Abstract
Acetyl-CoA:1-alkyl-2-1yso-sn-glycero-3-phosphocholine (lyso-PAF) acetyltransferase catalyzes the final step in the remodeling pathway of platelet-activating factor (PAF) biosynthesis. It has completely different characteristics than the acetyltransferase involved in the de novo pathway of PAF biosynthesis. This enzyme activity is stimulated by various inflammatory agents that cause the overproduction of PAF in hypersensitivity responses. The lyso-PAF substrate for this acetyltransferase can be derived from the precursor membrane pool of alkylarachidonoylglycerophosphocholines through the action of a putative phospholipase A2 or—as recently shown—via generation by a CoA-independent transacylase. Thus, the regulation of PAF formation by the remodeling pathway is extremely complex because of the need to consider factors affecting the activation of acetyltransferase, protein kinases, phospholipase A2, a transacylase, and catabolic enzymes that utilize PAF or lyso-PAF as substrates. Two methods are described to measure the activity of acetyltransferase in this chapter.
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