Translocation of HSP27 to sarcomere induced by ischemic preconditioning in isolated rat hearts.

Abstract:

:We investigated the role of the 27-kDa heat shock protein (HSP27) in cardiac protection using Langendorff-perfused rat hearts. After preconditioning (a single episode of 5 min global ischemia followed by 5 min of reperfusion), HSP27 redistributed from the cytosol to the sarcomere and recovery of the contractile function, after 40 min of global ischemia and 50 min of reperfusion, was significantly enhanced. Both SB203580, a p38 MAP kinase inhibitor, and bisindolylmaleimide I, a protein kinase C inhibitor, prevented the effects of preconditioning. Both 2-chloro-N(6)-cyclopentyladenosine (adenosine A1 agonist) and anisomycin (activator of p38 MAP kinase and c-jun N-terminal kinase) mimicked preconditioning. These results suggest that activation of protein kinase C followed by activation of p38 MAP kinase elicits translocation of HSP27 to the sarcomere, a process which may be involved in the cardioprotective mechanism afforded by ischemic preconditioning in rat heart.

authors

Sakamoto K,Urushidani T,Nagao T

doi

10.1006/bbrc.2000.2233

subject

Has Abstract

pub_date

2000-03-05 00:00:00

pages

137-42

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92233-2

journal_volume

269

pub_type

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