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1 Department of Vascular Biology Center, Medical College of Georgia, Augusta, GA, USA; Department of Pediatrics, Medical College of Georgia, Augusta, GA, USA
2 Department of Vascular Biology Center, Medical College of Georgia, Augusta, GA, USA
3 Department of Vascular Biology Center, Medical College of Georgia, Augusta, GA, USA; Department of Pediatrics, Medical College of Georgia, Augusta, GA, USA; Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta, GA, USA
* To whom correspondence should be addressed. E-mail: bharris{at}mail.mcg.edu.
Endothelial nitric oxide synthase (eNOS) is regulated by heat shock protein 90 (Hsp90), a heat-inducible protein, however, the effect of heat shock on eNOS expression and endothelial nitric oxide (NO) release is unknown. Bovine aortic endothelial cells were incubated for 1 h at 37oC, 42oC or 45oC and cell lysates were evaluated using Western blot. A 2.1±0.1-fold increase in eNOS protein content, but no change in Hsp90 content,Hsp70 content, or Hsp90/eNOS association was observed 24 h following heat shock at 42oC. A 7.7±1.5-fold increase in Hsp70 protein content, but no change in eNOS or Hsp90 was observed 24 h after heat shock at 45oC. eNOS activity and maximal bradykinin-stimulated NO release was significantly increased 24 h following heat shock at 42oC. Heat shock in rats (Tc 42oC, 15 min) resulted in a significant increase in aortic eNOS, Hsp90, and Hsp70 protein content. Aorta from heat shocked rats exhibited a decreased maximal contractile response to phenylephrine, which was abolished by preincubation with L-NNA. We conclude that prior heat shock is a physical stimulus of increased eNOS expression and is associated with an increase in eNOS activity, agonist-stimulated NO release as well as a decreased vasoconstrictor response.
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