Evidence map›Paper›PMID 24753259›Full record

ArticleThe Journal of biological chemistry2014

Binding of CD157 protein to fibronectin regulates cell adhesion and spreading.

Simona Morone, Stefania Augeri, Massimiliano Cuccioloni, Matteo Mozzicafreddo, Mauro Angeletti, Nicola Lo Buono, Alice Giacomino, Erika Ortolan, Ada Funaro

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

17 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

9 authors at 2 institutions in 1 country.

Simona MoroneFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and.
Stefania AugeriFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and.
Massimiliano Cucciolonithe School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Matteo Mozzicafreddothe School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Mauro Angelettithe School of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Nicola Lo BuonoFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and.
Alice GiacominoFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and.
Erika OrtolanFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and.
Ada FunaroFrom the Laboratory of Immunogenetics, Department of Medical Sciences, University of Torino, 10126 Torino and ada.funaro@unito.it.
University of Turin · ITUniversità di Camerino · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CD157/BST-1 behaves both as an ectoenzyme and signaling receptor and is an important regulator of leukocyte trafficking and ovarian cancer progression. However, the molecular interactions underpinning the role of CD157 in these processes remain obscure. The biological functions of CD157 and its partnership with members of the integrin family prompted us to assume the existence of a direct interaction between CD157 and an unknown component of the extracellular matrix. Using solid-phase binding assays and surface plasmon resonance analysis, we demonstrated that CD157 binds fibronectin with high affinity within its heparin-binding domains 1 and 2. Furthermore, we found that CD157 binds to other extracellular matrix proteins containing heparin-binding domains. Finally, we proved that the CD157-fibronectin interaction occurs with living cells, where it elicits CD157-mediated cell responses. Indeed, knockdown of CD157 in Met-5A mesothelial cells changed their morphology and cytoskeleton organization and attenuated the activation of intracellular signaling pathways triggered by fibronectin. This led to impaired cell spreading and adhesion to selected extracellular matrix proteins. Collectively, these findings indicate a central role of CD157 in cell-extracellular matrix interactions and make CD157 an attractive therapeutic target in inflammation and cancer.

Indexed as

ADP-ribosyl CyclaseAntigens, CDCell AdhesionCell DifferentiationCell LineCell MovementEpithelial CellsExtracellular Matrix ProteinsFemaleFibronectinsGPI-Linked ProteinsHumansOvarian NeoplasmsProtein BindingProtein Structure, TertiarySignal TransductionADP-ribosyl CyclaseADP-ribosyl cyclase 2Antigens, CDExtracellular Matrix ProteinsFibronectinsGPI-Linked ProteinsBST-1CD157Cell AdhesionCell Surface ReceptorExtracellular MatrixFibronectinHeparin-binding DomainMembrane Protein

Identifiers

PMID24753259
PMCPMC4140914
OpenAlexW2021046857

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.