Exercise-mediated regulation of Hsp70 expression following aerobic exercise training

1 School of Kinesiology, Faculty of Health Sciences, and 2 Lawson Health Research Institute, The University of Western Ontario, London, Ontario, Canada Submitted 16 July 2007 ; accepted in final form 29 September 2007 An issue central to understanding the biological benefits associated with regular exercise training is to elucidate the intracellular mechanisms governing exercise-conferred cardioprotection. Heat shock proteins (HSPs), most notably the inducible 70-kDa HSP family member Hsp70, are believed to participate in the protection of the myocardium during cardiovascular stress. Following acute exercise, activation of PKA mediates the suppression of an intermediary protein kinase, ERK1/2, which phosphorylates and suppresses the activation of the heat shock transcription factor 1 (HSF1). However, following exercise training, ERK1/2 has been reported to regulate the transcriptional activation of several genes involved in cell growth and proliferation and has been shown to be associated with training-mediated myocardial hypertrophy. The present project examined the transcriptional activation of hsp70 gene expression in acutely exercised (60 min at 30 m/min) naïve sedentary and aerobically trained (8 wk, low intensity) male Sprague-Dawley rats. Following acute exercise stress, no significant differences were demonstrated in the expression of myocardial Hsp70 mRNA and activation of PKA between sedentary and trained animals. However, trained animals elicited expression of the hsp70 gene ( P < 0.05) in the presence of elevated ERK1/2 activation. Given the association of ERK1/2 and the suppression of hsp70 gene expression following acute exercise in naïve sedentary rats, these results suggest that training results in adaptations that allow for the simultaneous initiation of both proliferative and protective responses. While it is unclear what factors are associated with this training-related shift, increases in HSF1 DNA binding affinity ( P < 0.05) and posttranscriptional modifications of the Hsp70 transcript are suggested. protein kinase A; mitogen-activated protein kinase; protein phosphorylation; receptors; signal transduction Address for reprint requests and other correspondence: E. G. Noble, School of Kinesiology, Faculty of Health Sciences, and Lawson Health Research Institute, The Univ. of Western Ontario, London, Ontario, Canada N6A 3K7 (e-mail: enoble{at}uwo.ca )