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The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion.

Abstract：

:Using red cells as an experimental model, we previously showed that a limited degradation of certain membrane proteins by calpain (Ca2+-activated thiol protease) was a necessary prerequisite for cell fusion and that fusibility depended on the ratio of calpain to its endogenous inhibitor calpastatin. Here we show that fusion of rat L8 line myoblasts is accompanied by a dramatic change in the calpain/calpastatin ratio. The protein levels of mu-calpain and m-calpain increased only slightly during myoblast differentiation. In contrast, calpastatin diminished by a factor of 10 at the stages of myoblast alignment and start of fusion, allowing calpain activity to become apparent. Calpastatin reappeared at a late stage of myoblast fusion (myotube formation). The results indicate that calpastatin is regulated during myoblast differentiation, and that its diminution is important in determining the activity of the calpain required for myoblast fusion.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Barnoy S,Glasner T,Kosower NS

doi

10.1006/bbrc.1996.0509

subject

Has Abstract

pub_date

1996-03-27 00:00:00

pages

933-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X96905094

journal_volume

220

pub_type

杂志文章

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