[HTML][HTML] Reciprocal regulation of endothelial nitric-oxide synthase by Ca2+-calmodulin and caveolin
The endothelial nitric-oxide synthase (eNOS) is a key determinant of vascular homeostasis.
Like all known nitric-oxide synthases, eNOS enzyme activity is dependent on Ca 2+-
calmodulin. eNOS is dynamically targeted to specialized cell surface signal-transducing
domains termed plasmalemmal caveolae and interacts with caveolin, an integral membrane
protein that comprises a key structural component of caveolae. We have previously reported
that the association between eNOS and caveolin is quantitative and tissue-specific (Feron …
Like all known nitric-oxide synthases, eNOS enzyme activity is dependent on Ca 2+-
calmodulin. eNOS is dynamically targeted to specialized cell surface signal-transducing
domains termed plasmalemmal caveolae and interacts with caveolin, an integral membrane
protein that comprises a key structural component of caveolae. We have previously reported
that the association between eNOS and caveolin is quantitative and tissue-specific (Feron …