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Death of dystrophin-deficient muscle purportedly results from
increases in [Ca]
Volume 270,
Number 18,
Issue of May 5, pp. 10909-10914, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
that cause the activation of
calpains. We have tested whether calpains play a role in this process
by assaying for changes in calpain concentration and activation in peak
necrotic mdx mice (4 weeks of age) and in completely regenerated mdx
mice (14 weeks of age). Biochemical fractionation and immunoblotting
with epitope-specific antisera allowed measurement of the
concentrations of m- and µ-calpains and the extent of
autoproteolytic modification. Our findings show that total calpain
concentration is elevated in both 4-week and 14-week mdx mice. This
increase in concentration was shown to result primarily from a
significant increase in m-calpain concentration at 4 weeks. Northern
analysis demonstrated that neither m- nor µ-calpain mRNA
concentrations differed between mdx and controls suggesting that the
increased calpain concentration results from post-translational
regulation. Immunoblotting with antibodies directed against
amino-terminal peptides revealed an increase in autoproteolysis of
µ-calpain, indicative of increased activation. The extent of
autoproteolysis of µ-calpain returns to control levels during
regeneration. This is not a consequence of increased calpastatin mRNA
or protein. The findings reported here support a role for calpains in
both the degenerative and regenerative aspects of mdx dystrophy.
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