Evidence map›Paper›PMID 23089916›Full record

ArticleJournal of lipid research2013

Structural basis of specific interactions of Lp-PLA2 with HDL revealed by hydrogen deuterium exchange mass spectrometry.

Jian Cao, Yuan-Hao Hsu, Sheng Li, Virgil L Woods, Edward A Dennis

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Lipoprotein-associated phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Review
  7. Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018
    Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Jian CaoDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0601, USA.
Yuan-Hao Hsu
Sheng Li
Virgil L Woods
Edward A Dennis
University of California, San Diego · US

Funding

ACTION OF LIPOLYTIC ENZYMESR01GM020501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 1985 to 2020
$7.3M
NIGMS NIH HHS R01 GM020501NIGMS NIH HHS R01-GM20501
6 · The paper itself

Abstract

Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)), specifically Group VIIA PLA(2), is a member of the phospholipase A(2) superfamily and is found mainly associated with LDL and HDL in human plasma. Lp-PLA(2) is considered as a risk factor, a potential biomarker, a target for therapy in the treatment of cardiovascular disease, and evidence suggests that the level of Lp-PLA(2) in plasma is associated with the risk of future cardiovascular and stroke events. The differential location of the enzyme in LDL/HDL lipoproteins has been suggested to affect Lp-PLA(2) function and/or its physiological role and an abnormal distribution of the enzyme may correlate with diseases. Although a mutagenesis study suggested that a surface helix (residues 362-369) mediates the association between Lp-PLA(2) and HDL, the molecular details and mechanism of association has remained unknown. We have now employed hydrogen deuterium exchange mass spectrometry to characterize the interaction between recombinant human Lp-PLA(2) and human HDL. We have found that specific residues 113-120, 192-204, and 360-368 likely mediate HDL binding. In a previous study, we showed that residues 113-120 are important for Lp-PLA(2)-liposome interactions. We now find that residues 192-204 show a decreased deuteration level when Lp-PLA(2) is exposed to apoA-I, but not apoA-II, the most abundant apoproteins in HDL, and additionally, residues 360-368 are only affected by HDL.The results suggest that apoA-I and phospholipid membranes play crucial roles in Lp-PLA(2) localization to HDL.

Indexed as

Deuterium Exchange MeasurementMass Spectrometry1-Alkyl-2-acetylglycerophosphocholine EsteraseApolipoprotein A-IBinding SitesHumansLipoproteins, HDLModels, MolecularProtein BindingProtein Conformation1-Alkyl-2-acetylglycerophosphocholine EsteraseApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID23089916
PMCPMC3520519
OpenAlexW2050961740

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.