Abstract
The receptor-mediated activation of neutrophils by ligands such as the chemotactic peptide N-formyl-methionine-leucin-phenylalanine (FMLP) is associated with the activation of phospholipase C (PLC) and phospholipase A2 (PLA2) [1,2]. Whereas the activation of PLC leads to generation of inositol-1, 4, 5-triphosphate (IP3), which liberates Ca++ i from intracellular stores, and 1,2-diacylglycerol (DG), which activates protein kinase C (PKC), stimulation of PLA2 leads to breakdown of phosphatidylcholine (PC) to produce arachidonic acid (AA) and lyso-platelet-activating factor (lyso-PAF). The latter serves as precursor for the biosynthesis of platelet-activating factor (PAF) with the help of acetylCoA:lyso-PAF acetyltransferase [3]. However, the mechanism controlling these processes are not clearly understood. To what extent protein kinase C (PKC) contributes to the [14C]AA release and the production of PAF in stimulated human neutrophils has been studied in our laboratory with the help of putative inhibitors as well as activators of PKC.
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Müller, S., Nigam, S. (1993). Enhancement by Staurosporine of PLA2-Activity and PAF-Biosynthesis in FMLP- Stimulated Human Neutrophils: Specific Role of Endogenously Synthesized PAF. In: Nigam, S., Honn, K.V., Marnett, L.J., Walden, T.L. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury. Developments in Oncology, vol 71. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3520-1_40
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DOI: https://doi.org/10.1007/978-1-4615-3520-1_40
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