Participation of AMPK in the Control of Skeletal Muscle Mass

Egawa, Tatsuro

doi:10.1007/978-981-10-3292-9_12

Cited by 1 publication

(4 citation statements)

References 173 publications

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“…37 The AMPK-stimulated protein degradation in skeletal muscle can also be mediated by activation of NF-κB-regulated MuRF1/Atrogin-1 signalling pathway. 38 In the present study, our results showed that low-dose TBT effectively induced myostatin protein expression in C2C12 myoblasts during myogenic differentiation and differentiated C2C12 myotubes and mouse muscles. The increased protein expression of phosphorylated AMPKα and phosphorylated NF-κB-p65 and the decreased protein expression of phosphorylated FoxO1 were also observed in myotubes and mouse soleus muscles in the presence of TBT.…”

Section: Discussionsupporting

confidence: 64%

“…The pharmacological or genetic inhibition of NF‐κB has been shown to effectively prevent the denervation‐ or tumour‐induced muscle atrophy 37 . The AMPK‐stimulated protein degradation in skeletal muscle can also be mediated by activation of NF‐κB‐regulated MuRF1/Atrogin‐1 signalling pathway 38 . In the present study, our results showed that low‐dose TBT effectively induced myostatin protein expression in C2C12 myoblasts during myogenic differentiation and differentiated C2C12 myotubes and mouse muscles.…”

Section: Discussionsupporting

confidence: 58%

“…Myostatin protein expression could also be increased by AMPK activator AICAR in L6 myoblasts‐derived myotubes 36 . Moreover, NF‐κB is a transcription factor that can also be detected in skeletal muscles under physiological and pathological atrophic conditions, such as diabetes, ageing, denervation, unloading, and sepsis 37,38 . The pharmacological or genetic inhibition of NF‐κB has been shown to effectively prevent the denervation‐ or tumour‐induced muscle atrophy 37 .…”

Section: Discussionmentioning

confidence: 99%

“… 36 Moreover, NF‐κB is a transcription factor that can also be detected in skeletal muscles under physiological and pathological atrophic conditions, such as diabetes, ageing, denervation, unloading, and sepsis. 37 , 38 The pharmacological or genetic inhibition of NF‐κB has been shown to effectively prevent the denervation‐ or tumour‐induced muscle atrophy. 37 The AMPK‐stimulated protein degradation in skeletal muscle can also be mediated by activation of NF‐κB‐regulated MuRF1/Atrogin‐1 signalling pathway.…”

Section: Discussionmentioning

confidence: 99%

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A ubiquitous endocrine disruptor tributyltin induces muscle wasting and retards muscle regeneration

Chiu

Yang

Weng

et al. 2022

J cachexia sarcopenia muscle

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Background Organotin pollutant tributyltin (TBT) is an environmental endocrine disrupting chemical and is a known obesogen and diabetogen. TBT can be detected in human following consumption of contaminated seafood or water. The decrease in muscle strength and quality has been shown to be associated with type 2 diabetes in older adults. However, the adverse effects of TBT on the muscle mass and function still remain unclear. Here, we investigated the effects and molecule mechanisms of low‐dose TBT on skeletal muscle regeneration and atrophy/wasting using the cultured skeletal muscle cell and adult mouse models. Methods The mouse myoblasts (C2C12) and differentiated myotubes were used to assess the in vitro effects of low‐dose tributyltin (0.01–0.5 μM). The in vivo effects of TBT at the doses of 5 and 25 μg/kg/day (n = 6/group), which were five times lower than the established no observed adverse effect level (NOAEL) and equal to NOAEL, respectively, by oral administration for 4 weeks on muscle wasting and muscle regeneration were evaluated in a mouse model with or without glycerol‐induced muscle injury/regeneration. Results TBT reduced myogenic differentiation in myoblasts (myotube with 6–10 nuclei: 53.9 and 35.8% control for 0.05 and 0.1 μM, respectively, n = 4, P < 0.05). TBT also decreased myotube diameter, upregulated protein expression levels of muscle‐specific ubiquitin ligases (Atrogin‐1 and MuRF1), myostatin, phosphorylated AMPKα, and phosphorylated NFκB‐p65, and downregulated protein expression levels of phosphorylated AKT and phosphorylated FoxO1 in myotubes (0.2 and 0.5 μM, n = 6, P < 0.05). Exposure of TBT in mice elevated body weight, decreased muscle mass, and induced muscular dysfunction (5 and 25 μg/kg, P > 0.05 and P < 0.05, respectively, n = 6). TBT inhibited soleus muscle regeneration in mice with glycerol‐induced muscle injury (5 and 25 μg/kg, P > 0.05 and P < 0.05, respectively, n = 6). TBT upregulated protein expression levels of Atrogin‐1, MuRF1, myostatin, and phosphorylated AMPKα and downregulated protein expression level of phosphorylated FoxO1 in the mouse soleus muscles (5 and 25 μg/kg, P > 0.05 and P < 0.05, respectively, n = 6). Conclusions This study demonstrates for the first time that low‐dose TBT significantly inhibits myogenic differentiation and triggers myotube atrophy in a cell model and significantly decreases muscle regeneration and muscle mass and function in a mouse model. These findings suggest that low‐dose TBT exposure may be an environmental risk factor for muscle regeneration inhibition, atrophy/wasting, and disease‐related myopathy.

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Section: Discussionsupporting

confidence: 64%

Section: Discussionsupporting

confidence: 58%