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Articles in PresS, published online ahead of print January 17, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00675.2001
Submitted on July 31, 2001
Accepted on January 10, 2002
1 Pharmacology, Yale University School of Medicine, New Haven, CT, USA; Section of Digestive Diseases, Yale University School of Medicine, New Haven, CT, USA; Hepatic Hemodynamic Laboratory, VA CT Healthcare System, West Haven, CT, USA
2 Hepatic Hemodynamic Laboratory, VA CT Healthcare System, West Haven, CT, USA
3 Pharmacology, Yale University School of Medicine, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: william.sessa{at}yale.edu.
The protein kinase Akt becomes couples to the activation of receptor tyrosine kinases, G-protein coupled receptors, and mechanical forces such as shear stress. Akt can phosphorylate endothelial nitric oxide synthase (eNOS) and activate the enzyme, leading to nitric oxide (NO) production. The aim of this study is to test the hypothesis that the phosphorylation of eNOS plays a role in enhanced NO production observed in early portal hypertension. Rats were subjected to either sham or portal vein ligation (PVL) and mesenteric artery beds were used for ex vivo perfusion studies. Mesenteric arterial beds from PVL rats had reduced responsiveness to methoxamine, an effect normalized by L-NMMA. The enhanced responsiveness in PVL was not due to changes in eNOS expression but was due to an increase in enzyme specific activity. The phosphorylation of eNOS at serine 1176 and Akt at serine 473 were increased in the PVL group. These results suggest that the phosphorylation of eNOS by Akt activates the enzyme and may be the first step leading to the initial increase in NO production in portal hypertension.
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