Direct Interaction of Endothelial Nitric-oxide Synthase and Caveolin-1 Inhibits Synthase Activity*
Results obtained show that both N- and C-terminal cytosolic domains of caveolin-1 interact directly with the eNOS oxygenase domain, suggesting that Regulation of eN OS in endothelial cells may involve not only positive allosteric regulation by Ca2+/CaM, but also negative allosterics regulation by caveolini-1.
Reciprocal Phosphorylation and Regulation of Endothelial Nitric-oxide Synthase in Response to Bradykinin Stimulation*
Data suggest that BK activation of eNOS in BAECs primarily involves deinhibition of the enzyme through calcineurin-mediated dephosphorylation at Thr-497, suggesting that Akt activation occurs downstream from phosphatidylinositol 3-kinase.
Identification of Regulatory Sites of Phosphorylation of the Bovine Endothelial Nitric-oxide Synthase at Serine 617 and Serine 635*
- B. MichellM. Harris B. Kemp
- 1 November 2002
Biology, Chemistry
Data show that phosphorylation of both Ser617 and Ser635 regulates eNOS activity and contributes to the agonist-stimulated eN OS activation process.
Interaction of Neuronal Nitric-oxide Synthase with Caveolin-3 in Skeletal Muscle
Interactions between nNOS and caveolin-3 appear to be direct and to involve two distinct caveolin scaffolding/inhibitory domains, which may be a general feature of enzyme docking to caveolin proteins in plasmalemmal caveolae.
Subunit Interactions of Endothelial Nitric-oxide Synthase
Comparative analysis of NOS domain interactions shows that subunit association of eNOS and nNOS involves not only head to head interactions of oxygenase domains but also tail to tail interactions of reductase domains and head to Tail interactions between oxygenase and reduct enzyme domains.
A novel vascular smooth muscle chymase is upregulated in hypertensive rats.
- C. GuoH. JuD. LeungH. MassaeliM. ShiM. Rabinovitch
- 15 March 2001
Biology, Medicine
Spontaneously hypertensive rats show elevated chymase expression and increased chymostatin-inhibitable angiotensin-converting activity, suggesting a possible role for this novel enzyme in the pathophysiology of hypertension.
Regulation of Angiotensin II-induced Phosphorylation of STAT3 in Vascular Smooth Muscle Cells*
- Haiying LiangV. VenemaXiaodan WangH. JuR. VenemaM. Marrero
- 9 July 1999
Biology, Medicine
It is shown that Ang II-induced tyrosine phosphorylation and nuclear translocation of STAT3 in VSMCs is mediated by p60 c-Src, whereas tyrosines dephosphorylation is mediatedBy calcineurin, and that mitogen-activated protein kinase and protein phosphatase 2A (PP2A).
Inhibitory Interactions of the Bradykinin B2 Receptor with Endothelial Nitric-oxide Synthase*
- H. JuV. VenemaM. MarreroR. Venema
- 11 September 1998
Medicine, Chemistry
Reversible and inhibitory membrane-docking interactions of eNOS are not restricted to those with caveolin-1 but also occur with the bradykinin B2 receptor.
Heat-induced increases in endothelial NO synthase expression and activity and endothelial NO release.
- M. B. HarrisM. BlackstoneH. JuV. VenemaR. Venema
- 1 July 2003
Environmental Science, Medicine
It is concluded that prior heat shock is a physical stimulus of increased eNOS expression and is associated with an increase in eN OS activity, agonist-stimulated NO release, and a decreased vasoconstrictor response.
Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation.
- V. VenemaR. ZouH. JuM. MarreroR. Venema
- 9 July 1997
Biology, Medicine
Agonist-activation of eNOS in endothelial cells thus appears to involve tyrosine phosphorylation-dependent changes in the interaction ofeNOS with caveolin-1, which may deactivate the enzyme subsequent to its activation by Ca2+/calmodulin.
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