Cited by 363Nitric Oxide and Endothelin EffectsCoagulation, Bradykinin, Polyphosphates, and AngioedemaProtein Kinase Regulation and GTPase Signaling

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Reciprocal Phosphorylation and Regulation of Endothelial Nitric-oxide Synthase in Response to Bradykinin Stimulation

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Harris, M. Brennan, Ju, Hong, Venema, Virginia J., Liang, Haiying, Zou, Rong, Michell, Belinda J., Chen, Zhi-Ping, Kemp, Bruce E., Venema, Richard C.·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m100229200

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Abstract

Endothelial nitric-oxide synthase (eNOS) is phosphorylated at Ser-1179 (bovine sequence) by Akt after growth factor or shear stress stimulation of endothelial cells, resulting in increased eNOS activity. Purified eNOS is also phosphorylated at Thr-497 by purified AMP-activated protein kinase, resulting in decreased eNOS activity. We investigated whether bradykinin (BK) stimulation of bovine aortic endothelial cells (BAECs) regulates eNOS through Akt activation and Ser-1179 or Thr-497 phosphorylation. Akt is transiently activated in BK-stimulated BAECs. Activation is blocked completely by wortmannin and LY294002, inhibitors of phosphatidylinositol 3-kinase, suggesting that Akt activation occurs downstream from phosphatidylinositol 3-kinase. BK stimulates a transient phosphorylation of eNOS at Ser-1179 that is correlated temporally with a transient dephosphorylation of eNOS at Thr-497. Phosphorylation at Ser-1179, but not dephosphorylation at Thr-497, is blocked by wortmannin and LY294002. BK also stimulates a transient nitric oxide (NO) release from BAECs with a time-course similar to Ser-1179 phosphorylation and Thr-497 dephosphorylation. NO release is not altered by wortmannin. BK-stimulated dephosphorylation of Thr-497 and NO release are blocked by the calcineurin inhibitor, cyclosporin A. These data suggest that BK activation of eNOS in BAECs primarily involves deinhibition of the enzyme through calcineurin-mediated dephosphorylation at Thr-497.

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Authors: Harris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z.-P., Kemp, B. E., & Venema, R. C.
Affiliations: Augusta University (US)
Center for Vascular Biology Research (US)
St Vincents Institute of Medical Research (AU)
Corresponding author: Venema, Richard C.
ORCID: Harris, M. Brennan
Liang, Haiying
Zou, Rong
Kemp, Bruce E.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2001-05
Volume: 276
Issue: 19
Pages: 16587-16591
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m100229200
OpenAlex: W2144179854
Cited by: 363
References: 29
Citations by year: 2026: 1 · 2025: 5 · 2024: 2 · 2023: 2 · 2022: 9 · 2021: 10 · 2020: 3 · 2019: 7 · 2018: 8 · 2017: 9 · 2016: 10 · 2015: 9 · 2014: 13 · 2013: 16 · 2012: 16
FWCI: 18.77
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7089 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL-62152, R01HL062152, HL57201)
Topics: Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Health Sciences › Medicine › Hematology › Coagulation, Bradykinin, Polyphosphates, and Angioedema
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: endothelial nitric oxide synthase, bradykinin, Akt, phosphatidylinositol 3-kinase, calcineurin, cyclosporine, nitric oxide release, endothelial cells, enzyme regulation
MeSH terms: Wortmannin, Androstadienes, Animals, Aorta, Bradykinin, Cattle, Chromones, Endothelium, Vascular, Enzyme Activation, Enzyme Inhibitors, Kinetics, Morpholines, Phosphorylation, Phosphoserine, Phosphothreonine, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Cyclosporine, Protein Serine-Threonine Kinases, Nitric Oxide Synthase, Proto-Oncogene Proteins c-akt, Nitric Oxide Synthase Type III, Calcineurin Inhibitors

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Reciprocal Phosphorylation and Regulation of Endothelial Nitric-oxide Synthase in Response to Bradykinin Stimulation

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