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Articles in PresS, published online ahead of print July 8, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00214.2002
Submitted on March 13, 2002
Accepted on June 24, 2002
1 Wallace H. Coulter Department of Biomedical Engineering, Georgia Tech and Emory University, Atlanta, GA, USA
2 St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria, Australia
3 Pharmacology, Rush Presbyterian St. Luke's Medical Center, Chicago, IL, USA
* To whom correspondence should be addressed. E-mail: hanjoong.jo{at}bme.gatech.edu.
Shear stress stimulates NO production by phosphorylating eNOS at Ser1179 in a phosphoinositide-3-kinase (PI3K)- and protein kinase A (PKA)-dependent manner. The eNOS has additional potential phosphorylation sites including Ser116, Thr497 and Ser635. Here, we studied these potential phosphorylation sites in response to shear, vascular endothelial growth factor (VEGF) and 8-Br-cAMP in bovine aortic endothelial cells (BAEC). All three stimuli induced phosphorylation of eNOS at Ser635 that was consistently slower than that at Ser1179. Thr497 was rapidly dephosphorylated by 8-Br-cAMP, but not by shear and VEGF. None of the stimuli phosphorylated Ser116. While shear-stimulated Ser635 phosphorylation was not affected by PI3K inhibitors wortmannin and LY294002, it was blocked by either treating the cells with a PKA inhibitor H89 or infecting them with a recombinant adenovirus expressing PKA inhibitor (PKI). These results suggest that shear stimulates eNOS by two different mechanisms: 1) PKA- and PI3K-dependent and 2) PKA-dependent but PI3K-independent pathways. Phosphorylation of Ser635 may play an important role in chronic regulation of eNOS in response to mechanical and humoral stimuli.
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