The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Shear stress stimulates phosphorylation of eNOS at Ser635by a protein kinase A-dependent mechanism
Abstract
Shear stress stimulates nitric oxide (NO) production by phosphorylating endothelial NO synthase (eNOS) at Ser 1179 in a phosphoinositide-3-kinase (PI3K)- and protein kinase A (PKA)-dependent manner. The eNOS has additional potential phosphorylation sites, including Ser 116, Thr 497, and Ser 635. Here, we studied these potential phosphorylation sites in response to shear, vascular endothelial growth factor (VEGF), and 8-bromocAMP (8-BRcAMP) in bovine aortic endothelial cells (BAEC). All three stimuli induced phosphorylation of eNOS at Ser 635, which was consistently slower than that at Ser 1179. Thr 497 was rapidly dephosphorylated by 8-BRcAMP but not by shear and VEGF. None of the stimuli phosphorylated Ser 116. Whereas shear-stimulated Ser 635 phosphorylation was not affected by phosphoinositide-3-kinase inhibitors wortmannin and LY-294002, it was blocked by either treating the cells with a PKA inhibitor H89 or infecting them with a recombinant adenovirus-expressing PKA inhibitor. These results suggest that shear stress stimulates eNOS by two different mechanisms: 1) PKA- and PI3K-dependent and 2) PKA-dependent but PI3K-independent pathways. Phosphorylation of Ser 635 may play an important role in chronic regulation of eNOS in response to mechanical and humoral stimuli.
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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
McCabe, T. J., Fulton, D., Roman, L. J., & Sessa, W. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6123 · Cited by 387 · cited 2×
“Phosphorylation of Ser1179 upon challenge with eNOS stimulators is proposed to induce the conformation change of the carboxy-terminal, which removes the wedge and lowers Ca2 requirement leading to enzyme activation (29, 32).”
BackgroundHarris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z.-P., Kemp, B. E., & Venema, R. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100229200 · Cited by 363
Self-citation
Cited by
Vascular nitric oxide: Beyond eNOS
Zhao, Y., Vanhoutte, P. M., & Leung, S. W. S. (2015) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2015.09.002 · Cited by 826
Shear Stress–Initiated Signaling and Its Regulation of Endothelial Function
Zhou, J., Li, Y.-S., & Chien, S. (2014) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.114.303422 · Cited by 561
Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation
Mount, P. F., Kemp, B. E., & Power, D. A. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.05.023 · Cited by 498
Self-citationBalligand, J.-L., Feron, O., & Dessy, C. (2009) · Physiological Reviews · doi:10.1152/physrev.00042.2007 · Cited by 477
Molecular mechanisms of the vascular responses to haemodynamic forces
LEHOUX, S., CASTIER, Y., & TEDGUI, A. (2006) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2006.01624.x · Cited by 447
Metadata
- Authors
- Boo, Y. C., Hwang, J., Sykes, M., Michell, B. J., Kemp, B. E., Lum, H., & Jo, H.
- Venue
- American Journal of Physiology-Heart and Circulatory Physiology
- Publisher
- American Physiological Society
- Published
- 2002-11-01
- Volume
- 283
- Issue
- 5
- Pages
- H1819-H1828
- ISSN
- 0363-6135 (ISSN-L)
- 1522-1539
- OpenAlex
- W2024394653
- Cited by
- 239
- References
- 3
- FWCI
- 6.98
- Type
- journal article
- Language
- en
- Open access
- closed
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- Boo, Y. C., Hwang, J., Sykes, M., Michell, B. J., Kemp, B. E., Lum, H., & Jo, H. (2002). Shear stress stimulates phosphorylation of eNOS at Ser635by a protein kinase A-dependent mechanism. American Journal of Physiology-Heart and Circulatory Physiology. https://doi.org/10.1152/ajpheart.00214.2002
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