Evidence map›Paper›PMID 23960082›Full record

ArticleThe Journal of biological chemistry2013

Tyrosine phosphorylation on spleen tyrosine kinase (Syk) is differentially regulated in human and murine platelets by protein kinase C isoforms.

Lorena Buitrago, Dheeraj Bhavanasi, Carol Dangelmaier, Bhanu Kanth Manne, Rachit Badolia, Alessandra Borgognone, Alexander Y Tsygankov, Steven E McKenzie, Satya P Kunapuli

Open access · hybridAbstract read
In one paragraph

Article 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Suppressed ORAI1-STIM1-dependent CaThe Journal of biological chemistry · 2024
    Article
  3. Article
  4. Article
  5. mTOR regulates GPVI-mediated platelet activation.Journal of translational medicine · 2021
    Article
  6. Article
  7. Feedback Regulation of Syk by Protein Kinase C in Human Platelets.International journal of molecular sciences · 2019
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. 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

9 authors at 3 institutions in 2 countries.

Lorena BuitragoFrom the Department of Physiology.
Dheeraj Bhavanasi
Carol Dangelmaier
Bhanu Kanth Manne
Rachit Badolia
Alessandra Borgognone
Alexander Y Tsygankov
Steven E McKenzie
Satya P Kunapuli
Thrombosis Research Institute · GBThomas Jefferson University · USUniversity of Birmingham · GB

Funding

Functional PKC Isoforms in PlateletsR01HL093231 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 2009 to 2017
$3.6M
Regulation and function of PDK1-Akt-Pyk2 axis in plateletsR01HL118593 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KUNAPULI, SATYA P. · 2013 to 2016
$1.9M
NHLBI NIH HHS HL 93231NHLBI NIH HHS R01 HL093231NHLBI NIH HHS R01 HL118593
6 · The paper itself

Abstract

Protein kinase C (PKC) isoforms differentially regulate platelet functional responses downstream of glycoprotein VI (GPVI) signaling, but the role of PKCs regulating upstream effectors such as Syk is not known. We investigated the role of PKC on Syk tyrosine phosphorylation using the pan-PKC inhibitor GF109203X (GFX). GPVI-mediated phosphorylation on Syk Tyr-323, Tyr-352, and Tyr-525/526 was rapidly dephosphorylated, but GFX treatment inhibited this dephosphorylation on Tyr-525/526 in human platelets but not in wild type murine platelets. GFX treatment did not affect tyrosine phosphorylation on FcRγ chain or Src family kinases. Phosphorylation of Lat Tyr-191 and PLCγ2 Tyr-759 was also increased upon treatment with GFX. We evaluated whether secreted ADP is required for such dephosphorylation. Exogenous addition of ADP to GFX-treated platelets did not affect tyrosine phosphorylation on Syk. FcγRIIA- or CLEC-2-mediated Syk tyrosine phosphorylation was also potentiated with GFX in human platelets. Because potentiation of Syk phosphorylation is not observed in murine platelets, PKC-deficient mice cannot be used to identify the PKC isoform regulating Syk phosphorylation. We therefore used selective inhibitors of PKC isoforms. Only PKCβ inhibition resulted in Syk hyperphosphorylation similar to that in platelets treated with GFX. This result indicates that PKCβ is the isoform responsible for Syk negative regulation in human platelets. In conclusion, we have elucidated a novel pathway of Syk regulation by PKCβ in human platelets.

Indexed as

Adenosine DiphosphateAnimalsBlood PlateletsEnzyme ActivationFeedback, PhysiologicalHumansIntracellular Signaling Peptides and ProteinsIsoenzymesLectins, C-TypeMembrane GlycoproteinsMiceMice, Inbred C57BLPhospholipase C gammaPhosphorylationPhosphotyrosinePlatelet AggregationAdenosine DiphosphateCLEC2B protein, humanIntracellular Signaling Peptides and ProteinsIsoenzymesLectins, C-TypeMembrane GlycoproteinsPhospholipase C gammaPhosphotyrosineProtein Kinase C betaProtein Kinase InhibitorsProtein-Tyrosine KinasesReceptors, FcSyk KinaseSYK protein, humanSyk protein, mouseGPVIPhosphotyrosine SignalingPlateletsProtein Kinase C (PKC)Protein PhosphorylationProtein-tyrosine Kinase (Tyrosine Kinase)Syk

Identifiers

PMID23960082
PMCPMC3790015
OpenAlexW2000937700

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.