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• W1990872004 abstract "Purpose of review Regulation of muscle size is essential for proper development and homeostasis of adult musculature. This regulation is mediated in large part by signal transduction pathways that promote the synthesis or breakdown of skeletal muscle. PI(3)K/Akt, myostatin and NF-κB represent three such pathways that will be the focus of this review. Recent findings Recent reports solidify the requirement of the PI(3)K/Akt pathway in the regulation of muscle hypertrophy. In response to IGF-1, Akt activates downstream effectors, mTOR and p70S6K to stimulate protein synthesis thereby increasing the cytoplasmic compartment in muscle fibers. Tsc2 was also identified as a novel Akt target, whose phosphorylation and inactivation by Akt may lead to an increase in cell size. The mechanisms by which myostatin functions in muscle wasting was recently explored using in-vitro assays of myogenesis. Myostatin was found to repress myogenesis by inhibiting the synthesis and activity of MyoD. Paradoxically, myostatin expression is itself regulated by MyoD binding to the myostatin promoter. The NF-κB transcription factor also functions as a negative regulator of myogenesis by inhibiting MyoD. Chronic activation of NF-κB has been associated with muscle wasting, but the mechanisms by which this regulation occurs remain for the most part unknown. Summary Recent cell culture and animal studies have provided insight on the mechanisms by which Akt, myostatin, and NF-κB signaling pathways regulate muscle size. Clinical intervention to boost Akt signaling or modulate myostatin and NF-κB activities may prove useful in diseases associated with chronic muscle wasting." @default.
• W1990872004 created "2016-06-24" @default.
• W1990872004 creator A5088452270 @default.
• W1990872004 date "2004-07-01" @default.
• W1990872004 modified "2023-10-11" @default.
• W1990872004 title "Signaling pathways weigh in on decisions to make or break skeletal muscle" @default.
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• W1990872004 doi "https://doi.org/10.1097/01.mco.0000134364.61406.26" @default.
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