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PLoS One. 2013;8(3):e59267. doi: 10.1371/journal.pone.0059267. Epub 2013 Mar 22.

Assessing phospholipase A2 activity toward cardiolipin by mass spectrometry.

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  • 1Department of Chemistry, Tunghai University, Taichung, Taiwan. howardhsu@thu.edu.tw

Erratum in

  • PLoS One. 2013;8(6). doi:10.1371/annotation/47607b18-ed69-4a08-8619-60c39bd83a13.

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.

PMID:
23533611
[PubMed - indexed for MEDLINE]
PMCID:
PMC3606342
Free PMC Article
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