Evidence map›Paper›PMID 19946124›Full record

ArticleThe Journal of biological chemistry2010

Beta-actin association with endothelial nitric-oxide synthase modulates nitric oxide and superoxide generation from the enzyme.

Dmitry Kondrikov, Fabio V Fonseca, Shawn Elms, David Fulton, Steven M Black, Edward R Block, Yunchao Su

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.

  1. Pooled it
  2. Epigenomics and transcriptomics association study of blood pressure and incident diagnosis of hypertension in twins.Hypertension research : official journal of the Japanese Society of Hypertension · 2025
    Article
  3. Review
  4. Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Association ofIranian journal of basic medical sciences · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Nitric oxide: what's new to NO?American journal of physiology. Cell physiology · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Endothelial nitric oxide synthase in the microcirculation.Cellular and molecular life sciences : CMLS · 2015
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Dmitry KondrikovDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta, Georgia 30912, USA.
Fabio V Fonseca
Shawn Elms
David Fulton
Steven M Black
Edward R Block
Yunchao Su
Augusta University · USUniversity of Florida · US

Funding

eNOS-actin Interaction and Oxygen in Lung EndotheliumR01HL088261 · NHLBI · UNIVERSITY OF FLORIDA · PI SU, YUNCHAO · 2008 to 2012
$1.8M
NHLBI NIH HHS R01 HL088261NHLBI NIH HHS R01HL088261
6 · The paper itself

Abstract

Protein-protein interactions represent an important post-translational mechanism for endothelial nitric-oxide synthase (eNOS) regulation. We have previously reported that beta-actin is associated with eNOS oxygenase domain and that association of eNOS with beta-actin increases eNOS activity and nitric oxide (NO) production. In the present study, we found that beta-actin-induced increase in NO production was accompanied by decrease in superoxide formation. A synthetic actin-binding sequence (ABS) peptide 326 with amino acid sequence corresponding to residues 326-333 of human eNOS, one of the putative ABSs, specifically bound to beta-actin and prevented eNOS association with beta-actin in vitro. Peptide 326 also prevented beta-actin-induced decrease in superoxide formation and increase in NO and L-citrulline production. A modified peptide 326 replacing hydrophobic amino acids leucine and tryptophan with neutral alanine was unable to interfere with eNOS-beta-actin binding and to prevent beta-actin-induced changes in NO and superoxide formation. Site-directed mutagenesis of the actin-binding domain of eNOS replacing leucine and tryptophan with alanine yielded an eNOS mutant that exhibited reduced eNOS-beta-actin association, decreased NO production, and increased superoxide formation in COS-7 cells. Disruption of eNOS-beta-actin interaction in endothelial cells using ABS peptide 326 resulted in decreased NO production, increased superoxide formation, and decreased endothelial monolayer wound repair, which was prevented by PEG-SOD and NO donor NOC-18. Taken together, this novel finding indicates that beta-actin binding to eNOS through residues 326-333 in the eNOS protein results in shifting the enzymatic activity from superoxide formation toward NO production. Modulation of NO and superoxide formation from eNOS by beta-actin plays an important role in endothelial function.

Indexed as

ActinsAnimalsChlorocebus aethiopsCitrullineCOS CellsHumansImmunoprecipitationMiceMutagenesis, Site-DirectedNitric OxideNitric Oxide Synthase Type IIIPeptidesProtein BindingSuperoxidesActinsCitrullineNitric OxideNitric Oxide Synthase Type IIIPeptidesSuperoxides

Identifiers

PMID19946124
PMCPMC2836036
OpenAlexW2036498436

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.