[HTML][HTML] Caspase-1-induced calpastatin degradation in myoblast differentiation and fusion: cross-talk between the caspase and calpain systems

S Barnoy, NS Kosower - FEBS letters, 2003 - Elsevier
S Barnoy, NS Kosower
FEBS letters, 2003Elsevier
Previously, we found that calpastatin diminished transiently prior to myoblast fusion (rat L8
myoblasts), allowing calpain-induced protein degradation, required for fusion. Here we
show that the transient diminution in calpastatin is due to its degradation by caspase-1.
Inhibition of caspase-1 prevents calpastatin diminution and prevents myoblast fusion.
Caspase-1 activity is transiently increased during myoblast differentiation. Both calpain and
caspase appear to be responsible for the fusion-associated membrane protein degradation …
Previously, we found that calpastatin diminished transiently prior to myoblast fusion (rat L8 myoblasts), allowing calpain-induced protein degradation, required for fusion. Here we show that the transient diminution in calpastatin is due to its degradation by caspase-1. Inhibition of caspase-1 prevents calpastatin diminution and prevents myoblast fusion. Caspase-1 activity is transiently increased during myoblast differentiation. Both calpain and caspase appear to be responsible for the fusion-associated membrane protein degradation. Caspase-1 has been implicated in the activation of proinflammatory cytokines, and in cell apoptosis. The involvement of caspase-1 in L8 myoblast fusion represents a novel function for this caspase in a non-apoptotic differentiation process, and points to cross-talk between the calpain and caspase systems in some differentiation processes.
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