Evidence map›Paper›PMID 27588738›Full record

ArticleCell adhesion & migration2017

Fibronectin induces macrophage migration through a SFK-FAK/CSF-1R pathway.

Graziana Digiacomo, Ignazia Tusa, Marina Bacci, Maria Grazia Cipolleschi, Persio Dello Sbarba, Elisabetta Rovida

Open access · goldAbstract read
In one paragraph

Article in Cell adhesion & migration, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. Pooled it
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  12. The integrin adhesome and control of anti-tumour immunity.Biochemical Society transactions · 2024
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  20. IncreasedLife (Basel, Switzerland) · 2023
    Article
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

6 authors at 1 institution in 1 country.

Graziana Digiacomoa Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
Ignazia Tusaa Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
Marina Baccia Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
Maria Grazia Cipolleschia Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
Persio Dello Sbarbaa Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
Elisabetta Rovidaa Department of Experimental and Clinical Biomedical Sciences , Università degli Studi di Firenze and Istituto Toscano Tumori , Florence , Italy.
University of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrins, following binding to proteins of the extracellular matrix (ECM) including collagen, laminin and fibronectin (FN), are able to transduce molecular signals inside the cells and to regulate several biological functions such as migration, proliferation and differentiation. Besides activation of adaptor molecules and kinases, integrins transactivate Receptor Tyrosine Kinases (RTK). In particular, adhesion to the ECM may promote RTK activation in the absence of growth factors. The Colony-Stimulating Factor-1 Receptor (CSF-1R) is a RTK that supports the survival, proliferation, and motility of monocytes/macrophages, which are essential components of innate immunity and cancer development. Macrophage interaction with FN is recognized as an important aspect of host defense and wound repair. The aim of the present study was to investigate on a possible cross-talk between FN-elicited signals and CSF-1R in macrophages. FN induced migration in BAC1.2F5 and J774 murine macrophage cell lines and in human primary macrophages. Adhesion to FN determined phosphorylation of the Focal Adhesion Kinase (FAK) and Src Family Kinases (SFK) and activation of the SFK/FAK complex, as witnessed by paxillin phosphorylation. SFK activity was necessary for FAK activation and macrophage migration. Moreover, FN-induced migration was dependent on FAK in either murine macrophage cell lines or human primary macrophages. FN also induced FAK-dependent/ligand-independent CSF-1R phosphorylation, as well as the interaction between CSF-1R and β1. CSF-1R activity was necessary for FN-induced macrophage migration. Indeed, genetic or pharmacological inhibition of CSF-1R prevented FN-induced macrophage migration. Our results identified a new SFK-FAK/CSF-1R signaling pathway that mediates FN-induced migration of macrophages.

Indexed as

Cell MovementSignal TransductionAnimalsCytoskeletonEnzyme ActivationFibronectinsFocal Adhesion Protein-Tyrosine KinasesHumansMacrophagesMiceModels, BiologicalNIH 3T3 CellsPhosphorylationReceptor, Macrophage Colony-Stimulating Factorsrc-Family KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesReceptor, Macrophage Colony-Stimulating Factorsrc-Family Kinasesfibronectinmigrationmonocytes/macrophagesprotein kinasesreceptor tyrosine kinasesignal transduction

Identifiers

PMID27588738
PMCPMC5569968
OpenAlexW2516287451

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.