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Reference: Gijon MA, et al. (2008) Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils. J Biol Chem 283(44):30235-45

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Abstract

The cycle of deacylation and reacylation of phospholipids plays a critical role in regulating availability of arachidonic acid for eicosanoid production. The major yeast lysophospholipid acyltransferase, Ale1p, is related to mammalian membrane-bound O-acyltransferase (MBOAT) proteins. We expressed four human MBOATs in yeast strains lacking Ale1p, and studied their acyl-CoA and lysophospholipid specificities using novel mass spectrometry-based enzyme assays. MBOAT1 is a lyso-PS acyltransferase with preference for oleoyl-CoA. MBOAT2 also prefers oleoyl-CoA, using lyso-PA and lyso-PE as acyl acceptors. MBOAT5 prefers lyso-PC and lyso-PS to incorporate linoleoyl and arachidonoyl chains. MBOAT7 is a lyso-PI acyltransferase with remarkable specificity for arachidonoyl-CoA. MBOAT5 and MBOAT7 are particularly susceptible to inhibition by thimerosal. Human neutrophils express mRNA for these four enzymes, and neutrophil microsomes incorporate arachidonoyl chains into PI, PC, PS and PE in a thimerosal sensitive manner. These results strongly implicate MBOAT5 and MBOAT7 in arachidonate recycling, thus regulating free arachidonic acid levels and leukotriene synthesis in neutrophils.

Reference Type
Journal Article
Authors
Gijon MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR
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