Acute resistance exercise induces sestrin2 phosphorylation and p62 dephosphorylation in human skeletal muscle

Zeng, Nina, D’Souza, Randall F., Figueiredo, Vandre C., Markworth, James F., Roberts, Llion A., Peake, Jonathan M., Mitchell, Cameron J. and Cameron-Smith, David (2017) Acute resistance exercise induces sestrin2 phosphorylation and p62 dephosphorylation in human skeletal muscle. Physiological Reports, 5 24: . doi:10.14814/phy2.13526


Author Zeng, Nina
D’Souza, Randall F.
Figueiredo, Vandre C.
Markworth, James F.
Roberts, Llion A.
Peake, Jonathan M.
Mitchell, Cameron J.
Cameron-Smith, David
Title Acute resistance exercise induces sestrin2 phosphorylation and p62 dephosphorylation in human skeletal muscle
Journal name Physiological Reports   Check publisher's open access policy
ISSN 2051-817X
Publication date 2017-12-01
Sub-type Article (original research)
DOI 10.14814/phy2.13526
Open Access Status DOI
Volume 5
Issue 24
Publisher American Physiological Society
Language eng
Subject 1314 Physiology
2737 Physiology (medical)
Abstract Sestrins (1, 2, 3) are a family of stress-inducible proteins capable of attenuating oxidative stress, regulating metabolism, and stimulating autophagy. Sequestosome1 (p62) is also a stress-inducible multifunctional protein acting as a signaling hub for oxidative stress and selective autophagy. It is unclear whether Sestrin and p62Ser403 are regulated acutely or chronically by resistance exercise (RE) or training (RT) in human skeletal muscle. Therefore, the acute and chronic effects of RE on Sestrin and p62 in human skeletal muscle were examined through two studies. In Study 1, nine active men (22.1 ± 2.2 years) performed a bout of single-leg strength exercises and muscle biopsies were collected before, 2, 24, and 48 h after exercise. In Study 2, 10 active men (21.3 ± 1.9 years) strength trained for 12 weeks (2 days per week) and biopsies were collected pre- and post-training. Acutely, 2 h postexercise, phosphorylation of p62 was downregulated, while there was a mobility shift of Sestrin2, indicative of increased phosphorylation. Forty-eight hours postexercise, the protein expression of both Sestrin1 and total p62 increased. Chronic exercise had no impact on the gene or protein expression of Sestrin2/3 or p62, but Sestrin1 protein was upregulated. These findings demonstrated an inverse relationship between Sestrin2 and p62 phosphorylation after a single bout of RE, indicating they are transiently regulated. Contrarily, 12 weeks of RT increased protein expression of Sestrin1, suggesting that despite the strong sequence homology of the Sestrin family, they are differentially regulated in response to acute RE and chronic RT.
Keyword Exercise training
p62
Resistance exercise
Sequestosome 1
Sestrin
Skeletal muscle
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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Created: Mon, 01 Jan 2018, 01:26:03 EST