Evidence map›Paper›PMID 18434304›Full record

ArticleThe Journal of biological chemistry2008

Identification of a domain that mediates association of platelet-activating factor acetylhydrolase with high density lipoprotein.

Alison A Gardner, Ethan C Reichert, Matthew K Topham, Diana M Stafforini

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.1field-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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Relationship between platelet activating factor acetylhydrolase activity and apolipoprotein B levels in patients with peanut allergy.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Review
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  12. Article
  13. Noninvasive molecular imaging reveals role of PAF in leukocyte-endothelial interaction in LPS-induced ocular vascular injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  14. Article
  15. Article
  16. Article
  17. Review
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  20. Phospholipase A2 biochemistry.Cardiovascular drugs and therapy · 2009
    Review
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

4 authors at 1 institution in 1 country.

Alison A GardnerHuntsman Cancer Institute and Department of Internal Medicine, University of Utah, Salt Lake City, Utah 84112, USA.
Ethan C Reichert
Matthew K Topham
Diana M Stafforini
Huntsman Cancer Institute · US

Funding

METABOLISM OF PLATELET-ACTIVATING FACTORR01HL035828 · NHLBI · UNIVERSITY OF UTAH · PI STAFFORINI, DIANA M · 1986 to 2008
$1.9M
NHLBI NIH HHS HL35828
6 · The paper itself

Abstract

The plasma form of platelet-activating factor (PAF) acetylhydrolase (PAF-AH), also known as lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) inactivates potent lipid messengers such as PAF and modified phospholipids generated in settings of oxidant stress. In humans, PAF-AH circulates in blood in fully active form and associates with high and low density lipoproteins (HDL and LDL). Several studies suggest that the location of PAF-AH affects both the catalytic efficiency and the function of the enzyme in vivo. The distribution of PAF-AH among lipoproteins varies widely among mammals. Here, we report that mouse and human PAF-AHs associate with human HDL particles of different density. We made use of this observation in the development of a binding assay to identify domains required for association of human PAF-AH with human HDL. Sequence comparisons among species combined with domain-swapping and site-directed mutagenesis studies led us to the identification of C-terminal residues necessary for the association of human PAF-AH with human HDL. Interestingly, the region identified is not conserved among PAF-AHs, suggesting that PAF-AH interacts with HDL particles in a manner that is unique to each species. These findings contribute to our understanding of the mechanisms responsible for association of human PAF-AH with HDL and may facilitate future studies aimed at precisely determining the function of PAF-AH in each lipoprotein particle.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAmino Acid SequenceAnimalsCatalysisConserved SequenceHumansLipoproteinsLipoproteins, HDLMiceModels, BiologicalMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidSubstrate Specificity1-Alkyl-2-acetylglycerophosphocholine EsteraseLipoproteinsLipoproteins, HDL

Identifiers

PMID18434304
PMCPMC2427361
OpenAlexW2039464415

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.