Evidence map›Paper›PMID 24704826›Full record

ArticleOncogene2015

ICAM-2 confers a non-metastatic phenotype in neuroblastoma cells by interaction with α-actinin.

J M Feduska, S G Aller, P L Garcia, S L Cramer, L N Council, R C A M van Waardenburg, K J Yoon

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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  5. Biomedicines · 2023
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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.

J M FeduskaDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL, USA.
S G AllerDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL, USA.
P L GarciaDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL, USA.
S L CramerDepartment of Pediatrics, University of Alabama at Birmingham, Birmingham, AL, USA.
L N CouncilDivision of Anatomic Pathology, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, USA.
R C A M van WaardenburgDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL, USA.
K J YoonDepartment of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL, USA.
University of Alabama at Birmingham · US

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Robert S Welner · 1985 to 2026
$165.9M
NCI NIH HHS P30 CA013148
6 · The paper itself

Abstract

Progressive metastatic disease is a major cause of mortality for patients diagnosed with multiple types of solid tumors. One of the long-term goals of our laboratory is to identify  molecular interactions that regulate metastasis, as a basis for developing agents that inhibit this process. Toward this goal, we recently demonstrated that intercellular adhesion molecule-2 (ICAM-2) converted neuroblastoma (NB) cells from a metastatic to a non-metastatic phenotype, a previously unknown function for ICAM-2. Interestingly, ICAM-2 suppressed metastatic but not tumorigenic potential in preclinical models, supporting a novel mechanism of regulating metastasis. We hypothesized that the effects of ICAM-2 on NB cell phenotype depend on the interaction of ICAM-2 with the cytoskeletal linker protein α-actinin. The goal of the study presented here was to evaluate the impact of α-actinin binding to ICAM-2 on the phenotype of NB tumor cells. We used in silico approaches to examine the likelihood that the cytoplasmic domain of ICAM-2 binds directly to α-actinin. We then expressed variants of ICAM-2 with mutated α-actinin-binding domains, and compared the impact of ICAM-2 and each variant on NB cell adhesion, migration, anchorage-independent growth, co-precipitation with α-actinin and production of localized and disseminated tumors in vivo. The in vitro and in vivo characteristics of cells expressing ICAM-2 variants with modified α-actinin-binding domains differed from cells expressing ICAM-2 wild type (WT) and also from cells that expressed no detectable ICAM-2. Like the WT protein, ICAM-2 variants inhibited cell adhesion, migration and colony growth in vitro. However, unlike the WT protein, ICAM-2 variants did not completely suppress development of disseminated NB tumors in vivo. The data suggest the presence of α-actinin-dependent and α-actinin-independent mechanisms, and indicate that the interaction of ICAM-2 with α-actinin is critical to conferring an ICAM-2-mediated non-metastatic phenotype in NB cells.

Indexed as

ActinsAnimalsAntigens, CDBinding SitesCell AdhesionCell Adhesion MoleculesCell Line, TumorFemaleHumansMiceMice, SCIDModels, MolecularMutationNeoplasm MetastasisNeuroblastomaProtein BindingActinsAntigens, CDCell Adhesion MoleculesICAM2 protein, humanICAM-2 protein, mouse

Identifiers

PMID24704826
PMCPMC6746311
OpenAlexW2020722780

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.