Evidence map›Paper›PMID 23533611›Full record

ArticlePloS one2013

Assessing phospholipase A2 activity toward cardiolipin by mass spectrometry.

Yuan-Hao Hsu, Darren S Dumlao, Jian Cao, Edward A Dennis

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Secretory phospholipase ACommunications biology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Fat of the Gut: Epithelial Phospholipids in Inflammatory Bowel Diseases.International journal of molecular sciences · 2021
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    Review
  17. Review
  18. Article
  19. Review
  20. Conodipine-P1-3, the First Phospholipases AMolecular & cellular proteomics : MCP · 2019
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 2 countries.

Yuan-Hao HsuDepartment of Chemistry, Tunghai University, Taichung, Taiwan. howardhsu@thu.edu.tw
Darren S Dumlao
Jian Cao
Edward A Dennis
University of California, San Diego · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
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 R0-1 GM 20,501-38NIGMS NIH HHS U54 GM 069338NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Cardiolipin, a major component of mitochondria, is critical for mitochondrial functioning including the regulation of cytochrome c release during apoptosis and proper electron transport. Mitochondrial cardiolipin with its unique bulky amphipathic structure is a potential substrate for phospholipase A2 (PLA2) in vivo. We have developed mass spectrometric methodology for analyzing PLA2 activity toward various cardiolipin forms and demonstrate that cardiolipin is a substrate for sPLA2, cPLA2 and iPLA2, but not for Lp-PLA2. Our results also show that none of these PLA2s have significant PLA1 activities toward dilyso-cardiolipin. To understand the mechanism of cardiolipin hydrolysis by PLA2, we also quantified the release of monolyso-cardiolipin and dilyso-cardiolipin in the PLA2 assays. The sPLA2s caused an accumulation of dilyso-cardiolipin, in contrast to iPLA2 which caused an accumulation of monolyso-cardiolipin. Moreover, cardiolipin inhibits iPLA2 and cPLA2, and activates sPLA2 at low mol fractions in mixed micelles of Triton X-100 with the substrate 1-palmitoyl-2-arachidonyl-sn-phosphtidylcholine. Thus, cardiolipin functions as both a substrate and a regulator of PLA2 activity and the ability to assay the various forms of PLA2 is important in understanding its function.

Indexed as

AnimalsCardiolipinsGroup IV Phospholipases A2HumansMass SpectrometryPhospholipases A2Phospholipases A2, Calcium-IndependentPhospholipases A2, SecretoryCardiolipinsGroup IV Phospholipases A2Phospholipases A2Phospholipases A2, Calcium-IndependentPhospholipases A2, Secretory

Identifiers

PMID23533611
PMCPMC3606342
OpenAlexW2032513880

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.