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1 Department of Surgery, University of Washington, Seattle, WA, USA
2 National Health and Environmental Effects Laboratory, Office of Research and Development, U.S. Environmental Protection Agency, Research Triangle Park, NC, USA
* To whom correspondence should be addressed. E-mail: tpohlman{at}u.washington.edu.
We investigated the role of inducible heat-shock proteins 70.1 (Hsp70.1) and 70.3 (Hsp70.3) in myocardial ischemic preconditioning (IP) in mice. Wild type (WT) mice and Hsp70.1/3 null mice were subjected to IP and examined 24 hours later during the late phase of protection. IP significantly increased steady-state levels of hsp70.1 and hsp70.3 mRNA, and expression for inducible Hsp70 protein in WT myocardium. To assess protection against tissue injury, mice were subjected to 30 minutes of regional ischemia and 3 hours of reperfusion (I/R). In WT mice, IP reduced infarct size by 43% compared to sham IP-treated mice. In contrast, IP did not reduce infarct size in Hsp70.1/3 null mice. Absence of inducible Hsp70.1 and 70.3, however, had no effect on classic, or early phase protection produced by IP, which significantly reduced infarct size in Hsp70.1/3 null mice. We conclude that inducible Hsp70.1 and Hsp70.3 are required for late phase protection against infarction following IP in mice.
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