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http://purl.uniprot.org/citations/23533611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23533611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23533611http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0059267"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0059267"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Dumlao D.S."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Dumlao D.S."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Dennis E.A."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Dennis E.A."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Hsu Y.H."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/author"Hsu Y.H."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/pages"E59267"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/pages"E59267"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/title"Assessing phospholipase A2 activity toward cardiolipin by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/title"Assessing phospholipase A2 activity toward cardiolipin by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/23533611http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/23533611http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23533611
http://purl.uniprot.org/citations/23533611http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23533611