ArticleThe Journal of physiology2002
Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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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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.
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Who cites it
78 citing papers in PubMed, 211 citations in OpenAlex.
- Dynamics of myosin degradation in intensive care unit-acquired weakness during severe critical illness.Intensive care medicine · 2014Trial
- Combating muscle atrophy: emerging therapeutic targets that are fiber-type-specific.The FEBS journal · 2025Review
- Muscle Disuse Atrophy.Advances in experimental medicine and biology · 2025Review
- Sepsis-Associated Muscle Wasting: A Comprehensive Review from Bench to Bedside.International journal of molecular sciences · 2023Review
- Calpain-dependent degradation of cytoskeletal proteins as a key mechanism for a reduction in intrinsic passive stiffness of unloaded rat postural muscle.Pflugers Archiv : European journal of physiology · 2022Article
- Postdevelopmental knockout of Orai1 improves muscle pathology in a mouse model of Duchenne muscular dystrophy.The Journal of general physiology · 2022Article
- Review
- Construction and Analysis of Disuse Atrophy Model of the Gastrocnemius Muscle in Chicken.International journal of molecular sciences · 2022Article
- Cardiovasomobility: an integrative understanding of how disuse impacts cardiovascular and skeletal muscle health.Journal of applied physiology (Bethesda, Md. : 1985) · 2022Review
- The inflammatory response, a mixed blessing for muscle homeostasis and plasticity.Frontiers in physiology · 2022Review
- Effects of Various Muscle Disuse States and Countermeasures on Muscle Molecular Signaling.International journal of molecular sciences · 2021Review
- Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation.Biomolecules · 2021Review
- Pseudo-Starvation Driven Energy Expenditure Negatively Affects Ovarian Follicle Development.International journal of molecular sciences · 2021Article
- Breakdown of Filamentous Myofibrils by the UPS-Step by Step.Biomolecules · 2021Review
- Calpain activation mediates microgravity-induced myocardial abnormalities in mice via p38 and ERK1/2 MAPK pathways.The Journal of biological chemistry · 2020Article
- Skeletal Muscle Recovery from Disuse Atrophy: Protein Turnover Signaling and Strategies for Accelerating Muscle Regrowth.International journal of molecular sciences · 2020Review
- Redox Control of Proteolysis During Inactivity-Induced Skeletal Muscle Atrophy.Antioxidants & redox signaling · 2020Review
- Article
- Mitochondrial dysfunction induces muscle atrophy during prolonged inactivity: A review of the causes and effects.Archives of biochemistry and biophysics · 2019Review
- Inhibition of calpain delays early muscle atrophy after rotator cuff tendon release in sheep.Physiological reports · 2018Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Muscle wasting is a prominent feature of several systemic diseases, neurological damage and muscle disuse. The contribution of calpain proteases to muscle wasting in any instance of muscle injury or disease has remained unknown because of the inability to specifically perturb calpain activity in vivo. We have generated a transgenic mouse with muscle-specific overexpression of calpastatin, which is the endogenous inhibitor of calpains, and induced muscle atrophy by unloading hindlimb musculature for 10 days. Expression of the transgene resulted in increases in calpastatin concentration in muscle by 30- to 50-fold, and eliminated all calpain activity that was detectable on zymograms. Muscle fibres in ambulatory, transgenic mice were smaller in diameter, but more numerous, so that muscle mass did not differ between transgenic and non-transgenic mice. This is consistent with the role of the calpain-calpastatin system in muscle cell fusion that has been observed in vitro. Overexpression of calpastatin reduced muscle atrophy by 30 % during the 10 day unloading period. In addition, calpastatin overexpression completely prevented the shift in myofibrillar myosin content from slow to fast isoforms, which normally occurs in muscle unloading. These findings indicate that therapeutics directed toward regulating the calpain-calpastatin system may be beneficial in preventing muscle mass loss in muscle injury and disease.
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Registered trials
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.