER ◽  
S. ST. GEORGE-STUBBS
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Isozyme Pattern ◽  
Electrophoretic Separation ◽  
Lactate Dehydrogenase Isozymes ◽  
Dehydrogenase Isozyme ◽  
Lactate Dehydrogenase Isozyme ◽  
Normal Human

A study of the distribution of lactate dehydrogenase isozymes in single fibers from normal human skeletal muscle is presented. The fibers were classified into red, intermediate and white types on histochemical grounds and their lactate dehydrogenase isozyme content assessed by electrophoretic separation in veronal buffered agar. The results generally agreed with previous homogenate studies on animal skeletal muscle, in that the white fibers contained almost exclusively isozymes IV and V, whereas red fibers were rich in isozymes I, II and III, but IV and V also appeared indigenous to these fibers. The intermediate fibers had an isozyme pattern combining the features of red and white fibers. The metabolic implications of these findings are discussed.

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 Engineered Production of Short-Chain Acyl-Coenzyme A Esters inSaccharomyces cerevisiae

2018 ◽  
Vol 7 (4) ◽  
pp. 1105-1115 ◽  
Author(s):  
Nicolas Krink-Koutsoubelis ◽  
Anne C. Loechner ◽  
Anna Lechner ◽  
Hannes Link ◽  
Charles M. Denby ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Short Chain ◽  
Chain Acyl ◽  
Acyl Coenzyme A ◽  
Coenzyme A Esters

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.

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