|Title:||Involvement of AMPK in regulating slow-twitch muscle atrophy during hindlimb unloading in mice|
|Authors:||Egawa, Tatsuro https://orcid.org/0000-0001-9363-1589 (unconfirmed)|
Hayashi, Tatsuya https://orcid.org/0000-0001-7600-4735 (unconfirmed)
|Author's alias:||江川, 達郎|
|Keywords:||AMP-activated protein kinase|
heat shock protein
|Publisher:||American Physiological Society|
|Journal title:||American Journal of Physiology - Endocrinology And Metabolism|
|Abstract:||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 = 24) and AMPK-DN (n = 24) mice were randomly divided into two groups: an untreated preexperimental control group (n = 12 in each group) and an unloading (n = 12 in each group) group. The relative soleus muscle weight and fiber cross-sectional area to body weight were decreased by ∼30% in WT mice by hindlimb unloading and by ∼20% 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 κBα, 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.|
|Rights:||© 2015 the American Physiological Society.|
This is the accepted version of the article, which has been published in final form at http://doi.org/10.1152/ajpendo.00165.2015
This is not the published version. Please cite only the published version.
|Appears in Collections:||Journal Articles|
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