dc.contributor.author |
Zeng, Nina |
en |
dc.contributor.author |
D'Souza, Randall |
en |
dc.contributor.author |
Figueiredo, Vandre C |
en |
dc.contributor.author |
Markworth, James F |
en |
dc.contributor.author |
Roberts, Llion A |
en |
dc.contributor.author |
Peake, Jonathan M |
en |
dc.contributor.author |
Mitchell, Cameron |
en |
dc.contributor.author |
Cameron-Smith, David |
en |
dc.date.accessioned |
2018-12-03T01:24:22Z |
en |
dc.date.issued |
2017-12 |
en |
dc.identifier.citation |
Physiological reports 5(24) Dec 2017 |
en |
dc.identifier.issn |
2051-817X |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/44776 |
en |
dc.description.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 p62Ser403 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. |
en |
dc.format.medium |
Print |
en |
dc.language |
eng |
en |
dc.relation.ispartofseries |
Physiological reports |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
en |
dc.subject |
Muscle, Skeletal |
en |
dc.subject |
Humans |
en |
dc.subject |
Nuclear Proteins |
en |
dc.subject |
Protein Processing, Post-Translational |
en |
dc.subject |
Phosphorylation |
en |
dc.subject |
Male |
en |
dc.subject |
Resistance Training |
en |
dc.subject |
Young Adult |
en |
dc.subject |
Sequestosome-1 Protein |
en |
dc.title |
Acute resistance exercise induces Sestrin2 phosphorylation and p62 dephosphorylation in human skeletal muscle. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.14814/phy2.13526 |
en |
pubs.issue |
24 |
en |
pubs.volume |
5 |
en |
dc.rights.holder |
Copyright: The authors |
en |
dc.identifier.pmid |
29263116 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
research-article |
en |
pubs.subtype |
Journal Article |
en |
pubs.elements-id |
719557 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Nutrition |
en |
pubs.org-id |
Pharmacology |
en |
dc.identifier.eissn |
2051-817X |
en |
pubs.record-created-at-source-date |
2017-12-22 |
en |
pubs.dimensions-id |
29263116 |
en |