Evidence map›Paper›PMID 22676268›Full record

ArticleBMC biochemistry2012

Phosphatidylcholine formation by LPCAT1 is regulated by Ca(2+) and the redox status of the cell.

Eric Soupene, Frans A Kuypers

Abstract read
In one paragraph

Article in BMC biochemistry, 2012. 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
–field-weighted citation impact
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.

  1. Review
  2. UPLC-ESI-TOF-MS Profiling of Metabolome Alterations in Barley (Journal of agricultural and food chemistry · 2025
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  16. Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
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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.

Eric SoupeneChildren's Hospital Oakland Research Institute, 5700 Martin Luther King Jr, Way, Oakland, CA 94609, USA. esoupene@chori.org
Frans A Kuypers

Funding

Flow lysometry and its biomedical applicationsR21HL092535 · NHLBI · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI KUYPERS, FRANS A. · 2008 to 2009
$440k
NHLBI NIH HHS R21HL092535
6 · The paper itself

Abstract

backgroundUnsaturated fatty acids are susceptible to oxidation and damaged chains are removed from glycerophospholipids by phospholipase A(2). De-acylated lipids are then re-acylated by lysophospholipid acyltransferase enzymes such as LPCAT1 which catalyses the formation of phosphatidylcholine (PC) from lysoPC and long-chain acyl-CoA.

resultsActivity of LPCAT1 is inhibited by Ca(2+), and a Ca(2+)-binding motif of the EF-hand type, EFh-1, was identified in the carboxyl-terminal domain of the protein. The residues Asp-392 and Glu-403 define the loop of the hairpin structure formed by EFh-1. Substitution of D(392) and E(403) to alanine rendered an enzyme insensitive to Ca(2+), which established that Ca(2+) binding to that region negatively regulates the activity of the acyltransferase amino-terminal domain. Residue Cys-211 of the conserved motif III is not essential for catalysis and not sufficient for sensitivity to treatment by sulfhydryl-modifier agents. Among the several active cysteine-substitution mutants of LPCAT1 generated, we identified one to be resistant to treatment by sulfhydryl-alkylating and sulfhydryl-oxidizer agents.

conclusionMutant forms of LPCAT1 that are not inhibited by Ca(2+) and sulfhydryl-alkylating and -oxidizing agents will provide a better understanding of the physiological function of a mechanism that places the formation of PC, and the disposal of the bioactive species lysoPC, under the control of the redox status and Ca(2+) concentration of the cell.

Indexed as

1-Acylglycerophosphocholine O-AcyltransferaseAcyl Coenzyme AAlanineAlkylationAmino Acid MotifsAmino Acid SequenceAnimalsBiocatalysisCalciumCysteineIonsMiceMutagenesis, Site-DirectedOxidation-ReductionPhosphatidylcholinesProtein Structure, Tertiary1-Acylglycerophosphocholine O-AcyltransferaseAcyl Coenzyme AAlanineCalciumCysteineIonsLpcat1 protein, mousePhosphatidylcholinesRecombinant Proteins

Identifiers

PMID22676268
PMCPMC3439698

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Registered trials

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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.