Evidence map›Paper›PMID 30976100›Full record

ArticleScientific reports2019

The secreted Ly6/uPAR-related protein-1 suppresses neutrophil binding, chemotaxis, and transmigration through human umbilical vein endothelial cells.

Sudha Swamynathan, Anil Tiwari, Chelsea L Loughner, John Gnalian, Nicholas Alexander, Vishal Jhanji, Shivalingappa K Swamynathan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 16 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 1 institution in 1 country.

Sudha SwamynathanDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
Anil TiwariDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
Chelsea L LoughnerDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
John GnalianDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
Nicholas AlexanderDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
Vishal JhanjiDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA.
Shivalingappa K SwamynathanDepartment of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, USA. Swamynathansk@upmc.edu.ORCID http://orcid.org/0000-0002-9158-1511
University of Pittsburgh · US

Funding

Virus Production and Manipulation of Protein/Gene Expression ModuleP30EY008098 · NEI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Ian A Sigal · 1989 to 2026
$17.8M
Corneal Expression and Function of Slurp1R01EY022898 · NEI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SWAMYNATHAN, SHIVALINGAPPA KOTTUR · 2013 to 2016
$1.5M
NEI NIH HHS P30 EY008098NEI NIH HHS R01 EY022898
6 · The paper itself

Abstract

The secreted Ly-6/uPAR Related Protein-1 (SLURP1) is an immunomodulatory protein that promotes corneal immune- and angiogenic-privilege. Here, we have examined the influence of SLURP1 on neutrophil-vascular endothelial cell interactions using human umbilical vein endothelial cells (HUVEC) and differentiated neutrophil-like HL-60 (dHL-60) cells, or primary human neutrophils. SLURP1 blocked the tumor necrosis factor-alpha (TNF-α)-activated dHL-60 cells (i) binding to TNF-α-activated HUVEC with a concurrent reduction in endothelial cell adhesion molecule E-selectin, (ii) transmigration through TNF-α-activated confluent HUVEC monolayer by stabilizing VE-cadherin and β-catenin on endothelial cell cytoplasmic membranes, (iii) chemotaxis towards chemoattractant formyl Met-Leu-Phe (fMLP) coupled with their decreased polarization, and (iv) TNF-α-stimulated matrix metalloproteinase-9 (MMP9) expression and activity. SLURP1 also suppressed the primary human neutrophil chemotaxis, and interaction with HUVEC. Furthermore, SLURP1 suppressed fMLP-induced phosphorylation of protein kinase-B (AKT) in dHL-60 cells. Collectively, these results provide evidence that SLURP1 suppresses neutrophil (i) docking on HUVEC cells by decreasing endothelial cell adhesion molecule E-Selectin production, (ii) transmigration through HUVEC monolayer by stabilizing endothelial cell membrane localization of VE-cadherin and β-catenin complex and promoting their barrier function, and (iii) chemotaxis by modulating their polarization and TNF-α-stimulated MMP9 production.

Indexed as

Cell AdhesionCell MovementChemotaxis, LeukocyteAntigens, LyE-SelectinHL-60 CellsHumansHuman Umbilical Vein Endothelial CellsNeutrophilsUrokinase-Type Plasminogen ActivatorAntigens, LyE-SelectinSELE protein, humanSLURP1 protein, humanUrokinase-Type Plasminogen Activator

Identifiers

PMID30976100
PMCPMC6459912
OpenAlexW2937121402

What OpenQuestion holds

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Registered trials

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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.