Evidence map›Paper›PMID 26048236›Full record

ArticleDiabetologia2015

Markers of autophagy are adapted to hyperglycaemia in skeletal muscle in type 2 diabetes.

Rikke Kruse, Birgitte F Vind, Stine J Petersson, Jonas M Kristensen, Kurt Højlund

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Article in Diabetologia, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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.

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3 · Its place in the literature

Who cites it

32 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Rikke KruseThe Section of Molecular Diabetes & Metabolism, Institute of Clinical Research and Institute of Molecular Medicine, University of Southern Denmark, Odense, Denmark.
Birgitte F Vind
Stine J Petersson
Jonas M Kristensen
Kurt Højlund

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aims/hypothesisAutophagy is a catabolic process that maintains cellular homeostasis by degradation of protein aggregates and selective removal of damaged organelles, e.g. mitochondria (mitophagy). Insulin resistance in skeletal muscle has been linked to mitochondrial dysfunction and altered protein metabolism. Here, we investigated whether abnormalities in autophagy are present in human muscle in obesity and type 2 diabetes.

methodsUsing a case-control design, skeletal muscle biopsies obtained in the basal and insulin-stimulated states from patients with type 2 diabetes during both euglycaemia and hyperglycaemia, and from glucose-tolerant lean and obese individuals during euglycaemia, were used for analysis of mRNA levels, protein abundance and phosphorylation of autophagy-related proteins.

resultsMuscle transcript levels of autophagy-related genes (ULK1, BECN1, PIK3C3, ATG5, ATG7, ATG12, GABARAPL1, MAP1LC3B, SQSTM1, TP53INP2 and FOXO3A [also known as FOXO3]), including some specific for mitophagy (BNIP3, BNIP3L and MUL1), and protein abundance of autophagy-related gene (ATG)7 and Bcl-2/adenovirus E1B 19-kDa-interacting protein 3 (BNIP3), as well as content and phosphorylation of forkhead box O3A (FOXO3A) were similar among the groups. Insulin reduced lipidation of microtubule-associated protein light chain 3 (LC3)B-I to LC3B-II, a marker of autophagosome formation, with no effect on p62/sequestosome 1 (SQSTM1) content in muscle of lean and obese individuals. In diabetic patients, insulin action on LC3B was absent and p62/SQSTM1 content increased when studied under euglycaemia, whereas the responses of LC3B and p62/SQSTM1 to insulin were normalised during hyperglycaemia. CONCLUSIONS/

interpretationOur results demonstrate that the levels of autophagy-related genes and proteins in muscle are normal in obesity and type 2 diabetes. This suggests that muscle autophagy in type 2 diabetes has adapted to hyperglycaemia, which may contribute to preserve muscle mass.

Indexed as

AutophagyApoptosis Regulatory ProteinsBiopsyCase-Control StudiesDiabetes Mellitus, Type 2FemaleForkhead Box Protein O3Forkhead Transcription FactorsGlucose Clamp TechniqueGlucose Tolerance TestHomeostasisHumansHyperglycemiaInsulin ResistanceMaleMicrotubule-Associated ProteinsApoptosis Regulatory ProteinsForkhead Box Protein O3Forkhead Transcription FactorsFOXO3 protein, humanMicrotubule-Associated ProteinsMTOR protein, humanRNA, MessengerTOR Serine-Threonine Kinases

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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.