Evidence map›Paper›PMID 32616654›Full record

ArticleThe Journal of biological chemistry2020

The NADPH oxidase NOX4 promotes the directed migration of endothelial cells by stabilizing vascular endothelial growth factor receptor 2 protein.

Kei Miyano, Shuichiro Okamoto, Akira Yamauchi, Chikage Kawai, Mizuho Kajikawa, Takuya Kiyohara, Minoru Tamura, Masahiko Taura, Futoshi Kuribayashi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  4. Dynamic regulation of receptor-modulated endothelial NADPH oxidases.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  5. Review
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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

9 authors at 5 institutions in 1 country.

Kei MiyanoDepartment of Biochemistry, Kawasaki Medical School, Okayama, Japan kei-miyano@med.kawasaki-m.ac.jp shuokamoto@med.kawasaki-m.ac.jp.
Shuichiro OkamotoDepartment of Biochemistry, Kawasaki Medical School, Okayama, Japan kei-miyano@med.kawasaki-m.ac.jp shuokamoto@med.kawasaki-m.ac.jp.
Akira YamauchiDepartment of Biochemistry, Kawasaki Medical School, Okayama, Japan.ORCID 0000-0001-9205-6922
Chikage KawaiDepartment of Biochemistry, Kawasaki Medical School, Okayama, Japan.
Mizuho KajikawaLaboratory of Microbiology, Showa Pharmaceutical University, Tokyo, Japan.
Takuya KiyoharaDepartment of Cerebrovascular Disease and Neurology, Hakujyuji Hospital, Fukuoka, Japan.ORCID 0000-0002-8819-1109
Minoru TamuraDepartment of Applied Chemistry, Graduate School of Science and Engineering, Ehime University, Ehime, Japan.
Masahiko TauraDepartment of Otorhinolaryngology, Faculty of Medicine, Fukuoka University, Fukuoka, Japan.
Futoshi KuribayashiDepartment of Biochemistry, Kawasaki Medical School, Okayama, Japan.
Kawasaki Medical School · JPEhime University · JPFukuoka University · JPShowa Pharmaceutical University · JPUji Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Directed migration of endothelial cells (ECs) is an important process during both physiological and pathological angiogenesis. The binding of vascular endothelial growth factor (VEGF) to VEGF receptor-2 (VEGFR-2) on the EC surface is necessary for directed migration of these cells. Here, we used TAXIScan, an optically accessible real-time horizontal cell dynamics assay approach, and demonstrate that reactive oxygen species (ROS)-producing NADPH oxidase 4 (NOX4), which is abundantly expressed in ECs, mediates VEGF/VEGFR-2-dependent directed migration. We noted that a continuous supply of endoplasmic reticulum (ER)-retained VEGFR-2 to the plasma membrane is required to maintain VEGFR-2 at the cell surface. siRNA-mediated NOX4 silencing decreased the ER-retained form of VEGFR-2, resulting in decreased cell surface expression levels of the receptor. We also found that ER-localized NOX4 interacts with ER-retained VEGFR-2 and thereby stabilizes this ER-retained form at the protein level in the ER. We conclude that NOX4 contributes to the directed migration of ECs by maintaining VEGFR-2 levels at their surface.

Indexed as

Cell MovementCell LineEndoplasmic ReticulumEndothelial CellsHeLa CellsHumansNADPH Oxidase 4Protein StabilityReactive Oxygen SpeciesVascular Endothelial Growth Factor Receptor-2KDR protein, humanNADPH Oxidase 4NOX4 protein, humanReactive Oxygen SpeciesVascular Endothelial Growth Factor Receptor-2angiogenesiscapillary formationendoplasmic reticulum (ER)endothelial cell migrationNADPH oxidaseNox4reactive oxygen species (ROS)redox signalingvascular endothelial growth factor receptor 2 (VEGFR-2)

Identifiers

PMID32616654
PMCPMC7450136
OpenAlexW3039787238

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.