Evidence map›Paper›PMID 18156367›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes.

Eric Soupene, Henrik Fyrst, Frans A Kuypers

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 117 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Metabolism of host lysophosphatidylcholine inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mechanisms and regulations of ferroptosis.Frontiers in immunology · 2023
    Review
  16. Observational
  17. Article
  18. Article
  19. Review
  20. Review

7 more citing papers are in PubMed but not listed here.

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

3 authors.

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

Funding

SICKLE CELL SCHOLAR PLANU54HL070583 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI VICHINKSY, ELLIOTT P. · 2003 to 2010
$12.0M
NHLBI NIH HHS HL070583NHLBI NIH HHS U54 HL070583
6 · The paper itself

Abstract

The mammalian RBC lacks de novo lipid synthesis but maintains its membrane composition by rapid turnover of acyl moieties at the sn-2 position of phospholipids. Plasma-derived fatty acids are esterified to acyl-CoA by acyl-CoA synthetases and transferred to lysophospholipids by acyl-CoA:lysophospholipid acyltransferases. We report the characterization of three lysophosphatidylcholine (lysoPC) acyltransferases (LPCATs), products of the AYTL1, -2, and -3 genes. These proteins are three members of a LPCAT family, of which all three genes are expressed in an erythroleukemic cell line. Aytl2 mRNA was detected in mouse reticulocytes, and the presence of the product of the human ortholog was confirmed in adult human RBCs. The three murine Aytl proteins generated phosphatidylcholine from long-chain acyl-CoA and lysoPC when expressed in Escherichia coli membranes. Spliced variants of Aytl1, affecting a conserved catalytic motif, were identified. Calcium and magnesium modulated LPCAT activity of both Aytl1 and -2 proteins that exhibit EF-hand motifs at the C terminus. Characterization of the product of the Aytl2 gene as the phosphatidylcholine reacylating enzyme in RBCs represents the identification of a plasma membrane lysophospholipid acyltransferase and establishes the function of a LPCAT protein.

Indexed as

1-Acylglycerophosphocholine O-AcyltransferaseAmino Acid SequenceAnimalsCatalytic DomainCell Line, TumorCell MembraneCloning, MolecularErythrocytesEscherichia coliFatty AcidsHumansMiceMolecular Sequence DataPhosphatidylcholinesReticulocytesSequence Homology, Amino Acid1-Acylglycerophosphocholine O-AcyltransferaseFatty AcidsLpcat1 protein, humanLpcat1 protein, mousePhosphatidylcholines

Identifiers

PMID18156367
PMCPMC2224237
OpenAlexW2115910689

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.