Involvement of MicroRNAs in the Regulation of Muscle Wasting during Catabolic Conditions

Soares, Ricardo; Cagnin, Stefano; Chemello, Francesco; Silvestrin, Matteo; Musarò, Antonio; Pittà, Cristiano De; Lanfranchi, Gerolamo; Sandri, Marco

doi:10.1074/jbc.m114.561845

Cited by 137 publications

(162 citation statements)

References 64 publications

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“…Based on the recent data by Soares et al . (2014), we hypothesize that microRNA‐143 function, as well as Igfbp5 regulation, is context dependent; specifically, miR‐143:Igfbp5 interactions in the satellite cells during aging are likely to be among the key interactions regulating the balance between cell viability and senescence during aging, whereas in other scenarios, such as diabetes or cachexia, Igfbp5 genes may be regulated by a different set of microRNAs.…”

Section: Discussionmentioning

confidence: 99%

Age‐related changes in miR‐143‐3p:Igfbp5 interactions affect muscle regeneration

et al. 2016

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SummaryA common characteristic of aging is defective regeneration of skeletal muscle. The molecular pathways underlying age‐related decline in muscle regenerative potential remain elusive. microRNAs are novel gene regulators controlling development and homeostasis and the regeneration of most tissues, including skeletal muscle. Here, we use satellite cells and primary myoblasts from mice and humans and an in vitro regeneration model, to show that disrupted expression of microRNA‐143‐3p and its target gene, Igfbp5, plays an important role in muscle regeneration in vitro. We identified miR‐143 as a regulator of the insulin growth factor‐binding protein 5 (Igfbp5) in primary myoblasts and show that the expression of miR‐143 and its target gene is disrupted in satellite cells from old mice. Moreover, we show that downregulation of miR‐143 during aging may act as a compensatory mechanism aiming at improving myogenesis efficiency; however, concomitant upregulation of miR‐143 target gene, Igfbp5, is associated with increased cell senescence, thus affecting myogenesis. Our data demonstrate that dysregulation of miR‐143‐3p:Igfbp5 interactions in satellite cells with age may be responsible for age‐related changes in satellite cell function.

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Section: Discussionmentioning

confidence: 99%

Age‐related changes in miR‐143‐3p:Igfbp5 interactions affect muscle regeneration

et al. 2016

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“…miR-1 appears to interact with FoxO3a activity through HSP72 during dexamethasone-mediated muscle atrophy (36). miR-206 is upregulated by denervation-induced atrophy in mice skeletal muscle, and inhibition of miR-206 partially protects the atrophy (68). miR-208b (9) and miR-499 (2) can potentially repress the expression of myostatin, a well-known negative regulator of muscle growth (58).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, our data in the study suggested that a posttranscriptional regulation by microRNA (miRNA) might be associated with the activating process of the ubiquitin-proteasome system. The discovery of miRNAs has provided a new aspect that could expand our knowledge to understand the mechanisms of skeletal muscle atrophy (68,77). Therefore, we also aimed to evaluate the possible involvement of these molecules in AMPK-mediated regulation of muscle mass during hindlimb unloading.…”

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confidence: 99%

Involvement of AMPK in regulating slow-twitch muscle atrophy during hindlimb unloading in mice

Egawa

Goto

Ohno

et al. 2015

American Journal of Physiology-Endocrinology and Metabolism

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-AMPK is considered to have a role in regulating skeletal muscle mass. However, there are no studies investigating the function of AMPK in modulating skeletal muscle mass during atrophic conditions. In the present study, we investigated the difference in unloading-associated muscle atrophy and molecular functions in response to 2-wk hindlimb suspension between transgenic mice overexpressing the dominant-negative mutant of AMPK (AMPK-DN) and their wild-type (WT) littermates. Male WT (n ϭ 24) and AMPK-DN (n ϭ 24) mice were randomly divided into two groups: an untreated preexperimental control group (n ϭ 12 in each group) and an unloading (n ϭ 12 in each group) group. The relative soleus muscle weight and fiber cross-sectional area to body weight were decreased by ϳ30% in WT mice by hindlimb unloading and by ϳ20% in AMPK-DN mice. There were no changes in puromycin-labeled protein or Akt/70-kDa ribosomal S6 kinase signaling, the indicators of protein synthesis. The expressions of ubiquitinated proteins and muscle RING finger 1 mRNA and protein, markers of the ubiquitin-proteasome system, were increased by hindlimb unloading in WT mice but not in AMPK-DN mice. The expressions of molecules related to the protein degradation system, phosphorylated forkhead box class O3a, inhibitor of B␣, microRNA (miR)-1, and miR-23a, were decreased only in WT mice in response to hindlimb unloading, and 72-kDa heat shock protein expression was higher in AMPK-DN mice than in WT mice. These results imply that AMPK partially regulates unloading-induced atrophy of slow-twitch muscle possibly through modulation of the protein degradation system, especially the ubiquitin-proteasome system. AMP-activated protein kinase; protein degradation; autophagy; ubiquitin-proteasome; microRNA; heat shock protein SKELETAL MUSCLE IS THE LARGEST TISSUE IN THE BODY, accounting for ϳ40% of the total body mass, and has a crucial role in metabolism as well as locomotion. Skeletal muscle has a high ability to adapt to multiple stimuli. Increased loading, such as resistance training and mechanical stretching, leads to skeletal muscle hypertrophy (18,75). In contrast, aging, poor nutrition, several diseases such as diabetes, cancer, sepsis, and chronic renal failure, and decreased loading, such as inactivity, lead to skeletal muscle atrophy (23,34,39). Skeletal muscle atrophy occurs as a result of changes in protein turnover: decreased protein synthesis, increased protein degradation, or a combination of both (17). The coordination of protein turnover in the atrophic process is regulated by complicated molecular responses, and the molecular mechanism involved in this process in skeletal muscle is not yet completely understood and remains to be elucidated.5=-AMP-activated protein kinase (AMPK) is well established as a metabolic sensor that helps maintain cellular energy homeostasis by modulating glucose, lipid, and protein metabolism (16,26,28). AMPK is a heterotrimeric kinase comprising a catalytic ␣-subunit and two regulatory subunits, the ␤-and ␥-subunits. Two ...

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“…Of note, some muscle specific miRNAs (also called myomiRs), such as miR 1 and miR 133, were reported to have roles in both cardiac hypertrophy and muscle atrophy 4 . Interestingly, miR 21, which critically con tributes to cardiac fibrosis, has been shown to promote muscle wasting 5,6 . Moreover, miR 23a, which contributes to cardiac hyper trophy, was found to protect against muscle atrophy by targeting E3 ubiquitin protein ligase TRIM63 (also known as MURF1) 7,8 .…”

mentioning

confidence: 99%

MicroRNAs in muscle wasting and cachexia induced by heart failure

Bei

Xiao

2017

Nat Rev Cardiol

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Involvement of MicroRNAs in the Regulation of Muscle Wasting during Catabolic Conditions

Cited by 137 publications

References 64 publications

Age‐related changes in miR‐143‐3p:Igfbp5 interactions affect muscle regeneration

Age‐related changes in miR‐143‐3p:Igfbp5 interactions affect muscle regeneration

Involvement of AMPK in regulating slow-twitch muscle atrophy during hindlimb unloading in mice

MicroRNAs in muscle wasting and cachexia induced by heart failure

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