Calpain-dependent regulation of the skeletal muscle atrophy following unloading

Шенкман, Борис; Belova, Svetlana P.; Lomonosova, Yulia; Kostrominova, Tatiana Y.; Nemirovskaya, T. L.

doi:10.1016/j.abb.2015.07.011

Cited by 55 publications

(47 citation statements)

References 38 publications

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“…This correlates well with our data on muscle atrophy in unloaded soleus muscle (Shenkman et al. 2015). A similar decrease in the I κ B α level of expression was reported previously after 3 and 7 days of unloading in the rat model (Judge et al.…”

Section: Discussionmentioning

confidence: 99%

“…Similar opposing changes in the level of FoxO and the expression of E3 ubiquitin ligases were previously observed during muscle unloading (Shenkman et al. 2015). In addition to FoxO several other transcription factors can influence expression of E3 ubiquitin ligases (Bodine and Baehr 2014).…”

Section: Discussionmentioning

confidence: 99%

“…2014; Shenkman et al. 2015). At the same time, changes in expression of Bcl‐3 at the early stages of unloading were not reported and role of Bcl‐3 in the expression of E3 ligases during first 3 days of unloading was not clear.…”

Section: Discussionmentioning

confidence: 99%

“…Similar injection protocol was used in our previous publication (Shenkman et al. 2015). Visual inspection of the dissected soleus muscle showed no obvious signs of damage from the injection.…”

Section: Methodsmentioning

confidence: 99%

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Paradoxical effect of IKKβ inhibition on the expression of E3 ubiquitin ligases and unloading-induced skeletal muscle atrophy

et al. 2017

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We tested whether NF‐κB pathway is indispensable for the increase in expression of E3‐ligases and unloading‐induced muscle atrophy using IKKβ inhibitor IMD‐0354. Three groups of rats were used: nontreated control (C), 3 days of unloading/hindlimb suspension with (HS+IMD) or without (HS) IMD‐0354. Levels of IκBα were higher in HS+IMD (1.16‐fold) and lower in HS (0.82‐fold) when compared with C group. IMD‐0354 treatment during unloading: had no effect on loss of muscle mass; increased mRNA levels of MuRF1 and MAFbx; increased level of pFoxO3; and had no effect on levels of Bcl‐3, p105, and p50 proteins. Our study for the first time showed that inhibiting IKK β in vivo during 3‐day unloading failed to diminish expression of ubiquitin ligases and prevent muscle atrophy.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Paradoxical effect of IKKβ inhibition on the expression of E3 ubiquitin ligases and unloading-induced skeletal muscle atrophy

et al. 2017

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“…The breakdown of sarcomeric proteins releases actin and myosin, which in turn are degraded by the ubiquitin proteasome system (UPS). In skeletal muscle, recent studies demonstrated that both calpains and caspase-3 were activated by hindlimb unloading [59,95,96]. Interestingly, pharmacological inhibition of calpains or caspase-3 prevents type I fibers atrophy observed in casted rats, demonstrating that these proteases are mandatory for skeletal muscle atrophy [89].…”

Section: Cellular Mechanisms Involved In Immobilization-induced Skelementioning

confidence: 99%

From physical inactivity to immobilization: Dissecting the role of oxidative stress in skeletal muscle insulin resistance and atrophy

Pierre

Appriou

Gratas-Delamarche

et al. 2016

Free Radical Biology and Medicine

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In the literature, the terms physical inactivity and immobilization are largely used as synonyms. The present review emphasizes the need to establish a clear distinction between these two situations. Physical inactivity is a behavior characterized by a lack of physical activity, whereas immobilization is a deprivation of movement for medical purpose. In agreement with these definitions, appropriate models exist to study either physical inactivity or immobilization, leading thereby to distinct conclusions. In this review, we examine the involvement of oxidative stress in skeletal muscle insulin resistance and atrophy induced by, respectively, physical inactivity and immobilization. A large body of evidence demonstrates that immobilization-induced atrophy depends on the chronic overproduction of reactive oxygen and nitrogen species (RONS). On the other hand, the involvement of RONS in physical inactivity-induced insulin resistance has not been investigated. This observation outlines the need to elucidate the mechanism by which physical inactivity promotes insulin resistance.

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The Role of Exercise and TFAM in Preventing Skeletal Muscle Atrophy

Theilen

Kunkel

Tyagi

2017

Journal Cellular Physiology

111

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Skeletal muscle atrophy is the consequence of protein degradation exceeding protein synthesis. This arises for a multitude of reasons including the unloading of muscle during microgravity, post-surgery bedrest, immobilization of a limb after injury, and overall disuse of the musculature. The development of therapies prior to skeletal muscle atrophy settings to diminish protein degradation is scarce. Mitochondrial dysfunction is associated with skeletal muscle atrophy and contributes to the induction of protein degradation and cell apoptosis through increased levels of ROS observed with the loss of organelle function. ROS binds mtDNA, leading to its degradation and decreasing functionality. Mitochondrial transcription factor A (TFAM) will bind and coat mtDNA, protecting it from ROS and degradation while increasing mitochondrial function. Exercise stimulates cell signaling pathways that converge on and increase PGC-1α, a well-known activator of the transcription of TFAM and mitochondrial biogenesis. Therefore, in the present review we are proposing, separately, exercise and TFAM treatments prior to atrophic settings (muscle unloading or disuse) alleviate skeletal muscle atrophy through enhanced mitochondrial adaptations and function. Additionally, we hypothesize the combination of exercise and TFAM leads to a synergistic effect in targeting mitochondrial function to prevent skeletal muscle atrophy.

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Calpain-dependent regulation of the skeletal muscle atrophy following unloading

Cited by 55 publications

References 38 publications

Paradoxical effect of IKKβ inhibition on the expression of E3 ubiquitin ligases and unloading-induced skeletal muscle atrophy

Paradoxical effect of IKKβ inhibition on the expression of E3 ubiquitin ligases and unloading-induced skeletal muscle atrophy

From physical inactivity to immobilization: Dissecting the role of oxidative stress in skeletal muscle insulin resistance and atrophy

The Role of Exercise and TFAM in Preventing Skeletal Muscle Atrophy

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