Evidence map›Paper›PMID 23548900›Full record

ArticleThe Journal of biological chemistry2013

Endomembrane H-Ras controls vascular endothelial growth factor-induced nitric-oxide synthase-mediated endothelial cell migration.

Dagmar J Haeussler, David R Pimentel, Xiuyun Hou, Joseph R Burgoyne, Richard A Cohen, Markus M Bachschmid

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Redox RegulationAntioxidants & redox signaling · 2020
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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

6 authors at 3 institutions in 2 countries.

Dagmar J HaeusslerVascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
David R Pimentel
Xiuyun Hou
Joseph R Burgoyne
Richard A Cohen
Markus M Bachschmid
Center for Vascular Biology Research · USBoston University · USKing's College London · GB

Funding

SIRT1, Polyphenols, and Endothelial OxidantsP01HL068758 · NHLBI · BOSTON MEDICAL CENTER · PI SAHA, ASISH K. · 2003 to 2013
$14.1M
Redox Regulation of p21ras in AngiogenesisR37HL104017 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COHEN, RICHARD A · 2010 to 2014
$2.2M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS P01 HL 068758NHLBI NIH HHS P01 HL068758NHLBI NIH HHS R37 HL104017Wellcome Trust 085483/Z/08/Z
6 · The paper itself

Abstract

We demonstrate for the first time that endomembrane-delimited H-Ras mediates VEGF-induced activation of endothelial nitric-oxide synthase (eNOS) and migratory response of human endothelial cells. Using thiol labeling strategies and immunofluorescent cell staining, we found that only 31% of total H-Ras is S-palmitoylated, tethering the small GTPase to the plasma membrane but leaving the function of the large majority of endomembrane-localized H-Ras unexplained. Knockdown of H-Ras blocked VEGF-induced PI3K-dependent Akt (Ser-473) and eNOS (Ser-1177) phosphorylation and nitric oxide-dependent cell migration, demonstrating the essential role of H-Ras. Activation of endogenous H-Ras led to recruitment and phosphorylation of eNOS at endomembranes. The loss of migratory response in cells lacking endogenous H-Ras was fully restored by modest overexpression of an endomembrane-delimited H-Ras palmitoylation mutant. These studies define a newly recognized role for endomembrane-localized H-Ras in mediating nitric oxide-dependent proangiogenic signaling.

Indexed as

Cell MovementCells, CulturedEndothelial CellsEnzyme InductionHumansNeovascularization, PhysiologicNitric Oxide Synthase Type IIIPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktProto-Oncogene Proteins p21(ras)Signal TransductionVascular Endothelial Growth Factor ANitric Oxide Synthase Type IIINOS3 protein, humanPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktProto-Oncogene Proteins p21(ras)Vascular Endothelial Growth Factor AVEGFA protein, humanAngiogenesisCell MigrationEndomembraneH-RasNitric OxideNitric-oxide SynthaseProtein PalmitoylationVascular Endothelial Growth Factor (VEGF)

Identifiers

PMID23548900
PMCPMC3663556
OpenAlexW2046941864

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.