ArticleThe Biochemical journal1998
Purification of native p94, a muscle-specific calpain, and characterization of its autolysis.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 119 citations in OpenAlex.
- Oligomer-dependent and oligomer-independent pathogenesis of muscular dystrophy-associated mutations within the penta-EF-hand domain of calpain-3.The Journal of biological chemistry · 2026Article
- Human calpain-3 and its structural plasticity: dissociation of a homohexamer into dimers on binding titin.bioRxiv : the preprint server for biology · 2024Article
- Calpain-3 Is Not a Sodium Dependent Protease and Simply Requires Calcium for Activation.International journal of molecular sciences · 2023Article
- Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.The Journal of biological chemistry · 2018Article
- Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.The Journal of biological chemistry · 2018Article
- Autolytic activation of calpain 3 proteinase is facilitated by calmodulin protein.The Journal of biological chemistry · 2015Article
- The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Role of calpains in the injury-induced dysfunction and degeneration of the mammalian axon.Neurobiology of disease · 2013Review
- PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.Journal of molecular biology · 2013Article
- A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review.Asian-Australasian journal of animal sciences · 2013Review
- Characterization of the expression profile of calpain-3 (CAPN3) gene in chicken.Molecular biology reports · 2012Article
- The atypical calpains: evolutionary analyses and roles in Caenorhabditis elegans cellular degeneration.PLoS genetics · 2012Article
- Pathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.Human molecular genetics · 2011Article
- Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodeling.PloS one · 2010Article
- Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretch.The Journal of biological chemistry · 2009Article
- Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Neuromuscular disorders : NMD · 2008Review
- Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle.European journal of applied physiology · 2008Article
- Comprehensive survey of p94/calpain 3 substrates by comparative proteomics--possible regulation of protein synthesis by p94.Biotechnology journal · 2007Article
- Regulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiation.Molecular and cellular biology · 2006Article
- Homodimerization of calpain 3 penta-EF-hand domain.The Biochemical journal · 2005Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p94, a skeletal muscle-specific calpain, has attracted much attention because its gene is responsible for limb-girdle muscular dystrophy type 2A. p94, however, has not been characterized at the protein and enzyme levels, owing to its very rapid autolysis. In the present study, a purification procedure for p94 was first established by using a recombinant inactive p94 expressed in COS cells in which the active site cysteine residue was changed to serine [p94(C129S)]. The isolation of native p94 from rabbit skeletal muscle by the established method with conventional procedures was extremely difficult because p94 became highly unstable in a crude extract on the addition of NaCl for separation. Purification of native p94 was possible with an antibody-affinity column but only as an inactive enzyme; p94(C129S) was purified as a homodimer. Characterization of p94, especially autolysis, was performed with partly purified native p94 and p94(C129S). The autolysis of p94, which consisted at least partly of an intermolecular reaction, proceeded in three consecutive steps; 60 and 58 kDa fragments were produced as intermediates before a stable 55 kDa fragment appeared. Autolysis of p94 was regarded as a degradative step rather than for the activation of the enzyme. All the autolysis cleavage sites were located in the p94-specific insertion sequence 1 region, which explains why p94 is unstable compared with the other calpains. The autolysis sites in p94 clearly showed a different specificity relative to the autolytic and proteolytic cleavage sites of the ubiquitous mu- and m-calpains, in its preference for residues at the P3 to P1' sites, indicating a distinct substrate specificity and function for the muscle enzyme.
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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.