Evidence map›Paper›PMID 10861248›Full record

ArticleThe Biochemical journal2000

Inhibition of Ca(2+) signalling by p130, a phospholipase-C-related catalytically inactive protein: critical role of the p130 pleckstrin homology domain.

H Takeuchi, M Oike, H F Paterson, V Allen, T Kanematsu, Y Ito, C Erneux, M Katan, M Hirata

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  9. Article
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  12. Calcium signalling in early embryos.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008
    Review
  13. Article
  14. Phospholipase C-related inactive protein is involved in trafficking of gamma2 subunit-containing GABA(A) receptors to the cell surface.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains.Protein science : a publication of the Protein Society · 2003
    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 1 institution in 1 country.

H TakeuchiDepartment of Biochemistry, Faculty of Dentistry, Kyushu University and Kyushu University Station for Collaborative Research, Fukuoka 812-8582, Japan.
M Oike
H F Paterson
V Allen
T Kanematsu
Y Ito
C Erneux
M Katan
M Hirata
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p130 was originally identified as an Ins(1,4,5)P(3)-binding protein similar to phospholipase C-delta but lacking any phospholipase activity. In the present study we have further analysed the interactions of p130 with inositol compounds in vitro. To determine which of the potential ligands interacts with p130 in cells, we performed an analysis of the cellular localization of this protein, the isolation of a protein-ligand complex from cell lysates and studied the effects of p130 on Ins(1,4,5)P(3)-mediated Ca(2+) signalling by using permeabilized and transiently or stably transfected COS-1 cells (COS-1(p130)). In vitro, p130 bound Ins(1,4,5)P(3) with a higher affinity than that for phosphoinositides. When the protein was isolated from COS-1(p130) cells by immunoprecipitation, it was found to be associated with Ins(1,4,5)P(3). Localization studies demonstrated the presence of the full-length p130 in the cytoplasm of living cells, not at the plasma membrane. In cell-based assays, p130 had an inhibitory effect on Ca(2+) signalling. When fura-2-loaded COS-1(p130) cells were stimulated with bradykinin, epidermal growth factor or ATP, it was found that the agonist-induced increase in free Ca(2+) concentration, observed in control cells, was inhibited in COS-1(p130). This inhibition was not accompanied by the decreased production of Ins(1,4,5)P(3); the intact p130 pleckstrin homology domain, known to be the ligand-binding site in vitro, was required for this effect in cells. These results suggest that Ins(1,4,5)P(3) could be the main p130 ligand in cells and that this binding has the potential to inhibit Ins(1,4,5)P(3)-mediated Ca(2+) signalling.

Indexed as

3T3 CellsAdenosine TriphosphateAnimalsBlood ProteinsBradykininCalciumCalcium ChannelsCarrier ProteinsCatalysisCell LineCell MembraneCOS CellsCytoplasmDogsDose-Response Relationship, DrugEpidermal Growth FactorAdenosine TriphosphateBlood ProteinsBradykininCalciumCalcium ChannelsCarrier ProteinsEpidermal Growth FactorGreen Fluorescent ProteinsInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsLigandsLiposomesLuminescent ProteinsPhosphoproteinsplatelet protein P47Plcl1 protein, ratReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsType C Phospholipases

Identifiers

PMID10861248
PMCPMC1221157
OpenAlexW2067173516

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.