Hsp27 as a Negative Regulator of Cytochrome c Release
Hsp27
Cytochalasin D
DOI:
10.1128/mcb.22.3.816-834.2002
Publication Date:
2009-04-22T02:44:35Z
AUTHORS (6)
ABSTRACT
We previously showed that Hsp27 protects against apoptosis through its interaction with cytosolic cytochrome c. have revisited this protective activity in murine cell lines expressing different levels of Hsp27. report also interferes, a manner dependent on level expression, the release c from mitochondria. Moreover, decreased endogenous Hsp27, which sensitized HeLa cells to apoptosis, reduced delay required for and procaspase 3 activation. The molecular mechanism regulating function is unknown. In our systems, mainly only small fraction protein colocalized we show very interacts hence excluding role retention Bid intracellular relocalization was altered by changes suggesting interferes apoptotic signals upstream therefore investigated if ability act as an expression-dependent modulator F-actin microfilaments integrity linked here depolymerizing agent cytochalasin D rapidly induced mitochondria caspase This phenomenon delayed pretreated stabilizer phalloidin high suggests existence signaling pathway linking cytoskeleton damages pathway, induces redistribution, negatively regulated protect network integrity. However, probably not one be since, staurosporine-treated cells, partially inhibited etoposide-treated still redistribution conditions where altered.
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