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Caspase‐1‐induced calpastatin degradation in myoblast differentiation and fusion: cross‐talk between the caspase and calpain systems
Author(s) -
Barnoy Sivia,
Kosower Nechama S.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00573-8
Subject(s) - calpastatin , calpain , microbiology and biotechnology , caspase , chemistry , caspase 1 , caspase 3 , fusion , apoptosis , biochemistry , biology , programmed cell death , enzyme , linguistics , philosophy
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.