© 1999 by European Society of Cardiology
Copyright © 1999, European Society of Cardiology
Signal transduction of eNOS activation
Institut für Kardiovaskuläre Physiologie, Klinikum der J.W. Goethe-Universität, Theodor-Stern-Kai 7, D-60590 Frankfurt am Main, Germany
* Corresponding author. Tel.: +49-69-63016052; fax: +49-60-63017668 Fleming{at}em.uni-frankfurt.de
Consistent with its classification as a Ca2+/calmodulin-dependent enzyme the constitutive endothelial nitric oxide (NO) synthase (eNOS) can be activated by receptor-dependent and -independent agonists as a consequence of an increase in the intracellular concentration of free Ca2+ ([Ca2+]i) and the association of the Ca2+/calmodulin complex with eNOS. Additional post-translational mechanisms regulate the activity of eNOS, including the interaction of eNOS with caveolin-1, heat shock protein 90 (Hsp90), or membrane phospholipids, as well as enzyme translocation and phosphorylation. In response to fluid shear stress the maintained production of NO by native and cultured endothelial cells is associated with only a transient increase in [Ca2+]i. In the absence of extracellular Ca2+ and in the presence of calmodulin antagonists, shear stress stimulates a maintained production of NO which is insensitive to the removal of extracellular Ca2+, but sensitive to tyrosine kinase inhibitors, Hsp90-binding proteins and phosphatidylinositol 3-kinase inhibitors. A pharmacologically identical activation of eNOS can be induced by protein tyrosine phosphatase inhibitors suggesting that the phosphorylation of eNOS, and possibly that of an associated regulatory protein(s), is crucial for its Ca2+-independent activation.
KEYWORDS Endothelial function; Nitric oxide; Signal transduction
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B. J. Michell, Z.-p. Chen, T. Tiganis, D. Stapleton, F. Katsis, D. A. Power, A. T. Sim, and B. E. Kemp Coordinated Control of Endothelial Nitric-oxide Synthase Phosphorylation by Protein Kinase C and the cAMP-dependent Protein Kinase J. Biol. Chem., May 18, 2001; 276(21): 17625 - 17628. [Abstract] [Full Text] [PDF]
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Y. Laumonnier, S. Nadaud, M. Agrapart, and F. Soubrier Characterization of an Upstream Enhancer Region in the Promoter of the Human Endothelial Nitric-oxide Synthase Gene J. Biol. Chem., December 22, 2000; 275(52): 40732 - 40741. [Abstract] [Full Text] [PDF]
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A. Brouet, P. Sonveaux, C. Dessy, J.-L. Balligand, and O. Feron Hsp90 Ensures the Transition from the Early Ca2+-dependent to the Late Phosphorylation-dependent Activation of the Endothelial Nitric-oxide Synthase in Vascular Endothelial Growth Factor-exposed Endothelial Cells J. Biol. Chem., August 24, 2001; 276(35): 32663 - 32669. [Abstract] [Full Text] [PDF]
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M. Montagnani, H. Chen, V. A. Barr, and M. J. Quon Insulin-stimulated Activation of eNOS Is Independent of Ca2+ but Requires Phosphorylation by Akt at Ser1179 J. Biol. Chem., August 3, 2001; 276(32): 30392 - 30398. [Abstract] [Full Text] [PDF]
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X. Wang and A. A. Abdel-Rahman Estrogen modulation of eNOS activity and its association with caveolin-3 and calmodulin in rat hearts Am J Physiol Heart Circ Physiol, June 1, 2002; 282(6): H2309 - H2315. [Abstract] [Full Text] [PDF]
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