ArticleFrontiers in physiology2013
Effect of HSP25 loss on muscle contractile function and running wheel activity in young and old mice.
Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Chaperone Proteins: The Rising Players in Muscle Atrophy.Journal of cachexia, sarcopenia and muscle · 2025Review
- Skeletal Muscle Heat Shock Protein Content and the Repeated Bout Effect.International journal of molecular sciences · 2024Article
- Preconditioning with whole-body or regional hyperthermia attenuates exercise-induced muscle damage in rodents.Physiological research · 2022Article
- The small heat shock protein HSPB1 protects mice from sepsis.Scientific reports · 2018Article
- The Invalidation of HspB1 Gene in Mouse Alters the Ultrastructural Phenotype of Muscles.PloS one · 2016Article
- The action of pre-exercise low-level laser therapy (LLLT) on the expression of IL-6 and TNF-α proteins and on the functional fitness of elderly rats subjected to aerobic training.Lasers in medical science · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Aging is associated with an adverse decline in muscle function, often manifesting as decreased strength and increased muscle fatigability that negatively affects the overall health of the elderly. Heat shock proteins (HSPs), a family of stress inducible proteins known to protect cells from damage, are highly induced in muscle cells following exercise, but both basal and inducible levels decline with age. Utilizing young and old mice lacking HSP25 (Hsp25(-/-)) we tested the hypothesis that HSP25 is required to maintain normal muscle function and that age related decreases in HSP25 directly contribute to declining muscle function. Running wheel distances over 14 days for young Hsp25(-/-) mice were significantly lower than for the corresponding Hsp25(+/+) genotype (81238 vs. 33956 AUC, respectively). While older groups both ran significantly less than young groups, in aged mice HSP25 loss did not lead to any additional decrease. Significantly lower myofibrillar (contractile) protein levels in young Hsp25(-/-) vs. Hsp25(+/+) (15.7 ± 0.2 vs. 13.4 ± 0.3 mg/mg muscle) mice suggests HSP25 loss was associated with greater muscle breakdown during voluntary wheel running. In vivo, plantarflexor maximal isometric force was significantly decreased in aged vs. young mice, but the loss of HSP25 had no effect on either group. However, plantarflexor fatigability over 10 contractions was significantly higher in young Hsp25(-/-) vs. Hsp25(+/+) mice (59 ± 3 vs. 49 ± 4% of initial force, respectively) but no similar effect of genotype was detected in the older groups. There was no difference in muscle caspase-3 activity between Hsp25(-/-) and Hsp25(+/+ mice), whether young or old, but there was a significant genotype independent increase in activity with age. Overall, the results suggest that the absence of HSP25 primarily contributes to muscle fatigue resistance, rather than maximal force production, and that this effect is most evident in young compared to older mice.
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Registered trials
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