Evidence map›Paper›PMID 31637713›Full record

ArticleJournal of cellular physiology2020

Podosome formation impairs endothelial barrier function by sequestering zonula occludens proteins.

Yan-Ning Rui, Yawen Chen, Yichen Guo, Caroline E Bock, John P Hagan, Dong H Kim, Zhen Xu

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular physiology, 2020. 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
0.2field-weighted citation impact, top 39% 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, 12 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Yan-Ning RuiDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Yawen ChenDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Yichen GuoDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Caroline E BockDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
John P HaganDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Dong H KimDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.
Zhen XuDepartment of Neurosurgery, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas.ORCID 0000-0002-2190-3861
The University of Texas Health Science Center at Houston · USFirst Affiliated Hospital of Xi'an Jiaotong University · CN

Funding

Role of THSD1 and its Disease Causing Variants in Intracranial AneurysmR01NS104280 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HAGAN, JOHN PATRICK · 2018 to 2022
$1.7M
The Role of Podosomes in Cerebrovascular Integrity and Intracranial AneurysmR01NS126664 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI Zhen Xu · 2023 to 2026
$1.5M
Role of Autophagy in THSD1-Mediated Intracranial AneurysmR21NS108310 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI RUI, YANNING · 2019 to 2019
$425k
NINDS NIH HHS R01 NS104280NINDS NIH HHS R01 NS126664NINDS NIH HHS R21 NS108310
6 · The paper itself

Abstract

Podosomes and tight junctions (TJs) are subcellular compartments that both exist in endothelial cells and localize at cell surfaces. In contrast to the well-characterized role of TJs in maintaining cerebrovascular integrity, the specific function of endothelial podosomes remains unknown. Intriguingly, we discovered cross-talk between podosomes and TJs in human brain endothelial cells. Tight junction scaffold proteins ZO-1 and ZO-2 localize at podosomes in response to phorbol-12-myristate-13-acetate treatment. We found that both ZO proteins are essential for podosome formation and function. Rather than being derived from new protein synthesis, podosomal ZO-1 and ZO-2 are relocated from a pre-existing pool found at the peripheral plasma membrane with enhanced physical interaction with cortactin, a known protein marker for podosomes. Sequestration of ZO proteins in podosomes weakens tight junction complex formation, leading to increased endothelial cell permeability. This effect can be further attenuated by podosome inhibitor PP2. Altogether, our data revealed a novel cellular function of podosomes, specifically, their ability to negatively regulate tight junction and endothelial barrier integrity, which have been linked to a variety of cerebrovascular diseases.

Indexed as

BrainCells, CulturedEndothelial CellsHumansPermeabilityPodosomesProtein MultimerizationProtein TransportTetradecanoylphorbol AcetateTight JunctionsZonula Occludens-1 ProteinZonula Occludens-2 Proteinphorbolol myristate acetateTetradecanoylphorbol AcetateTJP1 protein, humanTJP2 protein, humanZonula Occludens-1 ProteinZonula Occludens-2 Proteincerebrovascular diseasecortactinendothelial barrierPodosometight junctionZO-1ZO-2

Identifiers

PMID31637713
PMCPMC7087352
OpenAlexW2981752115

What OpenQuestion holds

Textmetadata
LicenceTDM
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.