Evidence map›Paper›PMID 28418925›Full record

ArticleOncotarget2017

Syntenin promotes VEGF-induced VEGFR2 endocytosis and angiogenesis by increasing ephrin-B2 function in endothelial cells.

Nara Tae, Suhyun Lee, Okwha Kim, Juhee Park, Sunghun Na, Jeong-Hyung Lee

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  6. MDA-9/Syntenin in the tumor and microenvironment defines prostate cancer bone metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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.

Nara TaeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Suhyun LeeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Okwha KimDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Juhee ParkDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Sunghun NaDepartment of Obstetrics and Gynecology, Kangwon National University Hospital, school of Medicine, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Jeong-Hyung LeeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Gangwon-Do 243-41, Republic of Korea.
Kangwon National University · KRKangwon National University Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syntenin, a tandem PDZ-domain-containing scaffold protein, is involved in the regulation of diverse biological functions, including protein trafficking, exosome biogenesis, and cancer metastasis. Here, we present the first study to explore the significance of syntenin in endothelial cells. Syntenin knockdown in human umbilical vein endothelial cells (HUVECs) impaired vascular endothelial growth factor (VEGF)-mediated proliferation, migration, invasion, vascular permeability, and nitric oxide (NO) production. Syntenin knockdown also suppressed expression of the VEGFR2 target genes VEGF, MMP2, and Nurr77 as well as VEGF-induced angiogenesis in vitro and in vivo. And it decreased cell-surface levels of ephrin-B2. Biochemical analyses revealed that syntenin exists in complex with VEGFR2 and ephrin-B2. Syntenin knockdown abolished the association between VEGFR2 and ephrin-B2, suggesting syntenin functions as a scaffold protein facilitating their association in HUVECs. Consistent with these observations, knocking down syntenin or ephrin-B2 abolished VEGF-induced endocytosis and VEGFR2 phosphorylation and activation of its downstream signaling molecules. Treatment with MG132, a proteasome inhibitor, rescued the downregulation of ephrin-B2 and VEGFR2 signaling induced by syntenin knockdown. These findings demonstrate that syntenin promotes VEGF signaling and, through its PDZ-dependent interaction with ephrin-B2, enhances VEGF-mediated VEGFR2 endocytosis and subsequent downstream signaling and angiogenesis in endothelial cells.

Indexed as

AnimalsCells, CulturedEndocytosisEndothelial CellsEphrin-B2HumansMiceNeovascularization, PathologicSynteninsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2Ephrin-B2SynteninsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2angiogenesisendothelial cellephrin-B2synteninVEGFR2 endocytosis

Identifiers

PMID28418925
PMCPMC5503580
OpenAlexW2602581279

What OpenQuestion holds

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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.