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Endothelial nitric oxide synthase activity is inhibited by the plasma membrane calcium ATPase in human endothelial cells
Faculty
Pharmacy
Year:
2010
Type of Publication:
Article
Pages:
440-448
Authors:
Mohamed, Tamer M. A, Neyses, Ludwig, Oceandy, Delvac, Holton, Marylouisa, Wang, Weiguang, Armesilla, Angel L, Emerson, Michael, Lamas, Santiago
DOI:
10.1093/cvr/cvq077
Journal:
CARDIOVASCULAR RESEARCH OXFORD UNIV PRESS
Volume:
87
Research Area:
Cardiovascular System \& Cardiology
ISSN
ISI:000280014900008
Keywords :
Plasma membrane calcium ATPase, eNOS, Functional interaction, Nitric oxide regulation
Abstract:
Nitric oxide (NO) plays a pivotal role in the regulation of cardiovascular physiology. Endothelial NO is mainly produced by the endothelial nitric oxide synthase (eNOS) enzyme. eNOS enzymatic activity is regulated at several levels, including Ca(2+)/calmodulin binding and the interaction of eNOS with associated proteins. There is emerging evidence indicating a role for the plasma membrane calcium ATPase (PMCA) as a negative regulator of Ca(2+)/calmodulin-dependent signal transduction pathways via its interaction with partner proteins. The aim of our study was to investigate the possibility that the activity of eNOS is regulated through its association with endothelial PMCA. We show here a novel interaction between endogenous eNOS and PMCA in human primary endothelial cells. The interaction domains were located to the region 735-934 of eNOS and the catalytic domain of PMCA. Ectopic expression of PMCA in endothelial cells resulted in an increase in phosphorylation of the residue Thr-495 of endogenous eNOS. However, disruption of the PMCA-eNOS interaction by expression of the PMCA interaction domain significantly reversed the PMCA-mediated effect on eNOS phosphorylation. These results suggest that eNOS activity is negatively regulated via interaction with PMCA. Moreover, NO production by endothelial cells was significantly reduced by ectopic expression of PMCA. Our results show strong evidence for a novel functional interaction between endogenous PMCA and eNOS in endothelial cells, suggesting a role for endothelial PMCA as a negative modulator of eNOS activity, and, therefore, NO-dependent signal transduction pathways.
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