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Non-proteolytic functions of calpain-3 in sarcoplasmic reticulum in skeletal muscles. | LitMetric

AI Article Synopsis

  • Recent studies using "knock-in" mice (Capn3(CS/CS)) show that while these mice lack protease activity, they exhibit milder symptoms than mice completely deficient in calpain-3, suggesting calpain-3 has important non-proteolytic functions.
  • The research highlights calpain-3's role in the sarcoplasmic reticulum, where it interacts with key proteins to facilitate calcium release during muscle contraction, indicating that its nonenzymatic function is critical for proper muscle function and contributes

Article 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 Capn3(CS/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, Capn3(CS/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 Capn3(CS/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, Capn3(CS/CS) mice showed that the nonenzymatic role of calpain-3 is required for proper Ca(2+) efflux from the SR to cytosol during muscle contraction. These results indicate that calpain-3 functions as a nonenzymatic element for the Ca(2+) 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3056149PMC
http://dx.doi.org/10.1016/j.jmb.2011.01.057DOI Listing

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