Evidence map›Paper›PMID 24675526›Full record

ArticleOncotarget2014

Endothelial integrin α3β1 stabilizes carbohydrate-mediated tumor/endothelial cell adhesion and induces macromolecular signaling complex formation at the endothelial cell membrane.

Olga V Glinskii, Feng Li, Landon S Wilson, Stephen Barnes, Kate Rittenhouse-Olson, Joseph J Barchi, Kenneth J Pienta, Vladislav V Glinsky

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-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

16 citing papers in PubMed, 30 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

8 authors at 7 institutions in 1 country.

Olga V GlinskiiResearch Service, Harry S. Truman Memorial Veterans Hospital, Columbia, MO.
Feng Li
Landon S Wilson
Stephen Barnes
Kate Rittenhouse-Olson
Joseph J Barchi
Kenneth J Pienta
Vladislav V Glinsky
Harry S. Truman Memorial Veterans' Hospital · USBuffalo State University · USCenter for Cancer Research · USJohns Hopkins University · USUniversity at Buffalo, State University of New York · USUniversity of Alabama at Birmingham · USUniversity of Missouri · US

Funding

Glycopeptide Antigen-bearing Nanoparticles for Passive and Active Antitumor Therapy for Pancreatic CancerZIABC010451 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BARCHI, JOSEPH JOHN · 2009 to 2025
$8.0M
Clinical Translation of an Anti-Metastatic Antibody for Breast Cancer TherapyR42CA176951 · NCI · FOR-ROBIN · PI RITTENHOUSE-OLSON, KATE W · 2015 to 2016
$2.0M
Intravascular Integrin - Mediated Steps in Breast Cancer MetastasisR01CA160461 · NCI · UNIVERSITY OF MISSOURI-COLUMBIA · PI GLINSKII, VLADISLAV V · 2013 to 2017
$1.4M
The Role of Beta-Gal Mediated Interactions in Prostate Cancer MetastasisI01BX000609 · VA · HARRY S. TRUMAN MEMORIAL VA HOSPITAL · PI GLINSKII, VLADISLAV V · 2009 to 2013
–
BLRD VA I01 BX000609NCI NIH HHS R01 CA160461NCI NIH HHS R01CA160461NCI NIH HHS R42 CA176951
6 · The paper itself

Abstract

Blood borne metastatic tumor cell adhesion to endothelial cells constitutes a critical rate-limiting step in hematogenous cancer metastasis. Interactions between cancer associated carbohydrate Thomsen-Friedenreich antigen (TF-Ag) and endothelium-expressed galectin-3 (Gal-3) have been identified as the leading molecular mechanism initiating tumor/endothelial cell adhesion in several types of cancer. However, it is unknown how these rather weak and transient carbohydrate/lectin mediated interactions are stabilized. Here, using Western blot and LC tandem mass spectrometry analyses of pull-downs utilizing TF-Ag loaded gold nanoparticles, we identified Gal-3, endothelial integrin α3β1, Src kinase, as well as 5 additional molecules mapping onto focal adhesion pathway as parts of the macromolecular complexes formed at the endothelial cell membranes downstream of TF-Ag/Gal-3 interactions. In a modified parallel flow chamber assay, inhibiting α3β1 integrin greatly reduced the strength of tumor/endothelial cell interactions without affecting the initial cancer cell adhesion. Further, the macromolecular complex induced by TF-Ag/Gal-3/α3β1 interactions activates Src kinase, p38, and ERK1/2, pathways in endothelial cells in a time- and α3β1-dependent manner. We conclude that, following the initial metastatic cell attachment to endothelial cells mediated by TF-Ag/Gal-3 interactions, endothelial integrin α3β1 stabilizes tumor/endothelial cell adhesion and induces the formation of macromolecular signaling complex activating several major signaling pathways in endothelial cells.

Indexed as

MAP Kinase Signaling SystemAntigens, Tumor-Associated, CarbohydrateCell AdhesionCell Line, TumorCell MembraneEndothelial CellsGalectin 3HumansIntegrin alpha3beta1Macromolecular SubstancesMaleNeoplasm MetastasisProstatic Neoplasmssrc-Family KinasesAntigens, Tumor-Associated, CarbohydrateGalectin 3Integrin alpha3beta1Macromolecular Substancessrc-Family KinasesThomsen-Friedenreich antigen

Identifiers

PMID24675526
PMCPMC4012737
OpenAlexW1848635928

What OpenQuestion holds

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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.