Evidence map›Paper›PMID 18362147›Full record

ArticleThe Journal of biological chemistry2008

Activation of Syk by protein kinase C-delta regulates thrombin-induced intercellular adhesion molecule-1 expression in endothelial cells via tyrosine phosphorylation of RelA/p65.

Kaiser M Bijli, Fabeha Fazal, Mohd Minhajuddin, Arshad Rahman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Cd47-Sirpα interaction and IL-10 constrain inflammation-induced macrophage phagocytosis of healthy self-cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Serpine2 deficiency results in lung lymphocyte accumulation and bronchus-associated lymphoid tissue formation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Kaiser M BijliDepartment of Pediatrics (Neonatology), Lung Biology and Disease Program, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.
Fabeha Fazal
Mohd Minhajuddin
Arshad Rahman
University of Rochester · US

Funding

VISUAL INDICES OF NEUROTOXICITYP30ES001247 · NIEHS · UNIVERSITY OF ROCHESTER · PI Martha Susiarjo · 1985 to 2026
$42.8M
G-protein-induced Signaling of PMN-mediated Lung InjuryR01HL067424 · NHLBI · UNIVERSITY OF ROCHESTER · PI RAHMAN, ARSHAD · 2002 to 2010
$2.3M
NHLBI NIH HHS HL 67424NIEHS NIH HHS ES 01247
6 · The paper itself

Abstract

Protein kinase C-delta (PKC-delta) plays a pivotal role in mediating thrombin-induced NF-kappaB activation and ICAM-1 expression in endothelial cells. However, the downstream mechanisms mediating its function are unclear. In this study, we show that PKC-delta-mediated activation of protein-tyrosine kinase Syk plays an important role in thrombin signaling of NF-kappaB activation and intercellular adhesion molecule-1 (ICAM-1) expression in endothelial cells. Stimulation of human vascular endothelial cells with thrombin resulted in a time-dependent phosphorylation of Syk on tyrosine 525 and 526, an indication of Syk activation. Inhibition of PKC-delta by pharmacological and genetic approaches prevented Syk activation by thrombin. These results place Syk downstream of PKC-delta in transmitting thrombin-activated signaling in endothelial cells. Consistent with this, thrombin-induced NF-kappaB activity and ICAM-1 expression were prevented by the expression of a kinase-defective mutant or RNA interference knockdown of Syk. Similarly, inhibiting Syk also impaired NF-kappaB activity and ICAM-1 expression induced by a constitutively active mutant of PKC-delta. Analysis of the NF-kappaB pathway showed that Syk contributes to thrombin-induced NF-kappaB activation by controlling its transactivation potential and that this response is associated with tyrosine phosphorylation of RelA/p65. Thus, these data unveil a novel pathway in which Syk signals downstream of PKC-delta to mediate thrombin induced ICAM-1 expression in endothelial cells by increasing transcriptional capacity of NF-kappaB via a mechanism that relies on tyrosine phosphorylation of RelA/p65.

Indexed as

Active Transport, Cell NucleusCells, CulturedDNAEndothelial CellsEnzyme ActivationGene Expression RegulationHumansI-kappa B KinaseIntercellular Adhesion Molecule-1Intracellular Signaling Peptides and ProteinsNF-kappa BPhosphotyrosineProtein BindingProtein Kinase C-deltaProtein-Tyrosine KinasesSignal TransductionDNAI-kappa B KinaseIntercellular Adhesion Molecule-1Intracellular Signaling Peptides and ProteinsNF-kappa BPhosphotyrosineProtein Kinase C-deltaProtein-Tyrosine KinasesRELA protein, humanSyk KinaseSYK protein, humanThrombinTranscription Factor RelA

Identifiers

PMID18362147
PMCPMC2386948
OpenAlexW1973256540

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.