Evidence map›Paper›PMID 26298291›Full record

ReviewCellular and molecular life sciences : CMLS2015

HIF-1-driven skeletal muscle adaptations to chronic hypoxia: molecular insights into muscle physiology.

F B Favier, F A Britto, D G Freyssenet, X A Bigard, H Benoit

Open access · bronzeAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

69 citing papers in PubMed, 114 citations in OpenAlex.

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  18. The Crucial Role of Exercise in Promoting Adolescent Muscle Development.Advances in experimental medicine and biology · 2026
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9 more citing papers are in PubMed but not listed here.

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

5 authors at 5 institutions in 2 countries.

F B FavierINRA, UMR 866 Dynamique Musculaire et Métabolisme, 34060, Montpellier, France. favier@supagro.inra.fr.
F A BrittoINRA, UMR 866 Dynamique Musculaire et Métabolisme, 34060, Montpellier, France.
D G FreyssenetLaboratoire de Physiologie de l'Exercice EA 4338, Université de Lyon, Université Jean Monnet, 42000, Saint Etienne, France.
X A BigardAgence Française de Lutte contre le Dopage, 75007, Paris, France.
H BenoitINSERM, U1042 Hypoxie Physio-Pathologie, 38000, Grenoble, France.
Agence française de lutte contre le dopage · FRDynamique Musculaire et MétabolismeInstitut National de la Recherche Agronomique · MAUniversité Claude Bernard Lyon 1 · FRUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skeletal muscle is a metabolically active tissue and the major body protein reservoir. Drop in ambient oxygen pressure likely results in a decrease in muscle cells oxygenation, reactive oxygen species (ROS) overproduction and stabilization of the oxygen-sensitive hypoxia-inducible factor (HIF)-1α. However, skeletal muscle seems to be quite resistant to hypoxia compared to other organs, probably because it is accustomed to hypoxic episodes during physical exercise. Few studies have observed HIF-1α accumulation in skeletal muscle during ambient hypoxia probably because of its transient stabilization. Nevertheless, skeletal muscle presents adaptations to hypoxia that fit with HIF-1 activation, although the exact contribution of HIF-2, I kappa B kinase and activating transcription factors, all potentially activated by hypoxia, needs to be determined. Metabolic alterations result in the inhibition of fatty acid oxidation, while activation of anaerobic glycolysis is less evident. Hypoxia causes mitochondrial remodeling and enhanced mitophagy that ultimately lead to a decrease in ROS production, and this acclimatization in turn contributes to HIF-1α destabilization. Likewise, hypoxia has structural consequences with muscle fiber atrophy due to mTOR-dependent inhibition of protein synthesis and transient activation of proteolysis. The decrease in muscle fiber area improves oxygen diffusion into muscle cells, while inhibition of protein synthesis, an ATP-consuming process, and reduction in muscle mass decreases energy demand. Amino acids released from muscle cells may also have protective and metabolic effects. Collectively, these results demonstrate that skeletal muscle copes with the energetic challenge imposed by O2 rarefaction via metabolic optimization.

Indexed as

Models, BiologicalStress, PhysiologicalAnimalsCell HypoxiaHumansHypoxia-Inducible Factor 1, alpha SubunitMetabolic Networks and PathwaysMiceMitochondriaMuscle, SkeletalOxygenRatsReactive Oxygen SpeciesSignal TransductionHypoxia-Inducible Factor 1, alpha SubunitOxygenReactive Oxygen SpeciesAltitudeAtrophyHypoxia inducible factorMetabolismMitochondriaOxidative stress

Identifiers

PMID26298291
PMCPMC11113128
OpenAlexW2118470982

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.