Evidence map›Paper›PMID 15821758›Full record

ArticleBritish journal of pharmacology2005

The role of intracellular Ca2+ in the regulation of proteinase-activated receptor-2 mediated nuclear factor kappa B signalling in keratinocytes.

Scott R Macfarlane, Callum M Sloss, Pamela Cameron, Toru Kanke, Roderick C McKenzie, Robin Plevin

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Trial
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  13. Article
  14. Trypsin-Like Proteases and Their Role in Muco-Obstructive Lung Diseases.International journal of molecular sciences · 2021
    Review
  15. Article
  16. PAR2 Mediates Itch via TRPV3 Signaling in Keratinocytes.The Journal of investigative dermatology · 2020
    Observational
  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

6 authors at 2 institutions in 1 country.

Scott R MacfarlaneDepartment of Physiology & Pharmacology, University of Strathclyde, Strathclyde Institute for Biomedical Sciences, 27 Taylor Street, Glasgow G4 0NR, Scotland.
Callum M Sloss
Pamela Cameron
Toru Kanke
Roderick C McKenzie
Robin Plevin
University of Strathclyde · GBUniversity of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1 In this study, we examined the role of Ca2+ in linking proteinase-activated receptor-2 (PAR2) to the nuclear factor kappa B (NFkappaB) pathway in a skin epithelial cell line NCTC2544 stably expressing PAR2 (clone G). 2 In clone G, PAR2-mediated NFkappaB luciferase reporter activity and NFkappaB DNA-binding activity was reduced by preincubation with BAPTA-AM but not BAPTA. Trypsin stimulation of inhibitory kappa B kinases, IKKalpha and IKKbeta, was also inhibited following pretreatment with BAPTA-AM. 3 BAPTA/AM also prevented PAR2-mediated IKKalpha activation in cultured primary human keratinocytes. 4 The effect of BAPTA-AM was also selective for the IKK/NFkappaB signalling axis; PAR2 coupling to ERK, or p38 MAP kinase was unaffected. 5 Pharmacological inhibition of the Ca2+-dependent regulatory protein calcineurin did not inhibit trypsin-stimulated IKK activity or NFkappaB-DNA binding; however, inhibition of Ca2+-dependent protein kinase C isoforms or InsP3 formation using GF109203X or the phospholipase C inhibitor U73122, respectively, reduced both IKK activity and NFkappaB-DNA binding. 6 Mutation of PAR2 within the C-terminal to produce a mutant receptor, which does not couple to Ca2+ signalling, but is able to activate ERK, abrogated NFkappaB-DNA binding and IKK activity stimulated by trypsin. 7 These results suggest a predominant role for the InsP3/Ca2+ axis in the regulation of IKK signalling and NFkappaB transcriptional activation.

Indexed as

1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineCalciumCell LineChelating AgentsEgtazic AcidEnzyme InhibitorsEstrenesHumansI-kappa B KinaseIndolesKeratinocytesMaleimidesMitogen-Activated Protein KinasesNF-kappa BOligonucleotidesPhosphodiesterase Inhibitors1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dionebisindolylmaleimide ICalciumChelating AgentsCHUK protein, humanEgtazic AcidEnzyme InhibitorsEstrenesI-kappa B KinaseIKBKB protein, humanIKBKE protein, humanIndolesKN 62MaleimidesMitogen-Activated Protein KinasesNF-kappa BOligonucleotidesPhosphodiesterase InhibitorsProtein Kinase CProtein Serine-Threonine KinasesPyrrolidinonesReceptor, PAR-2TacrolimusTetradecanoylphorbol AcetateTrypsinType C Phospholipases

Identifiers

PMID15821758
PMCPMC1576156
OpenAlexW1547828694

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.