Synergistic effects of combination of three wavelengths and different light sources in cytochrome c oxidase activity in intact skeletal muscle of rats

2019 ◽  
Author(s):  
Ernesto Cesar Pinto Leal-Junior ◽  
Shaiane da Silva Tomazoni
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Synergistic Effects ◽  
Light Sources

Early effects of spinal cord transection on skeletal muscle properties

2006 ◽  
Vol 31 (4) ◽  
pp. 398-406 ◽  
Author(s):  
Melissa D. Kelley ◽  
Satra Nim ◽  
Guy Rousseau ◽  
Jonathon R. Fowles ◽  
René J.L. Murphy
Keyword(s):  
Skeletal Muscle ◽  
Spinal Cord ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Muscle Mass ◽  
Oxidase Activity ◽  
Myofibrillar Protein ◽  
Spinal Cord Transection ◽  
Triceps Brachii ◽  
Muscle Properties

Modulation of β-adrenergic receptor (β-AR) activity affects muscle mass and could have a role in the reduction of muscle mass observed following spinal cord transection (Tx). The aims of this study were to examine the early acute effects of Tx on muscle mass, total and myofibrillar protein concentrations, cytochrome c oxidase activity, and β-AR density of skeletal muscle, to ascertain if any change in muscle properties could be related to β-AR signalling events. Female Sprague–Dawley rats (n = 33; ~255 g) were randomly assigned to 4 experimental groups: control 4 d, control 8 d, Tx 4 d, and Tx 8 d. A complete Tx was performed surgically at the T10 cord level. Compared with controls, muscle mass and muscle – body mass ratios decreased significantly following Tx, with no significant change observed in total and myofibrillar protein concentrations. Spinal cord Tx also resulted in a significant decrease in plantaris cytochrome c oxidase activity by 24% at Tx 4 d and 28% at Tx 8 d (p < 0.05). β-AR density of the lateral gastrocnemius was unchanged; however, the β-AR density of the forelimb triceps brachii m. was found to increase after Tx. Our results suggest that changes in muscle mass and cytochrome c oxidase activity rapidly occur after Tx and do not appear to be related to changes in β-AR density.

scholarly journals Comparisons of copper deficiency states in the murine mutants blotchy and brindled. Changes in copper-dependent enzyme activity in 13-day-old mice

1986 ◽  
Vol 238 (1) ◽  
pp. 177-183 ◽  
Author(s):  
M Phillips ◽  
J Camakaris ◽  
D M Danks
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Enzyme Activity ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Copper Concentration ◽  
Copper Deficiency ◽  
Single Temperature ◽  
Deficient Mice

The activity of two copper-dependent enzymes, cytochrome c oxidase and copper, zinc-superoxide dismutase, was determined in six tissues of age-matched (13-day-old) copper-deficient mutant and normal mice. In the two mutants ‘brindled’ and ‘blotchy’, brain, heart and skeletal muscle had significant enzyme deficiencies. Cytochrome c oxidase was more severely affected than was superoxide dismutase. In these three tissues the degree of deficiency could be correlated with decreased copper concentration; however, enzyme activity was normal in liver, kidney and lung, despite abnormal copper concentrations in these tissues. In nutritionally copper-deficient mice, all six tissues showed decreased enzyme activity, which was most marked in brain, heart and skeletal muscle, the tissues which showed enzyme deficiencies in the mutants. Analysis in vitro of cytochrome c oxidase (temperature coefficient = 2) at a single temperature was found to underestimate the deficiency of this enzyme in hypothermic copper-deficient animals. Cytochrome c oxidase deficiency may therefore be sufficiently severe in vivo to account for the clinical manifestations of copper deficiency. An injection of copper (50 micrograms of Cu+) at 7 days increased cytochrome c oxidase activity by 13 days in all deficient tissues of brindled mice, and in brain and heart from blotchy mice. However, skeletal-muscle cytochrome c oxidase in blotchy mutants did not respond to copper injection. Cytochrome c oxidase activity increased to normal in all tissues of nutritionally copper-deficient mice after copper injection, except in the liver. Hepatic enzyme activity remained severely deficient despite a liver copper concentration three times that found in copper-replete controls. Superoxide dismutase activity did not increase with treatment in either mutant, but its activity was higher than control levels in nutritionally deficient mice after injection. This difference is probably due to sequestration of copper in mutant tissue such as kidney, but a defect in the copper transport pathway to superoxide dismutase cannot be excluded.

Effect of pre-irradiation with different doses, wavelengths, and application intervals of low-level laser therapy on cytochrome c oxidase activity in intact skeletal muscle of rats

2014 ◽  
Vol 30 (1) ◽  
pp. 59-66 ◽  
Author(s):  
Gianna Móes Albuquerque-Pontes ◽  
Rodolfo de Paula Vieira ◽  
Shaiane Silva Tomazoni ◽  
Cláudia Oliveira Caires ◽  
Victoria Nemeth ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Laser Therapy ◽  
Oxidase Activity ◽  
Low Level Laser Therapy ◽  
Low Level ◽  
Low Level Laser ◽  
Level Laser ◽  
Different Doses

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

scholarly journals A genome-wide copper-sensitized screen identifies novel regulators of mitochondrial cytochrome c oxidase activity

2021 ◽  
Vol 296 ◽  
pp. 100485
Author(s):  
Natalie M. Garza ◽  
Aaron T. Griffin ◽  
Mohammad Zulkifli ◽  
Chenxi Qiu ◽  
Craig D. Kaplan ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Mitochondrial Cytochrome ◽  
Genome Wide ◽  
A Genome ◽  
Mitochondrial Cytochrome C

Effect of subunit III removal on control of cytochrome c oxidase activity by pH

Biochemistry ◽  
1988 ◽  
Vol 27 (17) ◽  
pp. 6307-6314 ◽  
Author(s):  
Linda C. Gregory ◽  
Shelagh Ferguson-Miller
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Subunit Iii
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