Evidence map›Paper›PMID 23530036›Full record

Trial reportThe Journal of biological chemistry2013

Discoidin domain receptor 1 protein is a novel modulator of megakaryocyte-collagen interactions.

Vittorio Abbonante, Cristian Gruppi, Diana Rubel, Oliver Gross, Remigio Moratti, Alessandra Balduini

Open access · hybridAbstract readClinical Trial
In one paragraph

Trial report in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

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  14. Imaging platelet biogenesis in vivo.Research and practice in thrombosis and haemostasis · 2018
    Review
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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

6 authors at 3 institutions in 2 countries.

Vittorio AbbonanteBiotechnology Research Laboratories, Department of Molecular Medicine, Istituto di Ricerca e Cura a Carattere Scientifico (IRCCS) San Matteo Foundation, University of Pavia, 27100 Pavia, Italy.
Cristian GruppiBiotechnology Research Laboratories, Department of Molecular Medicine, Istituto di Ricerca e Cura a Carattere Scientifico (IRCCS) San Matteo Foundation, University of Pavia, 27100 Pavia, Italy.
Diana RubelDepartment of Nephrology and Rheumatology, University Medical Center Goettingen, 37075 Goettingen, Germany.
Oliver GrossDepartment of Nephrology and Rheumatology, University Medical Center Goettingen, 37075 Goettingen, Germany.
Remigio MorattiBiotechnology Research Laboratories, Department of Molecular Medicine, Istituto di Ricerca e Cura a Carattere Scientifico (IRCCS) San Matteo Foundation, University of Pavia, 27100 Pavia, Italy.
Alessandra BalduiniBiotechnology Research Laboratories, Department of Molecular Medicine, Istituto di Ricerca e Cura a Carattere Scientifico (IRCCS) San Matteo Foundation, University of Pavia, 27100 Pavia, Italy; Department of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155. Electronic address: alessandra.balduini@unipv.it.
University of Pavia · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITTufts University · US

Funding

In vitro bioreactor system for platelet formationR01EB016041 · NIBIB · TUFTS UNIVERSITY MEDFORD · PI BALDUINI, ALESSANDRA, KAPLAN, DAVID L. · 2012 to 2020
$2.7M
NIBIB NIH HHS 1R01 EB016041-01NIBIB NIH HHS R01 EB016041
6 · The paper itself

Abstract

Growing evidence demonstrates that extracellular matrices regulate many aspects of megakaryocyte (MK) development; however, among the different extracellular matrix receptors, integrin α2β1 and glycoprotein VI are the only collagen receptors studied in platelets and MKs. In this study, we demonstrate the expression of the novel collagen receptor discoidin domain receptor 1 (DDR1) by human MKs at both mRNA and protein levels and provide evidence of DDR1 involvement in the regulation of MK motility on type I collagen through a mechanism based on the activity of SHP1 phosphatase and spleen tyrosine kinase (Syk). Specifically, we demonstrated that inhibition of DDR1 binding to type I collagen, preserving the engagement of the other collagen receptors, glycoprotein VI, α2β1, and LAIR-1, determines a decrease in MK migration due to the reduction in SHP1 phosphatase activity and consequent increase in the phosphorylation level of its main substrate Syk. Consistently, inhibition of Syk activity restored MK migration on type I collagen. In conclusion, we report the expression and function of a novel collagen receptor on human MKs, and we point out that an increasing level of complexity is necessary to better understand MK-collagen interactions in the bone marrow environment.

Indexed as

CD36 AntigensCell MovementCollagen Type IDiscoidin Domain Receptor 1FemaleHumansIntegrin alpha2beta1Intracellular Signaling Peptides and ProteinsMaleMegakaryocytesProtein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 6Receptor Protein-Tyrosine KinasesReceptors, ImmunologicRNA, MessengerSyk KinaseCD36 AntigensCollagen Type IDDR1 protein, humanDiscoidin Domain Receptor 1Integrin alpha2beta1Intracellular Signaling Peptides and Proteinsleukocyte-associated immunoglobulin-like receptor 1Protein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 6Receptor Protein-Tyrosine KinasesReceptors, ImmunologicRNA, MessengerSyk KinaseSYK protein, humanBone MarrowDiscoidin Domain Receptor 1Extracellular MatrixHematopoiesisMegakaryocytesPhosphataseReceptors

Identifiers

PMID23530036
PMCPMC3675607
OpenAlexW2062473792

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.