PMID: 9551085Apr 29, 1998Paper

The calpain-calpastatin system and protein degradation in fusing myoblasts

Biochimica Et Biophysica Acta
Sivia BarnoyNechama S Kosower

Abstract

Calpain (Ca(2+)-activated cysteine protease) induced proteolysis has been suggested to play a role in myoblast fusion. We previously found that calpastatin (the endogenous inhibitor of calpain) diminishes markedly in myoblasts during myoblast differentiation just prior to the start of fusion, allowing Ca(2+)-induced calpain activation at that stage. Here, we show that a limited degradation of some proteins occurs within the myoblasts undergoing fusion, but not in proliferating myoblasts. The protein degradation is observed at the stage when calpastatin is low. Protein degradation within the myoblasts and myoblast fusion are inhibited by EGTA, by the cysteine protease inhibitors calpeptin and E-64d and by calpastatin. The degradation appears to be selective for certain myoblast proteins. Integrin beta 1 subunit, talin and beta-tropomyosin are degraded in the fusing myoblasts, whereas alpha-actinin, beta-tubulin and alpha-tropomyosin are not. A similar pattern of degradation is observed in lysates of proliferating myoblasts when Ca2+ and excess calpain are added, a degradation that is inhibited by calpastatin. The results support the notion that degradation of certain proteins is required for myoblast fusion and that calpain part...Continue Reading

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Citations

Apr 13, 2007·European Journal of Applied Physiology·Deborah L EnnsAngelo N Belcastro
May 21, 2005·Biochemical and Biophysical Research Communications·Sivia BarnoyNechama S Kosower
Jun 14, 2005·Fertility and Sterility·Irit Ben-AharonRuth Shalgi
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