Evidence map›Paper›PMID 1599436›Full record

ArticleThe Biochemical journal1992

Synergistic activation of phospholipase D by protein kinase C- and G-protein-mediated pathways in streptolysin O-permeabilized HL60 cells.

B Geny, S Cockcroft

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

19 citing papers in PubMed, 104 citations in OpenAlex.

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  18. Opioid peptides activate phospholipase D and protein kinase C-epsilon in chicken embryo neuron cultures.Proceedings of the National Academy of Sciences of the United States of America · 1993
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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

2 authors at 1 institution in 1 country.

B GenyDepartment of Physiology, University College London, London, U.K.
S Cockcroft
University College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Stimulation of phospholipase D (PLD) by cell surface receptors has been observed in many cell types. We have investigated the mechanism of activation of this enzyme in undifferentiated HL60 cells. GTP analogues and Ca2+ (buffered in the nanomolar to micromolar range) were introduced into HL60 cells in the presence of the permeabilizing agent, streptolysin O. We report that guanosine 5'-[gamma-thio]triphosphate (GTP[S]) is a potent activator of phospholipase D when Ca2+ is available at micromolar levels. Phorbol 12-myristate 13-acetate or Ca2+ alone can also stimulate PLD, but to a limited extent. The activation of PLD by GTP[S] can be partially dissociated from GTP[S]-stimulated phosphoinositide-specific phospholipase C, suggesting that a G-protein may be directly involved in regulating PLD. However, maximal activation of PLD only occurs under conditions that are permissive to phospholipase C stimulation. We conclude that PLD activation is under dual control, i.e. protein kinase C- as well as G-protein-mediated regulation. Synergistic activation occurs when both pathways are simultaneously stimulated. We conclude that full activation of PLD requires protein kinase C, increased Ca2+ and a GTP-binding protein. Evidence for cytosolic components that may also be involved in obtaining full activation of PLD is also presented.

Indexed as

GlycerophospholipidsAdenosine TriphosphateAlkaloidsBacterial ProteinsCell LineCell Membrane PermeabilityDrug SynergismEnzyme ActivationGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)NeomycinPhosphatidic AcidsPhosphatidylcholinesPhospholipase DProtein Kinase CStaurosporineAdenosine TriphosphateAlkaloidsBacterial ProteinsGlycerophospholipidsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)NeomycinPhosphatidic AcidsPhosphatidylcholinesphosphatidylethanolPhospholipase DProtein Kinase CStaurosporinestreptolysin OStreptolysinsTetradecanoylphorbol AcetateType C Phospholipases

Identifiers

PMID1599436
PMCPMC1132670
OpenAlexW2300980569

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.