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Signal transduction by the platelet Fc receptor
GP Anderson and CL Anderson
Department of Internal Medicine, Ohio State University, Columbus.
We have evaluated the mechanism by which crosslinking human platelet Fc
receptor (FcR) for IgG triggers platelet aggregation and the platelet
release reaction. Platelet FcR was crosslinked by incubating purified human
platelets with anti-FcRII monoclonal antibody and F(ab')2 anti- mouse Ig.
The resultant [Ca2+]i increase, monitored by Fura-2 and measured in the
absence of extracellular Ca2+, reached a peak of 750 +/- 50 nmol/L. The
effects of cyclooxygenase inhibitors, aspirin and indomethacin, and a
phospholipase A2 inhibitor, dibromoacetophenone, were examined. Regardless
of the inhibitor, at least 25% of the [Ca2+]i increase remained. Thrombin
(0.2 U/mL) stimulated an immediate [Ca2+]i increase that reached 1.95 +/-
0.8 mumol/L. The [Ca2+]i increase generated by thrombin was only slightly
reduced by these inhibitors. Crosslinking the FcRII of platelets resulted
in a fivefold increase in the production of [3H]inositol phosphates, (IP)
which, in the absence of extracellular Ca2+ was insensitive to aspirin. The
activation of a [Ca2+]i increase along with the measured increases in IP
indicate that FcRII crosslinking leads to the activation of phospholipase C
(PLC). In contrast to thrombin, platelet activation via FcRII depends to a
large extent on arachidonic acid metabolites. However, neither
cyclooxygenase nor phospholipase A2 inhibitors completely blocked
FcRII-stimulated [Ca2+]i increase. These observations led us to propose
that crosslinking of platelet FcRII initially activates PLC.
Volume 76,
Issue 6,
pp. 1165-1172,
09/15/1990
Copyright © 1990 by The American Society of Hematology
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