Evidence map›Paper›PMID 8355574›Full record

ArticleLipids1993

Protein kinase C-dependent stimulation of phospholipase D in phospholipase C-treated fibroblasts.

Z Kiss, N Garamszegi

Abstract read
PubMed Publisher
In one paragraph

Article in Lipids, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Z KissHormel Institute, University of Minnesota, Austin 55912.
N Garamszegi
Hormel (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Treatment of [14C]choline- or [14C]ethanolamine-labeled NIH 3T3 fibroblasts with Bacillus cereus phosphatidyl-choline-specific phospholipase C (PLC) enhanced phospholipase D (PLD)-mediated hydrolysis of the respective 14C-labeled phospholipids. PLD activity was stimulated by 1.5 U/mL of PLC and by 100 nM of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) to similar extents. Treatment of [14C]palmitic acid-labeled fibroblasts with PLC in the presence of ethanol also enhanced PLD-mediated formation of phosphatidylethanol; the effects of PLC and PMA were nonadditive. PLC had no effect on PLD activity in fibroblasts in which PKC was down-regulated by prolonged (24 h) treatment with 300 nM PMA. These data indicate that treatment of fibroblasts with exogenous PLC results in PKC-dependent activation of PLD.

Indexed as

3T3 CellsAnimalsCholineDose-Response Relationship, DrugFibroblastsHydrolysisMicePhosphatidylcholinesPhosphatidylethanolaminesPhospholipase DPhospholipidsPhosphorylcholineProtein Kinase CTetradecanoylphorbol AcetateType C PhospholipasesCholinePhosphatidylcholinesPhosphatidylethanolaminesPhospholipase DPhospholipidsPhosphorylcholineProtein Kinase CTetradecanoylphorbol AcetateType C Phospholipases

Identifiers

PMID8355574
OpenAlexW2018566155

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.