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Am J Physiol Cell Physiol 283: C404-C411, 2002. First published March 27, 2002; doi:10.1152/ajpcell.00051.2002
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Vol. 283, Issue 2, C404-C411, August 2002

Redox signaling of cardiac HSF1 DNA binding

Zain Paroo1, Michael J. Meredith5, Marius Locke4, James V. Haist3, Morris Karmazyn3, and Earl G. Noble1,2

1 School of Kinesiology, Faculty of Health Sciences, 2 Lawson Health Research Institute, and 3 Department of Pharmacology and Toxicology, Faculty of Medicine and Dentistry, University of Western Ontario, London, Ontario, Canada N6A 3K7; 4 Faculty of Physical Education and Health, University of Toronto, Toronto, Ontario, Canada M5S 2W6; and 5 School of Dentistry, Oregon Health and Science University, Portland, Oregon 97201-3098

Experiments involving chemical induction of the heat shock response in simple biological systems have generated the hypothesis that protein denaturation and consequential binding of heat shock transcription factor 1 (HSF1) to proximal heat shock elements (HSEs) on heat shock protein (hsp) genes are the result of oxidation and/or depletion of intracellular thiols. The purpose of the present investigation was to determine the role of redox signaling of HSF1 in the intact animal in response to physiological and pharmacological perturbations. Heat shock and exercise induced HSF1-HSE DNA binding in the rat myocardium (P < 0.001) in the absence of changes in reduced glutathione (GSH), the major nonprotein thiol in the cell. Ischemia-reperfusion, which decreased GSH content (P < 0.05), resulted in nonsignificant HSF1-HSE formation. This dissociation between physiological induction of HSF1 and changes in GSH was not gender dependent. Pharmacological ablation of GSH with L-buthionine-[S,R]-sulfoximine (BSO) treatment increased myocardial HSF1-HSE DNA binding in estrogen-naive animals (P = 0.007). Thus, although physiological induction of HSF1-HSE DNA binding is likely regulated by mediators of protein denaturation other than cellular redox status, the proposed signaling pathway may predominate with pharmacological oxidation and may represent a plausible and accessible strategy in the development of HSP-based therapies.

protein denaturation; exercise; glutathione; heat shock protein; ischemia-reperfusion


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