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Am J Physiol Cell Physiol (February 5, 2003). doi:10.1152/ajpcell.00098.2002
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Submitted on March 4, 2002
Accepted on January 23, 2003

Early activation of p160ROCK by pressure overload in rat heart

Adriana S Torsoni1, Priscila M Fonseca1, Daniela P Crosara-Alberto1, and Kleber G Franchini1*

1 Internal Medicine, State University of Campinas - School of Medicine, Campinas, SP, Brazil

* To whom correspondence should be addressed. E-mail: franchin{at}obelix.unicamp.br.

We investigated the effects of acute pressure overload on activation of p160ROCK in rat myocardium. Constriction of transverse aorta, controlled to increase peak systolic pressure of ascending aorta by ~40 mmHg, induced a rapid association of RhoA with Dbl-3 and p160ROCK. The binding of p160ROCK to RhoA, was rapidly increased, peaked at 30 min (~3.5-fold), but reduced to lower levels (~1.9- fold) by 60 min of pressure overload. The activity of immunoprecipitated p160ROCK toward myosin light chain, increased ~2.5-fold within 10 min, but decreased to lower levels (~1.6-fold) after 60 min of pressure overload. Confocal microscopy analysis indicated that pressure overload induced the formation of aggregates of p160ROCK and RhoA along the longitudinal axis of cardiac myocytes. Immunoelectron microscopy analysis showed that pressure overload induced the association of p160ROCK and RhoA to Z-line, T-tubule and sub-sarcolemmal areas. The rapid activation of p160ROCK by pressure overload and its aggregation in subcellular structures involved in transmission of mechanical force suggest a role for this enzyme in the mechano-biochemical transduction in the myocardium.




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