The effect of hindlimb immobilization on acid phosphatase, metalloproteinases and nuclear factor-κB in muscles of young and old rats

Bar-Shai, Marina; Carmeli, Eli; Coleman, Raymond; Rozen, Nimrod; Perek, Shoshan; Fuchs, Dror; Reznick, Abraham Z.

doi:10.1016/j.mad.2004.08.030

Cited by 43 publications

(36 citation statements)

References 22 publications

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“…Compared to controls, the activity of classical p65/p50 dimer of NF-κB in quadriceps muscles was down-regulated during the first two weeks of limb immobilization [99]. However, in the third week the activity of p65/p50 returned to the basal levels of the control muscles, while after the fourth week, there was a significant increase in p65/p50 activity [99]. In another study, Cuthbertson et al [100] reported decreased anabolic response in skeletal muscle of healthy older men compared to young after ingesting different amounts of essential amino acids.…”

Section: Agingmentioning

confidence: 72%

Section: Agingmentioning

confidence: 99%

“…Bar-Shai et al [99] studied the kinetics of activation of NF-κB in 24-months old rats in response to four weeks of immobilization by external fixation. Compared to controls, the activity of classical p65/p50 dimer of NF-κB in quadriceps muscles was down-regulated during the first two weeks of limb immobilization [99]. However, in the third week the activity of p65/p50 returned to the basal levels of the control muscles, while after the fourth week, there was a significant increase in p65/p50 activity [99].…”

Section: Agingmentioning

confidence: 99%

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Nuclear factor-kappa B signaling in skeletal muscle atrophy

2008

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Skeletal muscle atrophy/wasting is a serious complication of a wide range of diseases and conditions such as aging, disuse, AIDS, chronic obstructive pulmonary disease, space travel, muscular dystrophy, chronic heart failure, sepsis, and cancer. Emerging evidence suggests that nuclear factor-kappa B (NF-κB) is one of most important signaling pathways linked to the loss of skeletal muscle mass in various physiological and pathophysiological conditions. Activation of NF-κB in skeletal muscle leads to degradation of specific muscle proteins, induces inflammation and fibrosis, and blocks the regeneration of myofibers after injury/atrophy. Recent studies employing genetic mouse models have provided strong evidence that NF-κB can serve as an important molecular target for the prevention of skeletal muscle loss. In this article, we have outlined the current understanding regarding the role of NF-κB in skeletal muscle with particular reference to different models of muscle-wasting and the development of novel therapy.

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Section: Agingmentioning

confidence: 72%

Section: Agingmentioning

confidence: 99%

Section: Agingmentioning

confidence: 99%

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Nuclear factor-kappa B signaling in skeletal muscle atrophy

2008

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“…This correlates well with previous data showing that skeletal muscle immobilization due to external fixation has a biphasic effect on NF‐kB activation with initial decrease in activity at early stages and subsequent increase at the later stages (Bar‐Shai et al. 2005). It was previously suggested that decreased muscle atrophy mediated by genetic inhibition of NF‐ κ B signaling proteins can be attributed to the effects unrelated to the NF‐ κ B transcription factors (Jackman et al.…”

Section: Discussionmentioning

confidence: 99%

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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“…1 Recent studies suggest that matrix metalloproteinase-2 (MMP-2) plays a key role in the response of muscle tissue to various forms of injury and disuse. [2][3][4][5] However, the mechanisms of MMP-2 regulation associated with muscle atrophy remain undefined.…”

Section: Introductionmentioning

confidence: 99%

Matrix metalloproteinase‐2 expression and promoter/enhancer activity in skeletal muscle atrophy

Skittone

Liu

Tseng

et al. 2007

Journal Orthopaedic Research

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Matrix metalloproteinase-2 (MMP-2) appears to be the dominant MMP activated during skeletal muscle atrophy. However, little is known about cell-specific regulatory mechanisms of MMP-2 transcription in vivo. In this study, we used a mouse model of muscle atrophy induced by complete Achilles tendon transection. Time-dependent muscle weight loss, nuclei density reduction, and extracellular matrix degeneration were observed consistently after Achilles tendon transection. Increased MMP-2 expression was confirmed at the mRNA and protein level. Experiments using transgenic mice with a MMP-2 promoter/enhancer reporter construct demonstrated markedly increased MMP-2 promoter/enhancer activity in atrophic skeletal muscle. Tissue-specific upregulation of MMP-2 promoter activity was observed not only in myocytes, but also in blood vessels, nerve, and fascia. The transcription factors c-Jun and FosB were expressed at high levels in atrophic muscle, suggesting a role in MMP-2 upregulation. These findings show that increased MMP-2 activity in disused atrophic muscle and supporting tissues is regulated, at least in part, by increased MMP-2 promoter/enhancer activity. ß

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The effect of hindlimb immobilization on acid phosphatase, metalloproteinases and nuclear factor-κB in muscles of young and old rats

Cited by 43 publications

References 22 publications

Nuclear factor-kappa B signaling in skeletal muscle atrophy

Nuclear factor-kappa B signaling in skeletal muscle atrophy

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

Matrix metalloproteinase‐2 expression and promoter/enhancer activity in skeletal muscle atrophy

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