Evidence map›Paper›PMID 19477952›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2009

Compartmentalizing VEGF-induced ERK2/1 signaling in placental artery endothelial cell caveolae: a paradoxical role of caveolin-1 in placental angiogenesis in vitro.

Wu-Xiang Liao, Lin Feng, Honghai Zhang, Jing Zheng, Thomas R Moore, Dong-Bao Chen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

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  9. Regulation of heterotrimeric G-protein signaling by NDPK/NME proteins and caveolins: an update.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
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  20. VEGF-induced neoangiogenesis is mediated by NAADP and two-pore channel-2-dependent Ca2+ signaling.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 2 institutions in 1 country.

Wu-Xiang LiaoDepartment of Reproductive Medicine, University of California, San Diego, La Jolla, California 92093, USA.
Lin Feng
Honghai Zhang
Jing Zheng
Thomas R Moore
Dong-Bao Chen
University of California, San Diego · USUniversity of Wisconsin–Madison · US

Funding

Actions of Estrogen on Uterine Artery EndotheliumR01HL070562 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, DONGBAO · 2001 to 2025
$6.3M
EFFECTS OF NITRIC OXIDE ON FETOPLACENTAL ANGIOGENESISR01HL064703 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI ZHENG, JING · 2000 to 2008
$1.9M
Caveolin-1, Caveolae and Placental AngiogenesisR01HL074947 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, DONGBAO · 2004 to 2007
$1.3M
NHLBI NIH HHS HL64703NHLBI NIH HHS HL70562NHLBI NIH HHS HL74947NHLBI NIH HHS R01 HL064703NHLBI NIH HHS R01 HL070562NHLBI NIH HHS R01 HL074947
6 · The paper itself

Abstract

On vascular endothelial growth factor (VEGF) stimulation, both VEGF R1 and R2 receptors were phosphorylated in ovine fetoplacental artery endothelial (oFPAE) cells. Treatment with VEGF stimulated both time- and dose-dependent activation of ERK2/1 in oFPAE cells. VEGF-induced ERK2/1 activation was mediated by VEGFR2, but not VEGFR1, and was linked to intracellular calcium, protein kinase C, and Raf-1. VEGF stimulated oFPAE cell proliferation, migration, and tube formation in vitro. Blockade of ERK2/1 pathway attenuated VEGF-induced cell proliferation and tube formation but failed to inhibit migration in oFPAE cells. Disruption of caveolae by cholesterol depletion with methyl-beta-cyclodextrin or by down-regulation of its structural protein caveolin-1 blunted VEGF-induced ERK2/1 activation, proliferation, and tube formation in oFPAE cells, indicating an essential role of integral caveolae in these VEGF-induced responses. Adenoviral overexpression of caveolin-1 and addition of a caveolin scaffolding domain peptide also inhibited VEGF-stimulated ERK2/1 activation, cell proliferation, and tube formation in oFPAE cells. Furthermore, molecules comprising the ERK2/1 signaling module, including VEGFR2, protein kinase Calpha, Raf-1, MAPK kinase 1/2, and ERK2/1, resided with caveolin-1 in caveolae. VEGF transiently stimulated ERK2/1 activation in the caveolae similarly as in intact cells. Caveolae disruption greatly diminished ERK2/1 activation by VEGF in oFPAE cell caveolae. We conclude that caveolae function as a platform for compartmentalizing the VEGF-induced ERK2/1 signaling module. Caveolin-1 and caveolae play a paradoxical role in regulating VEGF-induced ERK2/1 activation and in vitro angiogenesis as evidenced by the similar inhibitory effects of down-regulation and overexpression of caveolin-1 and disruption of caveolae in oFPAE cells.

Indexed as

Gene Expression Regulation, EnzymologicNeovascularization, PathologicAnimalsArteriesCaveolin 1Endothelial CellsFemaleHumansIn Vitro TechniquesMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Models, BiologicalPlacentaPolymerase Chain ReactionVascular Endothelial Growth Factor ACaveolin 1Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Vascular Endothelial Growth Factor A

Identifiers

PMID19477952
PMCPMC2737550
OpenAlexW1985152241

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.