Evidence map›Paper›PMID 29574525›Full record

ArticleEuropean journal of applied physiology2018

The putative leucine sensor Sestrin2 is hyperphosphorylated by acute resistance exercise but not protein ingestion in human skeletal muscle.

Nina Zeng, Randall F D'Souza, Brie Sorrenson, Troy L Merry, Matthew P G Barnett, Cameron J Mitchell, David Cameron-Smith

Abstract read
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In one paragraph

Article in European journal of applied physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. Sestrins in Physiological Stress Responses.Annual review of physiology · 2021
    Review
  6. Review
  7. Article
  8. Review
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Nina ZengLiggins Institute, The University of Auckland, Private Bag 92 019, Victoria Street West, Auckland, 1142, New Zealand.
Randall F D'SouzaLiggins Institute, The University of Auckland, Private Bag 92 019, Victoria Street West, Auckland, 1142, New Zealand.
Brie SorrensonDepartment of Molecular Medicine and Pathology, Faculty of Medical and Health Sciences, The University of Auckland, Auckland, New Zealand.
Troy L MerryMaurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand.
Matthew P G BarnettFood Nutrition and Health Team, AgResearch, Palmerston North, 4474, New Zealand.
Cameron J MitchellLiggins Institute, The University of Auckland, Private Bag 92 019, Victoria Street West, Auckland, 1142, New Zealand.
David Cameron-SmithLiggins Institute, The University of Auckland, Private Bag 92 019, Victoria Street West, Auckland, 1142, New Zealand. d.cameron-smith@auckland.ac.nz.
University of Auckland · NZAgResearch · NZMaurice Wilkins Centre · NZ

Funding

AgResearch A19079 and A21246
6 · The paper itself

Abstract

purposeDietary protein and resistance exercise (RE) are both potent stimuli of the mammalian target of rapamycin complex 1 (mTORC1). Sestrins1, 2, 3 are multifunctional proteins that regulate mTORC1, stimulate autophagy and alleviate oxidative stress. Of this family, Sestrin2 is a putative leucine sensor implicated in mTORC1 and AMP-dependent protein kinase (AMPK) regulation. There is currently no data examining the responsiveness of Sestrin2 to dietary protein ingestion, with or without RE.

methodsIn Study 1, 16 males ingested either 10 or 20 g of milk protein concentrate (MPC) with muscle biopsies collected pre, 90 and 210 min post-beverage consumption. In Study 2, 20 males performed a bout of RE immediately followed by the consumption of 9 g of MPC or carbohydrate placebo. Analysis of Sestrins, AMPK and antioxidant responses was examined.

resultsDietary protein ingestion did not result in Sestrin2 mobility shift. After RE, Sestrin2 phosphorylation state was significantly altered and was not further modified by post-exercise protein or carbohydrate ingestion. With RE, AMPK phosphorylation remained stable, while the mRNA expressions of several antioxidants were upregulated.

conclusionsDietary protein ingestion did not affect the signalling by the family of Sestrins. With RE, Sestrin2 was hyperphosphorylated, with no further evidence of a relationship to AMPK signalling.

Indexed as

Protein Processing, Post-TranslationalResistance TrainingAMP-Activated Protein Kinase KinasesDietary ProteinsEatingHumansMaleMiddle AgedMuscle, SkeletalNuclear ProteinsPhosphorylationProtein KinasesSestrinsAMP-Activated Protein Kinase KinasesDietary ProteinsNuclear ProteinsProtein KinasesSESN2 protein, humanSestrinsAmino acidAntioxidantHyperphosphorylationMammalian target of rapamycinOxidative stressResistance exerciseSestrins

Identifiers

PMID29574525
OpenAlexW2789993394

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.