ArticleThe Journal of biological chemistry2009
Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretch.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Insights into the heterogeneous muscle lipidome of dysferlin-deficient mice: effects of age, muscle type, and sex.Skeletal muscle · 2026Article
- Variants in CAPN3 Causing Autosomal Dominant Limb-Girdle Muscular Dystrophy Combined With Calpain-3 Deficiency.Human mutation · 2025Article
- Degradative Signaling in ATG7-Deficient Skeletal Muscle Following Cardiotoxin Injury.Muscles (Basel, Switzerland) · 2023Article
- Calpain-3 Is Not a Sodium Dependent Protease and Simply Requires Calcium for Activation.International journal of molecular sciences · 2023Article
- Identification of Phosphorylated Calpain 3 in Rat Brain Mitochondria under mPTP Opening.International journal of molecular sciences · 2021Article
- The ERG1a potassium channel increases basal intracellular calcium concentration and calpain activity in skeletal muscle cells.Skeletal muscle · 2020Article
- Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies.Oxidative medicine and cellular longevity · 2019Review
- Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.The Journal of biological chemistry · 2018Article
- Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans.Sports medicine (Auckland, N.Z.) · 2018Review
- Characterization of muscle ankyrin repeat proteins in human skeletal muscle.American journal of physiology. Cell physiology · 2017Article
- Absence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.Physiological reviews · 2016Review
- Activity, abundance and expression of Ca²⁺-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
- Altered ubiquitin causes perturbed calcium homeostasis, hyperactivation of calpain, dysregulated differentiation, and cataract.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The role of proteases in excitation-contraction coupling failure in muscular dystrophy.American journal of physiology. Cell physiology · 2015Article
- Skeletal muscle atrophy in sedentary Zucker obese rats is not caused by calpain-mediated muscle damage or lipid peroxidation induced by oxidative stress.Journal of negative results in biomedicine · 2014Article
- Three calpain isoforms are autolyzed in rat fast-twitch muscle after eccentric contractions.Journal of muscle research and cell motility · 2014Article
- Altered cross-bridge properties in skeletal muscle dystrophies.Frontiers in physiology · 2014Review
- Article
- Calpain 3 is important for muscle regeneration: evidence from patients with limb girdle muscular dystrophies.BMC musculoskeletal disorders · 2012Article
- Targeted proteolysis of plectin isoform 1a accounts for hemidesmosome dysfunction in mice mimicking the dominant skin blistering disease EBS-Ogna.PLoS genetics · 2011Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolytically active calpain-3/p94 is clearly vital for normal muscle function, since its absence leads to limb girdle muscular dystrophy 2A, but its function and regulatory control are poorly understood. Here we use single muscle fibers, individually skinned by microdissection, to investigate the diffusibility and autolytic activation of calpain-3 in situ. Virtually all calpain-3 present in mature muscle fibers is tightly bound in the vicinity of the titin N2A line and triad junctions and remains so irrespective of fiber stretching or raised [Ca(2+)]. Most calpain-3 is evidently bound within the contractile filament lattice, because (i) its slow diffusional loss is slowed further by locking myosin and actin into rigor and (ii) detergent dispersion of membranes causes rapid washout of most ryanodine receptors and sarcoplasmic reticulum Ca(2+) pumps with little accompanying washout of calpain-3. Calpain-3 autolyzes (becoming proteolytically active) in a tightly calcium-dependent manner. It remains in its nonactivated full-length form if [Ca(2+)] is maintained at < or = 50 nm, the normal resting level, even with brief increases to 2-20 mum during repeated tetanic contractions, but it becomes active (though still bound) if [Ca(2+)] is kept slightly elevated at 200 nm ( approximately 20% autolysis in 1 h). Calpain-3 did not spontaneously autolyze even when free in solution with 200 nm Ca(2+) for up to 60 min. These findings explain why calpain-3 remains quiescent with normal exercise but is activated following eccentric (stretching) contractions, when resting [Ca(2+)] is elevated, and how a protease such as calpain-3 can be very Ca(2+)-sensitive yet highly specific in its actions.
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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.