Evidence map›Paper›PMID 32517158›Full record

ArticleCells2020

Elements of the Endomucin Extracellular Domain Essential for VEGF-Induced VEGFR2 Activity.

Zhengping Hu, Issahy Cano, Kahira L Saez-Torres, Michelle E LeBlanc, Magali Saint-Geniez, Yin-Shan Ng, Pablo Argüeso, Patricia A D'Amore

Abstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Research progress on the structure and function of endomucin.Animal models and experimental medicine · 2020
    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

8 authors.

Zhengping HuSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Issahy CanoSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Kahira L Saez-TorresSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Michelle E LeBlancSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Magali Saint-GeniezSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Yin-Shan NgSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Pablo ArgüesoSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.
Patricia A D'AmoreSchepens Eye Research Institute of Massachusetts Eye and Ear, Boston, MA 02114, USA.

Funding

VISION RESEARCHP30EY003790 · NEI · SCHEPENS EYE RESEARCH INSTITUTE · PI Patricia Ann D'Amore · 1985 to 2026
$25.5M
Training Program in the Molecular Bases of Eye DiseasesT32EY007145 · NEI · SCHEPENS EYE RESEARCH INSTITUTE · PI Patricia Ann D'Amore, MEREDITH GREGORY-KSANDER · 1997 to 2026
$4.5M
Investigation of endomucin as a novel regulator of angiogenesisR01EY026539 · NEI · SCHEPENS EYE RESEARCH INSTITUTE · PI D'AMORE, PATRICIA ANN · 2017 to 2024
$4.1M
NEI NIH HHS P30 EY003790NEI NIH HHS R01 EY026539NEI NIH HHS T32 EY007145
6 · The paper itself

Abstract

Endomucin (EMCN) is the type I transmembrane glycoprotein, mucin-like component of the endothelial cell glycocalyx. We have previously shown that EMCN is necessary for vascular endothelial growth factor (VEGF)-induced VEGF receptor 2 (VEGFR2) internalization and downstream signaling. To explore the structural components of EMCN that are necessary for its function and the molecular mechanism of EMCN in VEGF-induced endothelial functions, we generated a series of mouse EMCN truncation mutants and examined their ability to rescue VEGF-induced endothelial functions in human primary endothelial cells (EC) in which endogenous EMCN had been knocked down using siRNA. Expression of the mouse full-length EMCN (FL EMCN) and the extracellular domain truncation mutants ∆21-81 EMCN and ∆21-121 EMCN, but not the shortest mutant ∆21-161 EMCN, successfully rescued the VEGF-induced EC migration, tube formation, and proliferation. ∆21-161 EMCN failed to interact with VEGFR2 and did not facilitate VEGFR2 internalization. Deletion of COSMC (C1GalT1C1) revealed that the abundant mucin-type

Indexed as

Amino Acid SequenceEndocytosisGlycosylationHumansMutationProtein DomainsSialomucinsSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2SialomucinsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2angiogenesisEMCNglycosylationmucinVEGFVEGFR2

Identifiers

PMID32517158
PMCPMC7349057

What Socratic 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 Socratic graph.