Immunohistochemical demonstration of fibre type-specific isozymes of cytochrome c oxidase in human skeletal muscle

1990 ◽  
Vol 94 (2) ◽  
pp. 211-215 ◽  
Author(s):  
N. Romero ◽  
C. Marsac ◽  
M. Fardeau ◽  
M. Droste ◽  
B. Schneyder ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Fibre Type ◽  
Human Skeletal Muscle ◽  
Immunohistochemical Demonstration

scholarly journals Flux Control of Cytochrome c Oxidase in Human Skeletal Muscle

2000 ◽  
Vol 275 (36) ◽  
pp. 27741-27745 ◽  
Author(s):  
Wolfram S. Kunz ◽  
Alexei Kudin ◽  
Stefan Vielhaber ◽  
Christian E. Elger ◽  
Giuseppe Attardi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Human Skeletal Muscle ◽  
Flux Control

Cytochrome c oxidase assay in minute amounts of human skeletal muscle using single wavelength spectrophotometers

1998 ◽  
Vol 80 (1) ◽  
pp. 107-111 ◽  
Author(s):  
Òscar Miró ◽  
Francesc Cardellach ◽  
Antoni Barrientos ◽  
Jordi Casademont ◽  
Agnés Rötig ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Human Skeletal Muscle

scholarly journals Short-Term Intensified Cycle Training Alters Acute and Chronic Responses of PGC1α and Cytochrome C Oxidase IV to Exercise in Human Skeletal Muscle

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e53080 ◽  
Author(s):  
Nigel K. Stepto ◽  
Boubacar Benziane ◽  
Glenn D. Wadley ◽  
Alexander V. Chibalin ◽  
Benedict J. Canny ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Human Skeletal Muscle ◽  
Short Term ◽  
Cycle Training

Human skeletal muscle adaptation in response to chronic low-frequency electrical stimulation

1994 ◽  
Vol 77 (4) ◽  
pp. 1885-1889 ◽  
Author(s):  
R. Theriault ◽  
G. Theriault ◽  
J. A. Simoneau
Keyword(s):  
Skeletal Muscle ◽  
Electrical Stimulation ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Human Skeletal Muscle ◽  
Citrate Synthase ◽  
Low Frequency ◽  
Vastus Lateralis Muscle ◽  
Activity Levels ◽  
Hydroxyacyl Coa Dehydrogenase

The purpose of the study was to verify the influence of several weeks of chronic low-frequency electrical stimulation (LFES) on the metabolic profile and functional capacity of human skeletal muscle. Knee extensor muscles (KEM) of eight subjects were electrically stimulated at 8 Hz for 8 h/day and 6 days/wk. Vastus lateralis muscle samples were taken before, after 4 wk, and after 8 wk of LFES, and activities of anaerobic (creatine kinase, phosphofructokinase, glyceraldehyde-3-phosphate dehydrogenase) and aerobic-oxidative (citrate synthase, 3-hydroxyacyl-CoA dehydrogenase, cytochrome-c oxidase) enzyme markers were determined. KEM dynamic performance was also assessed before, after 4 wk, and after 8 wk of LFES. Activity levels of anaerobic enzymes were not altered, whereas the activity levels of citrate synthase (29%),3-hydroxyacyl-CoA dehydrogenase (22%), and cytochrome-c oxidase (25%) were significantly increased after 4 wk of LFES but were not further increased after 4 additional wk of LFES. KEM performance was also improved (P < 0.05) but leveled off after 4 wk of LFES. Although significant changes were observed, the results of the present study suggest that the muscle characteristics investigated in the current study have a limited capacity of adaptation in response to this form of chronic LFES.

Demonstration of two isoforms of subunit VIIa of cytochrome c oxidase from human skeletal muscle

FEBS Letters ◽  
1990 ◽  
Vol 263 (2) ◽  
pp. 213-216 ◽  
Author(s):  
Jozef J. Van Beeumen ◽  
André B.P. Van Kuilenburg ◽  
Stefaan Van Bun ◽  
Coby Van den Bogert ◽  
Joseph M. Tager ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Human Skeletal Muscle

Optimal conditions for assay of cytochrome-c-oxidase activity in human skeletal muscle tissue

1982 ◽  
Vol 2 (1) ◽  
pp. 71-79 ◽  
Author(s):  
A.-C. Bylund-Fellenius ◽  
M. Davidsson ◽  
A. Arvidsson ◽  
A. Elander ◽  
T. Scherstén
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Muscle Tissue ◽  
Oxidase Activity ◽  
Human Skeletal Muscle ◽  
Skeletal Muscle Tissue ◽  
Optimal Conditions

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.

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