Abstract
The initial step in the remodeling pathway of PAF synthesis is catalyzed by phospholipase A2 (PLA2).1 It has generally been accepted that PLA2 acts directly on 1-0-alkyl-2-arachidonoyl-sn-glycero-3-phosphocholine (alkyl-2-AA-GPC) to form lyso-PAF (1-alkyl-2-lyso-GPC) which is then acetylated to yield PAF. More recent studies suggest that PAF synthesis may also be initiated indirectly through the action of CoA-independent transacylase following the hydrolysis of l-0-alk-1′-enyl-2-AA-sn-glycero-3-phosphoethanolamine (alkenyl-2-AA-GPE) by PLA2.2,3 In the putative indirect pathway, an accumulation of alkenyl-2-lyso-GPE triggers the transfer of AA from alkyl-2-AA-GPC to the alkenyl-2-lyso-GPE thus forming lyso-PAF. It seems logical that both the direct and indirect pathways may contribute to PAF synthesis. However, the relative physiological importance of the two pathways has not been established.
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References
Prescott, S. M., Zimmerman, G. A., and McIntyre, T. M.: Platelet-activating factor. J. Biol. Chem. 265: 17381–17384 (1990).
Nieto, M. L., Venable, M. E., Bauldry, S. A., Greene, D. G., Kennedy, M., Bass, D. A., and Wykle, R. L.: Evidence that hydrolysis of ethanolamine plasmalogens triggers synthesis of platelet activating factor via a transacylation reaction. J. Biol. Chem. 266: 18699–18706 (1991).
Uemura, Y., Lee, T.-C., and Snyder, F.: A coenzyme A-independent transacylase is linked to the formation of platelet-activating factor (PAF) by generating the lyso-PAF intermediate in the remodeling pathway. J. Biol. Chem. 266: 8268–8272 (1991).
Ramesha, C. S., and Pickett, W. C.: Platelet-activating factor and leukotriene biosynthesis is inhibited in polymorphonuclear leukocytes depleted of arachidonic acid. J. Biol. Chem. 261: 7592–7595 (1986).
Suga, K., Kawasaki, T., Blank, M. L., and Snyder, F.: An arachidonoyl (polyenoic)-specific phospholipase A, activity regulates the synthesis of platelet-activating factor in granulocytic HL-60 cells. J. Biol. Chem. 265: 12363–12371 (1990).
Billah, M. M., Bryant, R. W., and Siegel, M. I.: Lipoxygenase products of arachidonic acid modulate biosynthesis of platelet-activating factor (1–0-alkyl-2-acetyl-sn-glycerol-3-phosphocholine) by human neutrophils via phospholipase A,. J. Biol. Chem. 260: 6899–6906 (1985).
Tessner, T. G., O’Flaherty, J. T., and Wykle, R. L.: Stimulation of platelet-activating factor synthesis by a nonmetabolizable bioactive analog of platelet-activating factor and influence of arachidonic acid metabolites. J. Biol. Chem. 264: 4794–4799 (1989).
Chilton, F. H., O’Flaherty, J. T., Ellis, J. M., Swendsen, C. L., and Wykle, R. L.: Selective acylation of lyso platelet activating factor by arachidonate in human neutrophils. J. Biol. Chem. 258: 7268–7271 (1983).
Mueller, H. W., O’Flaherty, J. T., Greene, D. G., Samuel, M. P., Wykle, R. L.: 1–0-alkyl-linked glycerophospholipids of human neutrophils: Distribution of arachidonate and other acyl residues in the ether-linked and diacyl species. J. Lipid Res. 25: 383–388 (1984).
Ramesha, C. S. and Ives, D. L.: Detection of arachidonoyl-selective phospholipase A, in human neutrophil cytòsol. Biochim. Biophys. Acta. 1168: 37–44 (1993).
Alonso, F., Henson, R. M., and Leslie, C. C.: A cytosolic phospholipase in human neutrophils that hydrolyzes arachidonoyl-containing phosphatidylcholine. Biochim. Biophys. Acta. 878: 273–280 (1986).
Lin, L.-L., Lin, A. Y., and Knopf, J. L.: Cytosolic phospholipase A, is coupled to hormonally regulated release of arachidonic acid. Proc. Natl. Acad. Sci. 89: 6147–6151 (1992).
Wijkander, J., O’Flaherty, J. T., and Wykle, R. L.: 5-Lipoxygenase products modulate the activity of the 85 kDa phospholipase A, in human neutrophils. J. Biol. Chem., in press.
Powell, W. S., Gravel, S., MacLeod, R. J., Mills, E., and Hashefi, M.: Stimulation of human neutrophils by 5-oxo-6,8,11,14-eicosatetraenoic acid by a mechanism independent of the leukotriene B4 receptor. J. Biol. Chem. 268: 9280–9286 (1993).
Bauldry, S. A., Wykle, R. L., and Bass, D. A.: Phospholipase A, activation in human neutrophils. Differential actions of diacylglycerols and alkylacylglycerols in priming cells for stimulation by N-formyl-met-leuphe. J. Biol. Chem. 263: 16787–16795 (1988).
Bauldry, S. A., Wykle, R. L., and Bass, D. A.: Differential actions of diacyl-and alkylacylglycerols in priming phospholipase A„ 5-lipoxygenase and acetyltransferase activation in human neutrophils. Biochim. Biophys. Acta 1084: 178–184 (1991)
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Wykle, R.L., Wijkander, J., Nixon, A.B., Daniel, L.W., O’Flaherty, J.T. (1996). Activation of 85 kDa PLA2 by Eicosanoids in Human Neutrophils and Eosinophils. In: Nigam, S., Kunkel, G., Prescott, S.M. (eds) Platelet-Activating Factor and Related Lipid Mediators 2. Advances in Experimental Medicine and Biology, vol 416. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0179-8_52
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DOI: https://doi.org/10.1007/978-1-4899-0179-8_52
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