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First published online November 5, 2008

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Caspase-9 muscles in

Caspases, which comprise a family of cysteine proteases, are best known for their central role in apoptosis. Evidence suggests, however, that caspase-3 – an effector caspase that, when activated, cleaves numerous intracellular proteins during apoptosis – is also necessary for the differentiation of muscle progenitor cells into myofibres. To determine how such disparate roles can be reconciled, Howard Fearnhead and colleagues (p. 3786) ask how caspase-3 activity is regulated during muscle differentiation. Using the C2C12 mouse myoblast cell line, the authors show that caspase-9 – which activates caspase-3 during the mitochondria-dependent apoptotic pathway – is activated during myotube formation. Moreover, knocking down caspase-9 expression strongly decreases both myoblast fusion and caspase-3 activation. The authors demonstrate that overexpression of Bcl-xL, which inhibits caspase-9 activation during apoptosis by preserving mitochondrial outer-membrane integrity, also inhibits myoblast fusion; counterintuitively, however, no depolarisation of the outer membrane is observed during C2C12 differentiation. Thus, caspase-9 appears to promote muscle differentiation – but it might, the authors propose, be activated by a mechanism that is not dependent on mitochondria.

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A non-apoptotic role for caspase-9 in muscle differentiation

Thomas V. A. Murray, Jill M. McMahon, Breege A. Howley, Alanna Stanley, Thomas Ritter, Andrea Mohr, Ralf Zwacka, and Howard O. Fearnhead
JCS 2008 121: 3786-3793. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?