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J. Lipid Res.
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A more recent version of this article appeared on November 1, 2007

Papers In Press, published online ahead of print August 10, 2007
J. Lipid Res., doi:10.1194/jlr.M700325-JLR200
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Submitted on July 19, 2007
Revised on August 3, 2007
Accepted on August 9, 2007

Intracellular PAF catabolism by PAF acetylhydrolase counteracts continual PAF synthesis

Jiawei Chen, Lili Yang, Jason M. Foulks, Andrew S. Weyrich, Guy A. Zimmerman, Gopal K. Marathe, and Thomas M. McIntyre

Cell Biology, Cleveland Clinic, Cleveland, OH 44195

Corresponding Author: mcintyt{at}ccf.org

Stimulated inflammatory cells synthesize platelet-activating factor (PAF), but lysates of these cells show little enhancement in PAF synthase activity. We show human neutrophils contain intracellular plasma PAF acetylhydrolase (PLA2G7), an enzyme normally secreted by monocytes. The esterase inhibitors methyl arachidonoyl fluorophosphonate (MAFP), its linoleoyl homolog, and Pefabloc inhibit plasma PAF acetylhydrolase. All these inhibitors induced PAF accumulation by quiescent neutrophils and monocytes that was equivalent to agonist stimulation. Agonist stimulation after esterase inhibition did not further increase PAF accumulation. PAF acetylhydrolase activity in intact neutrophils was reduced, but not abolished, by agonist stimulation. Erythrocytes, which do not participate in the acute inflammatory response, inexplicably express the type I PAF acetylhydrolase whose only known substrate is PAF. Inhibition of this enzyme by MAFP caused PAF accumulation by erythrocytes, which was hemolytic in the absence of PAF acetylhydrolase activity. We propose that PAF is continuously synthesized by a non-selective acyltransferase activity(ies) found even in non-inflammatory cells as a component of membrane remodeling, which is then selectively and continually degraded by intracellular PAF acetylhydrolase activity to modulate PAF production.


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