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• W2766656449 abstract "The ubiquitin-proteasome system (UPS)-dependent proteolysis plays a major role in the muscle catabolic action of glucocorticoids (GCs). Atrogin-1 and muscle-specific RING finger protein 1 (MuRF1), two E3 ubiquitin ligases, are uniquely expressed in muscle. It has been previously demonstrated that GC treatment induced MuRF1 and atrogin-1 overexpression. However, it is yet unclear whether the higher pharmacological dose of GCs induced muscle protein catabolism through MuRF1 and atrogin-1. In the present study, the role of atrogin-1 and MuRF1 in C2C12 cells protein metabolism during excessive dexamethasone (DEX) was studied. The involvement of Akt/forkhead box O1 (FoXO1) signaling pathway and the cross-talk between anabolic regulator mammalian target of rapamycin (mTOR) and catabolic regulator FoXO1 were investigated. High concentration of DEX increased MuRF1 protein level in a time-dependent fashion (P&lt;0.05), while had no detectable effect on atrogin-1 protein (P&gt;0.05). FoXO1/3a (Thr24/32) phosphorylation was enhanced (P&lt;0.05), mTOR phosphorylation was suppressed (P&lt;0.05), while Akt protein expression was not affected (P&gt;0.05) by DEX. RU486 treatment inhibited the DEX-induced increase of FoXO1/3a phosphorylation (P&lt;0.05) and MuRF1 protein; LY294002 (LY) did not restore the stimulative effect of DEX on the FoXO1/3a phosphorylation (P&gt;0.05), but inhibited the activation of MuRF1 protein induced by DEX (P&lt;0.05); rapamycin (RAPA) inhibited the stimulative effect of DEX on the FoXO1/3a phosphorylation and MuRF1 protein (P&lt;0.05)." @default.
• W2766656449 created "2017-11-10" @default.
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• W2766656449 date "2017-11-17" @default.
• W2766656449 modified "2023-09-23" @default.
• W2766656449 title "Excessive glucocorticoid-induced muscle MuRF1 overexpression is independent of Akt/FoXO1 pathway" @default.
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• W2766656449 doi "https://doi.org/10.1042/bsr20171056" @default.
• W2766656449 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5691142" @default.
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