Evidence map›Paper›PMID 26990660›Full record

ArticleCell death and differentiation2016

Identification of a novel agrin-dependent pathway in cell signaling and adhesion within the erythroid niche.

A Anselmo, E Lauranzano, C Soldani, C Ploia, R Angioni, G D'amico, A Sarukhan, C Mazzon, A Viola

Open access · hybridAbstract read
In one paragraph

Article in Cell death and differentiation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. An Agrin-YAP/TAZ Rigidity Sensing Module Drives EGFR-Addicted Lung Tumorigenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  11. Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020
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  20. Ephrin ligands and Eph receptors contribution to hematopoiesis.Cellular and molecular life sciences : CMLS · 2017
    Review
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

9 authors at 4 institutions in 2 countries.

A AnselmoHumanitas Clinical and Research Centre, Rozzano (Milan), Italy.
E LauranzanoHumanitas Clinical and Research Centre, Rozzano (Milan), Italy.
C SoldaniHumanitas Clinical and Research Centre, Rozzano (Milan), Italy.
C PloiaHumanitas Clinical and Research Centre, Rozzano (Milan), Italy.
R AngioniBiomedical Sciences Department, University of Padua, Padua, Italy.
G D'amicoCentro Ricerca Tettamanti, Department of Pediatrics, University of Milano-Bicocca, Fondazione MBBM/San Gerardo Hospital, Monza, Italy.
A SarukhanINSERM, Paris, France.
C MazzonHumanitas Clinical and Research Centre, Rozzano (Milan), Italy.
A ViolaBiomedical Sciences Department, University of Padua, Padua, Italy.
University of Padua · ITHumanitas University · ITInserm · FRUniversity of Milano-Bicocca · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Establishment of cell-cell adhesion is crucial in embryonic development as well as within the stem cell niches of an adult. Adhesion between macrophages and erythroblasts is required for the formation of erythroblastic islands, specialized niches where erythroblasts proliferate and differentiate to produce red blood cells throughout life. The Eph family is the largest known family of receptor tyrosine kinases (RTKs) and controls cell adhesion, migration, invasion and morphology by modulating integrin and adhesion molecule activity and by modifying the actin cytoskeleton. Here, we identify the proteoglycan agrin as a novel regulator of Eph receptor signaling and characterize a novel mechanism controlling cell-cell adhesion and red cell development within the erythroid niche. We demonstrate that agrin induces clustering and activation of EphB1 receptors on developing erythroblasts, leading to the activation of α5β1 integrins. In agreement, agrin knockout mice display severe anemia owing to defective adhesion to macrophages and impaired maturation of erythroid cells. These results position agrin-EphB1 as a novel key signaling couple regulating cell adhesion and erythropoiesis.

Indexed as

AgrinAnimalsCell AdhesionCell SurvivalErythrocytesHyaluronan ReceptorsIntegrin alpha5beta1LDL-Receptor Related ProteinsMegakaryocyte Progenitor CellsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, FluorescencePhosphorylationReceptor, EphB1Receptors, LDLAgrinHyaluronan ReceptorsIntegrin alpha5beta1LDL-Receptor Related ProteinsLrp4 protein, mouseReceptor, EphB1Receptors, LDL

Identifiers

PMID26990660
PMCPMC4947663
OpenAlexW2297413913

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.