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• W2009098855 abstract "Mutations in CAPN3/Capn3, which codes for skeletal muscle-specific calpain-3/p94 protease, are responsible for limb-girdle muscular dystrophy type 2A. Using “knock-in” (referred to as Capn3CS/CS) mice, in which the endogenous calpain-3 is replaced with a mutant calpain-3:C129S, which is a proteolytically inactive but structurally intact calpain-3, we demonstrated in our previous studies that loss of calpain-3 protease activity causes muscular dystrophy [Ojima, K. et al. (2010) J. Clin. Invest. 120, 2672–2683]. However, compared to Capn3-null (Capn3−/−) mice, Capn3CS/CS mice showed less severe dystrophic symptoms. This suggests that calpain-3 also has a non-proteolytic function. This study aimed to elucidate the non-proteolytic functions of calpain-3 through comparison of Capn3CS/CS mice with Capn3−/− mice. We found that calpain-3 is a component of the sarcoplasmic reticulum (SR), and that calpain-3 interacts with, but does not proteolyze, typical SR components such as ryanodine receptor and calsequestrin. Furthermore, Capn3CS/CS mice showed that the nonenzymatic role of calpain-3 is required for proper Ca2+ efflux from the SR to cytosol during muscle contraction. These results indicate that calpain-3 functions as a nonenzymatic element for the Ca2+ efflux machinery in the SR, rather than as a protease. Thus, defects in the nonenzymatic function of calpain-3 must also be involved in the pathogenesis of limb-girdle muscular dystrophy type 2A." @default.
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• W2009098855 date "2011-04-01" @default.
• W2009098855 modified "2023-10-15" @default.
• W2009098855 title "Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles" @default.
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• W2009098855 doi "https://doi.org/10.1016/j.jmb.2011.01.057" @default.
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