What does this research mean for the field?

Bradykinin activation of endothelial nitric-oxide synthase (eNOS) primarily involves deinhibition of the enzyme through calcineurin-mediated dephosphorylation at Thr-497. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

This research examines how bradykinin stimulates endothelial nitric-oxide synthase (eNOS) through Akt activation and specific phosphorylations.

May 1, 2001Journal of Biological ChemistryOpen Access

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

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Why the study?

Does bradykinin stimulation regulate eNOS activity through Akt activation and specific phosphorylation sites in bovine aortic endothelial cells?

Population

Bovine aortic endothelial cells (BAECs)

Comparison

Bradykinin (BK) stimulation vs Unstimulated cells or cells treated with…

Design

Preclinical

Authors

MHM. Brennan HarrisUniversity of North Carolina at Chapel Hill HJHong JuAnhui University of Technology VVVirginia J. VenemaAugusta University

Discussion

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Implication

May refine eNOS regulation models in endothelial cells; leaves open human translation and therapeutic targeting.

Key Points

This research examines how bradykinin stimulates endothelial nitric-oxide synthase (eNOS) through Akt activation and specific phosphorylations.
Investigated phosphorylation of eNOS at Ser-1179 and Thr-497 in bovine aortic endothelial cells (BAECs) after bradykinin stimulation.
Used wortmannin and LY294002 to analyze Akt activation and its dependence on phosphatidylinositol 3-kinase.
Applied cyclosporin A to assess the role of calcineurin in eNOS regulation.
Bradykinin stimulation transiently activates Akt and phosphorylates eNOS at Ser-1179, while dephosphorylating it at Thr-497.
Akt activation is entirely blocked by phosphatidylinositol 3-kinase inhibitors, confirming its downstream role.
eNOS activity is primarily increased through calcineurin-mediated dephosphorylation at Thr-497.

Structured PICO

Does bradykinin stimulation regulate eNOS activity through Akt activation and specific phosphorylation sites in bovine aortic endothelial cells?

Population

Bovine aortic endothelial cells (BAECs)

Intervention

Bradykinin (BK) stimulation

Comparator

Unstimulated cells or cells treated with inhibitors (wortmannin, LY294002, cyclosporin A)

Outcome

eNOS phosphorylation at Ser-1179 and Thr-497, and nitric oxide (NO) releasesurrogate

Bradykinin activates eNOS in endothelial cells primarily through calcineurin-mediated dephosphorylation at Thr-497, providing mechanistic insight into endothelial nitric oxide regulation.

Cite This Study

Harris et al. (2001) studied this question.

synapsesocial.com/papers/6a1ea83e989adebfe89a6ab7 https://doi.org/10.1074/jbc.m100229200

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

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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