1993
DOI: 10.1016/0014-5793(93)81788-2
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Oxidative stress during recovery from muscle atrophy

Abstract: Single ankle joints of male Wistar rats (15-week-old) were immobilized in the extended position for 7 days and remobilized for 5 days after the immobilization period. Atrophic and contralateral soleus, typical slow red muscles, were collected and their levels of thiobarbituric acid-reactive substance (TBARS) and glutathione were measured. Five-day remobilization did not increase muscle weight significantly. However, there were significant increases in TBARS and oxidized glutathione in the recovering muscle, wh… Show more

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Cited by 37 publications
(37 citation statements)
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(12 reference statements)
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“…It is also conceivable that HSP72 can play a protective role in the prevention of muscle protein degradation during periods of reduced contractile activity. The potential mechanistic link between HSP72 and protein degradation is that muscle atrophy induced by immobilization is accompanied by oxidative injury in myocytes (6). This increase in oxidative stress accelerates muscle protein breakdown because oxidatively modified proteins are very susceptible to proteolytic attack (5).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…It is also conceivable that HSP72 can play a protective role in the prevention of muscle protein degradation during periods of reduced contractile activity. The potential mechanistic link between HSP72 and protein degradation is that muscle atrophy induced by immobilization is accompanied by oxidative injury in myocytes (6). This increase in oxidative stress accelerates muscle protein breakdown because oxidatively modified proteins are very susceptible to proteolytic attack (5).…”
Section: Discussionmentioning
confidence: 99%
“…A conceivable link between HSP72 and reduced protein degradation in muscle is as follows. Recent evidence demonstrates that muscle atrophy induced by immobilization is associated with oxidative injury in myocytes (6). This increase in oxidative stress may accelerate muscle protein breakdown because oxidatively modified proteins are more susceptible to proteolytic attack.…”
mentioning
confidence: 99%
“…Additionally, due to the comparatively greater numbers of mitochondria contained within them, oxidative fibres produce comparatively larger quantities of reactive oxygen species as a byproduct of normal cell metabolism. Reactive oxygen species, or free radicals, are responsible for stochastically damaging cell architecture, including proteins and lipids, which leads to cellular apoptosis and hence muscle disuse atrophy (Kondo et al, 1993a;Kondo et al, 1993b;Kondo et al, 1993c;Kondo et al, 1994). The dramatic downregulation of activity in the oxidative muscle may trigger profound changes in the biochemical function of the muscle mitochondria.…”
Section: The Journal Of Experimental Biologymentioning
confidence: 99%
“…The metabolic profiles of oxidative and glycolytic myofibres are inextricably linked to muscle disuse atrophy because oxidative stress is thought to contribute to atrophy in mammalian muscle (Kondo et al, 1991;Kondo et al, 1993;Kondo et al, 1994). Reactive oxygen species (ROS) are a natural by-product of oxidative metabolism, and in a normal metabolic environment there is a balance between the production of ROS and the protective antioxidants that scavenge or deactivate them (Ames et al, 1993).…”
Section: Introductionmentioning
confidence: 99%