Evidence map›Paper›PMID 26112597›Full record

ArticleCellular and molecular life sciences : CMLS2015

Rab5-mediated VE-cadherin internalization regulates the barrier function of the lung microvascular endothelium.

Junjun Yang, Wei Yao, Guisheng Qian, Zhenghua Wei, Guangyu Wu, Guansong Wang

Open access · bronzeAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

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  9. ADAM10-a "multitasker" in sepsis: focus on its posttranslational target.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023
    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

6 authors at 3 institutions in 2 countries.

Junjun YangInstitute of Respiratory Diseases and Critical Care, Xinqiao Hospital, Third Military Medical University, Chongqing, 400037, China.
Wei YaoInstitute of Respiratory Diseases and Critical Care, Xinqiao Hospital, Third Military Medical University, Chongqing, 400037, China.
Guisheng QianInstitute of Respiratory Diseases and Critical Care, Xinqiao Hospital, Third Military Medical University, Chongqing, 400037, China.
Zhenghua WeiInstitute of Respiratory Diseases and Critical Care, Xinqiao Hospital, Third Military Medical University, Chongqing, 400037, China.
Guangyu WuDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Blvd., Augusta, GA, 30912, USA. guwu@gru.edu.
Guansong WangInstitute of Respiratory Diseases and Critical Care, Xinqiao Hospital, Third Military Medical University, Chongqing, 400037, China. wanggs2003@hotmail.com.
Army Medical University · CNXinqiao Hospital · CNAugusta University · US

Funding

ER-to-Golgi traffic and signal regulation of GPCRsR01GM076167 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WU, GUANGYU · 2006 to 2013
$2.2M
NIGMS NIH HHS GM076167NIGMS NIH HHS R01 GM076167
6 · The paper itself

Abstract

The small GTPase Rab5 has been well defined to control the vesicle-mediated plasma membrane protein transport to the endosomal compartment. However, its function in the internalization of vascular endothelial (VE)-cadherin, an important component of adherens junctions, and as a result regulating the endothelial cell polarity and barrier function remain unknown. Here, we demonstrated that lipopolysaccharide (LPS) simulation markedly enhanced the activation and expression of Rab5 in human pulmonary microvascular endothelial cells (HPMECs), which is accompanied by VE-cadherin internalization. In parallel, LPS challenge also induced abnormal cell polarity and dysfunction of the endothelial barrier in HPMECs. LPS stimulation promoted the translocation of VE-cadherin from the plasma membrane to intracellular compartments, and intracellularly expressed VE-cadherin was extensively colocalized with Rab5. Small interfering RNA (siRNA)-mediated depletion of Rab5a expression attenuated the disruption of LPS-induced internalization of VE-cadherin and the disorder of cell polarity. Furthermore, knockdown of Rab5 inhibited the vascular endothelial hyperpermeability and protected endothelial barrier function from LPS injury, both in vitro and in vivo. These results suggest that Rab5 is a critical mediator of LPS-induced endothelial barrier dysfunction, which is likely mediated through regulating VE-cadherin internalization. These findings provide evidence, implicating that Rab5a is a potential therapeutic target for preventing endothelial barrier disruption and vascular inflammation.

Indexed as

Capillary PermeabilityActin CytoskeletonAnimalsAntigens, CDCadherin 5CadherinsCell PolarityCells, CulturedGene Knockdown TechniquesHumansLungMaleMiceMice, Inbred C57BLrab5 GTP-Binding ProteinsAntigens, CDCadherin 5CadherinsRAB5C protein, humanrab5 GTP-Binding ProteinsActin cytoskeletonAcute lung injuryAdherens junctionBarrier functionCell polarityEndosomeEndotheliumInternalizationRab5 GTPaseVE-cadherin

Identifiers

PMID26112597
PMCPMC4827161
OpenAlexW789594139

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.