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Blood, Vol. 92 No. 6 (September 15), 1998:
pp. 2133-2140
Activation of the Small GTPase Rap1 in Human Neutrophils
Laura M'Rabet,
Paul Coffer,
Fried Zwartkruis,
Barbara Franke,
Anthony W. Segal,
Leo Koenderman, and
Johannes L. Bos
From the Laboratory for Physiological Chemistry and Department of
Pulmonary Diseases, Utrecht University, Utrecht, The Netherlands; and
the University of London Hospital, London, UK.
The small GTPase Rap1 is highly expressed in human neutrophils, but
its function is largely unknown. Using the Rap1-binding domain of
RalGDS (RalGDS-RBD) as an activation-specific probe for Rap1, we have
investigated the regulation of Rap1 activity in primary human
neutrophils. We found that a variety of stimuli involved in neutrophil
activation, including fMet-Leu-Phe (fMLP), platelet-activating factor
(PAF), granulocyte-macrophage colony-stimulating factor (GM-CSF), and
IgG-coated particles, induce a rapid and transient Rap1 activation. In
addition, we found that Rap1 is normally activated in neutrophils from
chronic granulomatous disease patients that lack cytochrome
b558 or p47phox and have a defective NADPH oxidase system.
From these results we conclude that in neutrophils Rap1 is activated
independently of respiratory burst induction. Finally, we found that
Rap1 is activated by both the Ca2+ ionophore ionomycin
and the phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA),
indicating that phospholipase C (PLC) activation leading to elevated
levels of intracellular free Ca2+ and diacylglycerol
(DAG) can mediate Rap1 activation. However, inhibition of PLC and
Ca2+ depletion only marginally affected fMLP-induced Rap1
activation, suggesting that additional pathways may control Rap1
activation.
© 1998 by The American Society of Hematology.
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