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pubmed-article:10428468pubmed:abstractTextThe N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD) generates N-acylethanolamines, including N-arachidonoyl-ethanolamine (anandamide), that may be neuroprotective and analgesic. The properties of NAPE-PLD from rat heart and brain microsomes are investigated and compared to those of other PLDs. NAPE-PLD is inhibited by the fatty acid aminohydrolase inhibitor MAFP in high concentrations (> or = 100 microM) while PMSF in high concentrations (10 mM) tends to stabilise NAPE-PLD activity. Oleate inhibits NAPE-PLD but the enzyme is not affected by PIP2, alpha-synuclein or mastoparan. Furthermore, it is for the first time reported that NAPE-PLD is not capable of catalysing a transphosphatidylation reaction like most other known PLDs.lld:pubmed
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pubmed-article:10428468pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:10428468pubmed:articleTitleN-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate.lld:pubmed
pubmed-article:10428468pubmed:affiliationDepartment of Pharmacology, The Royal Danish School of Pharmacy, Copenhagen.lld:pubmed
pubmed-article:10428468pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10428468pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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