The DOI matches its Crossref record; 130 of the 130 references it cites were found in a registry or an index.
Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase
Abstract
The endothelial nitric oxide synthase (eNOS), the expression of which is regulated by a range of transcriptional and posttranscriptional mechanisms, generates nitric oxide (NO) in response to a number of stimuli. The physiologically most important determinants for the continuous generation of NO and thus the regulation of local blood flow are fluid shear stress and pulsatile stretch. Although eNOS activity is coupled to changes in endothelial cell Ca 2+levels, an increase in Ca 2+alone is not sufficient to affect enzyme activity because the binding of calmodulin (CaM) and the flow of electrons from the reductase to the oxygenase domain of the enzyme is dependent on protein phosphorylation and dephosphorylation. Two amino acids seem to be particularly important in regulating eNOS activity and these are a serine residue in the reductase domain (Ser 1177) and a threonine residue (Thr 495) located within the CaM-binding domain. Simultaneous alterations in the phosphorylation of Ser 1177 and Thr 495 in response to a variety of stimuli are regulated by a number of kinases and phosphatases that continuously associate with and dissociate from the eNOS signaling complex. eNOS associated proteins, such as caveolin, heat shock protein 90, eNOS interacting protein, and possibly also motor proteins provide the scaffold for the formation of the protein complex as well as its intracellular localization.
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Cites
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
Self-citationRegulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D., Gratton, J.-P., McCabe, T. J., Fontana, J., Fujio, Y., Walsh, K., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,608
Upregulation of Endothelial Nitric Oxide Synthase by HMG CoA Reductase Inhibitors
Laufs, U., La Fata, V., Plutzky, J., & Liao, J. K. (1998) · Circulation · doi:10.1161/01.cir.97.12.1129 · Cited by 1,839
Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice
Drab, M., Verkade, P., Elger, M., Kasper, M., Lohn, M., Lauterbach, B., Menne, J., Lindschau, C., Mende, F., Luft, F. C., et al. (2001) · Science · doi:10.1126/science.1062688 · Cited by 1,552
Caveolin-1 Null Mice Are Viable but Show Evidence of Hyperproliferative and Vascular Abnormalities
Razani, B., Engelman, J. A., Wang, X. B., Schubert, W., Zhang, X. L., Marks, C. B., Macaluso, F., Russell, R. G., Li, M., Pestell, R. G., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105408200 · Cited by 1,158
Dynamic activation of endothelial nitric oxide synthase by Hsp90
García-Cardeña, G., Fan, R., Shah, V., Sorrentino, R., Cirino, G., Papapetropoulos, A., & Sessa, W. C. (1998) · Nature · doi:10.1038/33934 · Cited by 1,029
Modulation of Akt kinase activity by binding to Hsp90
Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967
AMP‐activated protein kinase phosphorylation of endothelial NO synthase
Chen, Z.-P., Mitchelhill, K. I., Michell, B. J., Stapleton, D., Rodriguez-Crespo, I., Witters, L. A., Power, D. A., Ortiz de Montellano, P. R., & Kemp, B. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01705-0 · Cited by 835
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin
Garcı́a-Cardeña, G., Martasek, P., Masters, B. S. S., Skidd, P. M., Couet, J., Li, S., Lisanti, M. P., & Sessa, W. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25437 · Cited by 821
Acylation Targets Endothelial Nitric-oxide Synthase to Plasmalemmal Caveolae
Shaul, P. W., Smart, E. J., Robinson, L. J., German, Z., Yuhanna, I. S., Ying, Y., Anderson, R. G. W., & Michel, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6518 · Cited by 800
Cited by
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
Balligand, J.-L., Feron, O., & Dessy, C. (2009) · Physiological Reviews · doi:10.1152/physrev.00042.2007 · Cited by 477
Physiological role of ROCKs in the cardiovascular system
Noma, K., Oyama, N., & Liao, J. K. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00459.2005 · Cited by 371
New insights on oxidative stress in the artery wall
STOCKER, R., & KEANEY, J. F. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01370.x · Cited by 188
eNOS phosphorylation in health and disease
Kolluru, G. K., Siamwala, J. H., & Chatterjee, S. (2010) · Biochimie · doi:10.1016/j.biochi.2010.03.020 · Cited by 183
Metadata
- Authors
- Fleming, I., & Busse, R.
- Venue
- American Journal of Physiology-Regulatory, Integrative and Comparative Physiology
- Publisher
- American Physiological Society
- Published
- 2003-01-01
- Volume
- 284
- Issue
- 1
- Pages
- R1-R12
- ISSN
- 0363-6119 (ISSN-L)
- 1522-1490
- OpenAlex
- W2042006175
- Cited by
- 940
- References
- 130
- FWCI
- 37.46
- Type
- journal article
- Language
- en
- Open access
- closed
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