Evidence map›Paper›PMID 18641368›Full record

ArticleBlood2008

Identification of FcgammaRIIa as the ITAM-bearing receptor mediating alphaIIbbeta3 outside-in integrin signaling in human platelets.

Brian Boylan, Cunji Gao, Vipul Rathore, Joan C Gill, Debra K Newman, Peter J Newman

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

93 citing papers in PubMed, 178 citations in OpenAlex.

  1. Trial
  2. Observational
  3. Article
  4. Article
  5. Review
  6. Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026
    Review
  7. Article
  8. Article
  9. Beyond hemostasis, the immunomodulatory nature of platelets.Research and practice in thrombosis and haemostasis · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Platelets in Alcohol-Associated Liver Disease: Interaction With Neutrophils.Cellular and molecular gastroenterology and hepatology · 2024
    Review
  18. Integrin βNature communications · 2023
    Article
  19. Review
  20. Review

33 more citing papers are in PubMed but not listed here.

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 3 countries.

Brian BoylanBlood Research Institute, BloodCenter of Wisconsin, Milwaukee, USA.
Cunji Gao
Vipul Rathore
Joan C Gill
Debra K Newman
Peter J Newman
Versiti Blood Center of Wisconsin · USCzech Academy of Sciences, Institute of Microbiology · CZInstitut de Biologie Moléculaire et Cellulaire · FR

Funding

Transgenic/Knockout CoreP01HL044612 · NHLBI · VERSITI WISCONSIN, INC. · PI NEWMAN, PETER J · 1990 to 2015
$33.4M
NHLBI NIH HHS HL-44612NHLBI NIH HHS P01 HL044612
6 · The paper itself

Abstract

Immunoreceptor tyrosine-based activation motif (ITAM)-containing proteins have recently been demonstrated in macrophages and neutrophils to be required for cell surface integrins to transmit activation signals into the cell. To identify ITAM-bearing proteins that mediate signaling via the platelet-specific integrin alphaIIbbeta3, fibrinogen binding was induced by (1) allowing platelets to spread directly on immobilized fibrinogen, or (2) activating the PAR1 thrombin receptor on platelets in suspension. Both initiated strong, ligand binding-dependent tyrosine phosphorylation of the ITAM-bearing platelet Fc receptor, FcgammaRIIa, as well as downstream phosphorylation of the protein tyrosine kinase Syk and activation of phospholipase Cgamma2 (PLCgamma2). Addition of Fab fragments of an FcgammaRIIa-specific monoclonal antibody strongly inhibited platelet spreading on immobilized fibrinogen, as well as downstream tyrosine phosphorylation of FcgammaRIIa, Syk, and PLCgamma2, and platelets from a patient whose platelets express reduced levels of FcgammaRIIa exhibited markedly reduced spreading on immobilized fibrinogen. Finally, fibrinogen binding-induced FcgammaRIIa phosphorylation did not occur in human platelets expressing a truncated beta3 cytoplasmic domain. Taken together, these data suggest that ligand binding to platelet alphaIIbbeta3 induces integrin cytoplasmic domain-dependent phosphorylation of FcgammaRIIa, which then enlists selected components of the immunoreceptor signaling cascade to transmit amplification signals into the cell.

Indexed as

Signal TransductionAmino Acid MotifsBlood PlateletsCell LineCell MovementChildFibrinogenHumansIntracellular Signaling Peptides and ProteinsLigandsPhospholipase C gammaPhosphorylationPlatelet ActivationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein Structure, TertiaryProtein-Tyrosine KinasesFc gamma receptor IIAFibrinogenIntracellular Signaling Peptides and ProteinsLigandsPhospholipase C gammaPlatelet Glycoprotein GPIIb-IIIa ComplexProtein-Tyrosine KinasesReceptors, IgGSyk KinaseSYK protein, human

Identifiers

PMID18641368
PMCPMC2556613
OpenAlexW2075363343

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.