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Am J Physiol Heart Circ Physiol (July 24, 2003). doi:10.1152/ajpheart.00365.2003
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Submitted on April 21, 2003
Accepted on July 23, 2003

Acute p38 MAPK activation decreases force development in ventricular myocytes

Yi Chen1, Ravi Rajashree1, Qinghang Liu1, and Polly Hofmann1*

1 Department of Physiology, University of Tennessee, Memphis, TN, USA

* To whom correspondence should be addressed. E-mail: phofmann{at}physio1.utmem.edu.

Evidence suggests p38 MAPK activation influences cardiac function on an acute basis. The characterization and mechanisms by which this occurs was investigated in the present study. Adult rat ventricular myocytes treated with 1 mM arsenite for 30 minutes had a 16 fold increase in p38 MAPK phosphorylation that was attenuated by SB203580 (p38 MAPK inhibitor). ERK and JNK were also minimally activated, but this activation was not sensitive to SB203580. In addition, arsenite caused a p38 MAPK-independent translocation/activation of protein phosphatase 2a (PP2a) and decrease in phosphorylation of myosin light chain 2 (LC2). Arsenite-p38 MAPK activation lead to translocation of heat shock protein 27, but not {alpha}B-crystallin to the myofilaments. Using isolated cardiomyocytes we determined arsenite reduces isometric tension without a change in Ca2+ sensitivity of tension via p38 MAPK, and lowered myofibrillar actomyosin MgATPase activity in a p38 MAPK-independent manner. Thus, arsenite induces a p38 MAPK-independent change in PP2a and LC 2 that may account for the arsenite-dependent decrease in ATPase, and a p38 MAPK-dependent modification of the myofilaments which decrease myocardial force development.




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