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Am J Physiol Heart Circ Physiol 292: H2982-H2987, 2007. First published February 9, 2007; doi:10.1152/ajpheart.01303.2006
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Role of p38 mitogen-activated protein kinase pathway in estrogen-mediated cardioprotection following trauma-hemorrhage

Jun-Te Hsu,2 Ya-Ching Hsieh,1 Wen Hong Kan,1 Jian Guo Chen,1 Mashkoor A. Choudhry,1 Martin G. Schwacha,1 Kirby I. Bland,1 and Irshad H. Chaudry1

1Center for Surgical Research and Department of Surgery, University of Alabama at Birmingham, Birmingham, Alabama; and 2Department of Surgery, Chang Gung Memorial Hospital, Chang Gung University, Taoyuan, Taiwan

Submitted 28 November 2006 ; accepted in final form 6 February 2007

p38 mitogen-activated protein kinase (MAPK) activates a number of heat shock proteins (HSPs), including HSP27 and {alpha}B-crystallin, in response to stress. Activation of HSP27 or {alpha}B-crystallin is known to protect organs/cells by increasing the stability of actin microfilaments. Although our previous studies showed that 17beta-estradiol (E2) improves cardiovascular function after trauma-hemorrhage, whether the salutary effects of E2 under those conditions are mediated via p38 MAPK remains unknown. Male rats (275–325 g body wt) were subjected to soft tissue trauma and hemorrhage (35–40 mmHg mean blood pressure for ~90 min) followed by fluid resuscitation. At the onset of resuscitation, rats were injected intravenously with vehicle, E2 (1 mg/kg body wt), E2 + the p38 MAPK inhibitor SB-203580 (2 mg/kg body wt), or SB-203580 alone, and various parameters were measured 2 h thereafter. Cardiac functions that were depressed after trauma-hemorrhage were returned to normal levels by E2 administration, and phosphorylation of cardiac p38 MAPK, HSP27, and {alpha}B-crystallin was increased. The E2-mediated improvement of cardiac function and increase in p38 MAPK, HSP27, and {alpha}B-crystallin phosphorylation were abolished with coadministration of SB-203580. These results suggest that the salutary effect of E2 on cardiac function after trauma-hemorrhage is in part mediated via upregulation of p38 MAPK and subsequent phosphorylation of HSP27 and {alpha}B-crystallin.

heat shock proteins; {alpha}B-crystallin; p38 mitogen-activated protein kinase inhibitor


Address for reprint requests and other correspondence: I. H. Chaudry, Center for Surgical Research, Univ. of Alabama at Birmingham, 1670 Univ. Blvd., Volker Hall, Rm. G094, Birmingham, AL 35294-0019 (e-mail: Irshad.Chaudry{at}ccc.uab.edu)




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