Endothelial Nitric-oxide Synthase (Type III) Is Activated and Becomes Calcium Independent upon Phosphorylation by Cyclic Nucleotide-dependent Protein Kinases*

@article{Butt2000EndothelialNS,
  title={Endothelial Nitric-oxide Synthase (Type III) Is Activated and Becomes Calcium Independent upon Phosphorylation by Cyclic Nucleotide-dependent Protein Kinases*},
  author={E. Butt and M. Bernhardt and A. Smolenski and P. Kotsonis and L. Fr{\"o}hlich and A. Sickmann and H. Meyer and S. Lohmann and H. Schmidt},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={5179 - 5187}
}
Endothelial nitric-oxide synthase (NOS-III) is defined as being strictly dependent on Ca2+/calmodulin (CaM) for activity, although NO release from endothelial cells has been reported to also occur at intracellular free Ca2+ levels that are substimulatory for the purified enzyme. We demonstrate here that NOS-III, but neither NOS-I nor -II, is rapidly and strongly activated and phosphorylated on both Ser and Thr in the presence of cGMP-dependent protein kinase II (cGK II) and the catalytic… Expand
Regulation of endothelial nitric oxide synthase by protein kinase C.
Molecular regulation of endothelial nitric oxide synthase.
Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase.
  • I. Fleming, R. Busse
  • Biology, Medicine
  • American journal of physiology. Regulatory, integrative and comparative physiology
  • 2003
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 53 REFERENCES
Signal transduction of eNOS activation.
Phosphorylation and subcellular translocation of endothelial nitric oxide synthase.
  • T. Michel, G. Li, L. Busconi
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1993
An Autoinhibitory Control Element Defines Calcium-regulated Isoforms of Nitric Oxide Synthase*
...
1
2
3
4
5
...