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*
Department of Pediatrics, Division of Hematology/Oncology and
Department of Internal Medicine, Division of Nephrology, University of Michigan, Ann Arbor, MI 48109
We investigated the requirement for Syk activation to
initiate downstream signaling events during polymorphonuclear leukocyte
(PMN) phagocytosis of Ab-coated erythrocytes (EIgG). When PMN were
challenged with EIgG, Syk phosphorylation increased in a time-dependent
manner, paralleling the response of PMN phagocytosis. Pretreatment of
PMN with piceatannol, a Syk-selective inhibitor, blocked EIgG
phagocytosis and Syk phosphorylation. We found that piceatannol
inhibited protein kinase C
(PKC) and Raf-1 translocation from
cytosol to plasma membrane by >90%. Extracellular signal-regulated
protein kinase-1 and -2 (ERK1 and ERK2) phosphorylation was similarly
blocked. We also investigated phosphatidylinositide 3-kinase (PI
3-kinase) activity and Syk phosphorylation using piceatannol,
wortmannin, and LY294002, inhibitors of PI 3-kinase. The
phosphorylation of Syk preceded the activation of PI 3-kinase. Both
wortmannin and piceatannol inhibited PI 3-kinase, but only piceatannol
inhibited Syk. In contrast to piceatannol, wortmannin did not inhibit
PKC and Raf-1 translocation. To elucidate signaling downstream of
Syk activation, we assessed whether the cell-permeable diacylglycerol
analogue didecanoylglycerol could normalize PMN phagocytosis, PKC
and Raf-1 translocation, and ERK1 and ERK2 phosphorylation inhibited by
piceatannol. The addition of didecanoylglycerol to the Syk-inhibited
phagocytosing PMN normalized all three without a concomitant effect on
PI 3-kinase activity and Syk phosphorylation. We conclude that Syk
activation following Fc
receptor engagement initiates downstream
signaling events leading to mitogen-activated protein kinase activation
independent of PI 3-kinase activation.
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