INVESTIGADORES
MILANESI Lorena Magdalena
artículos
Título:
Participation of Hsp27 in the antiapoptotic action of 17beta-estradiol in skeletal muscle cells.
Autor/es:
VASCONSUELO, ANDREA; MILANESI, LORENA; BOLAND, RICARDO
Revista:
CELL STRESS & CHAPERONES.
Editorial:
SPRINGER
Referencias:
Año: 2010 vol. 15 p. 183 - 192
ISSN:
1355-8145
Resumen:
Abstract: Exposure to 17b-estradiol prior to induction of
apoptosis protects skeletal muscle cells against damage.
The mechanism involved in this protective action of the
hormone is poorly understood. In the present study, using
the murine muscle cell line C2C12, evidence was obtained
that inhibition of H2O2-induced apoptosis by the estrogen
requires the participation of heat shock protein 27 (HSP27).
Reverse transcriptase polymerase chain reaction, Western
blot, and immunocytochemistry assays showed that 17b-
estradiol induces a time-dependent (5?60 min) increase in
the expression of HSP27. In addition, in presence of
quercetin, an inhibitor of HSPs, the antiapoptotic effect of
the hormone was diminished. More specifically, blockage
experiments with short interference RNA targeting HSP27
confirmed the role of this chaperone in the protective effect
of the steroid. 17b-Estradiol abolished caspase-3 cleavage
elicited by H2O2. Coimmunoprecipitation assays suggested
physical interaction of HSP27 with caspase-3 in presence of
estradiol. Furthermore, we observed that this chaperone
interacts with estrogen receptors (ER) b in mitochondria.
Then, this study suggests that HSP27 plays a new role in
the antiapoptotic action triggered by 17b-estradiol by
modulating caspase-3 activity and stabilizing ERb in
skeletal muscle cells.