Evidence map›Paper›PMID 10085231›Full record

ArticleThe Biochemical journal1999

Characterization of the regulation of phospholipase D activity in the detergent-insoluble fraction of HL60 cells by protein kinase C and small G-proteins.

M N Hodgkin, J M Clark, S Rose, K Saqib, M J Wakelam

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. 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
2.3field-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

14 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Structure and regulation of human phospholipase D.Advances in biological regulation · 2021
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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

5 authors at 1 institution in 1 country.

M N HodgkinBirmingham Institute of Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TA, UK. m.hodgkin@bham.ac.uk
J M Clark
S Rose
K Saqib
M J Wakelam
Cancer Research UK Clinical Trials Unit · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Phospholipase D (PLD) activity has been shown to be GTP-dependent both in vivo and in vitro. One protein that confers GTP sensitivity to PLD activity in vitro is the low-molecular-mass G-protein ADP-ribosylation factor (Arf). However, members of the Rho family and protein kinase C (PKC) have also been reported to activate PLD in various cell systems. We have characterized the stimulation of PLD in HL60 cell membranes by these proteins. The results demonstrate that a considerable proportion of HL60 PLD activity is located in a detergent-insoluble fraction of the cell membrane that is unlikely to be a caveolae-like domain, but is probably cytoskeletal. This PLD activity required the presence of Arf1, a Rho-family member and PKC for efficient catalysis of the lipid substrate, suggesting that the activity represents PLD1. We show that recombinant human PLD1b is regulated in a similar manner to HL60-membrane PLD, and that PKCalpha and PKCdelta are equally effective PLD activators. Therefore maximum PLD activity requires Arf, a Rho-family member and PKC, emphasizing the high degree of regulation of this enzyme.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsCell MembraneCloning, MolecularDetergentsEnzyme ActivationGTP-Binding ProteinsHL-60 CellsHumansPhospholipase DProtein Kinase CRecombinant Fusion ProteinsSolubilityADP-Ribosylation Factor 1ADP-Ribosylation FactorsDetergentsGTP-Binding ProteinsPhospholipase DProtein Kinase CRecombinant Fusion Proteins

Identifiers

PMID10085231
PMCPMC1220131
OpenAlexW2014673107

What OpenQuestion holds

Texttitle and abstract
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.