Evidence map›Paper›PMID 15793303›Full record

ArticleThe American journal of pathology2005

Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia.

Xiu Fen Sui, Timothy D Kiser, Sang Won Hyun, Daniel J Angelini, Robert L Del Vecchio, Bradford A Young, Jeffrey D Hasday, Lewis H Romer, Antonino Passaniti, Nicholas K Tonks and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  4. Remarkable sex-specific differences at single-cell resolution in neonatal hyperoxic lung injury.American journal of physiology. Lung cellular and molecular physiology · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Xiu Fen SuiDepartment of Medicine and Pathology, Division of Infectious Diseases and Pulmonary Medicine, Mucosal Biology Research Center, University of Maryland School of Medicine, 22 Penn St., Baltimore, MD 21201, USA.
Timothy D Kiser
Sang Won Hyun
Daniel J Angelini
Robert L Del Vecchio
Bradford A Young
Jeffrey D Hasday
Lewis H Romer
Antonino Passaniti
Nicholas K Tonks
Simeon E Goldblum
University of Maryland, Baltimore · USCold Spring Harbor Laboratory · USJohns Hopkins Medicine · US

Funding

Tissue Culture Biomechanical CoreP01HL058064 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LAL, RATNESHWAR · 1998 to 2012
$27.8M
Receptor PTPs, Cell Contract and Signal TransductionR01GM055989 · NIGMS · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1997 to 2018
$6.7M
PTP-mu Regulates Lung Endothelial Paracellular PathwayR01HL070155 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI GOLDBLUM, SIMEON EMANUEL · 2002 to 2006
$1.4M
THROMBOSPONDIN 1 OPENS ENDOTHELIAL PARACELLULAR PATHWAYR01HL063217 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI GOLDBLUM, SIMEON EMANUEL · 1999 to 2002
$851k
NHLBI NIH HHS HL58064NHLBI NIH HHS HL63217NHLBI NIH HHS HL70155NHLBI NIH HHS P01 HL058064NHLBI NIH HHS R01 HL070155NIGMS NIH HHS GM55989NIGMS NIH HHS R01 GM055989
6 · The paper itself

Abstract

The pulmonary vascular endothelial paracellular pathway and zonula adherens (ZA) integrity are regulated, in part, through protein tyrosine phosphorylation. ZA-associated protein tyrosine phosphatase (PTP)s are thought to counterregulate tyrosine phosphorylation events within the ZA multiprotein complex. One such receptor PTP, PTPmu, is highly expressed in lung tissue and is almost exclusively restricted to the endothelium. We therefore studied whether PTPmu, in pulmonary vascular endothelia, associates with and/or regulates both the tyrosine phosphorylation state of vascular endothelial (VE)-cadherin and the paracellular pathway. PTPmu was expressed in postconfluent human pulmonary artery and lung microvascular endothelial cells (ECs) where it was almost exclusively restricted to EC-EC boundaries. In human lung microvascular ECs, knockdown of PTPmu through RNA interference dramatically impaired barrier function. In immortalized human microvascular ECs, overexpression of wild-type PTPmu enhanced barrier function. PTPmu-VE-cadherin interactions were demonstrated through reciprocal co-immunoprecipitation assays and co-localization with double-label fluorescence microscopy. When glutathione S-transferase-PTPmu was incubated with purified recombinant VE-cadherin, and when glutathione S-transferase-VE-cadherin was incubated with purified recombinant PTPmu, PTPmu directly bound to VE-cadherin. Overexpression of wild-type PTPmu decreased tyrosine phosphorylation of VE-cadherin. Therefore, PTPmu is expressed in human pulmonary vascular endothelia where it directly binds to VE-cadherin and regulates both the tyrosine phosphorylation state of VE-cadherin and barrier integrity.

Indexed as

Blood-Air BarrierCadherinsCapillary PermeabilityCells, CulturedEndothelium, VascularGlutathione TransferaseHumansImmunoblottingLungMicrocirculationPhosphorylationProtein Tyrosine PhosphatasesPulmonary ArteryReceptor-Like Protein Tyrosine Phosphatases, Class 2Reverse Transcriptase Polymerase Chain ReactionCadherinsFAT1 protein, humanGlutathione TransferaseProtein Tyrosine PhosphatasesPTPRM protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 2

Identifiers

PMID15793303
PMCPMC1602370
OpenAlexW2058078164

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.