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Selective inhibition of human neutrophil functional responsiveness by
erbstatin, an inhibitor of tyrosine protein kinase
PH Naccache, C Gilbert, AC Caon, M Gaudry, CK Huang, VA Bonak, K Umezawa and SR McColl
Department of Medicine, Universite Laval, Ste Foy, Quebec, Canada.
The role of tyrosine kinases in the responses of human neutrophils to
chemotactic factors was examined using the recently described inhibitor
erbstatin. Pre-incubation with erbstatin decreased the amount of tyrosine
phosphorylation induced by the formylated oligopeptide formyl-
methionyl-leucyl-phenylalanine (fMet-Leu-Phe) without effecting the binding
of [3H]-fMet-Leu-Phe. Erbstatin also dose-dependently inhibited the
production of superoxide anion induced by fMet-Leu-Phe and platelet-
activating factor, but did not affect the oxidative burst induced by either
the calcium ionophore A23187 or the phorbol ester phorbol 12- myristate
13-acetate. Furthermore, erbstatin diminished the cytosolic acidification
elicited by fMet-Leu-Phe, platelet-activating factor, and leukotriene B4.
In contrast, erbstatin was without effect on the increase in the levels of
cytoplasmic free calcium and polymerized actin elicited by fMet-Leu-Phe,
C5a, leukotriene B4 and platelet- activating factor, whereas the increase
in cytoplasmic free calcium elicited by platelet-derived growth factor was
inhibited by erbstatin. In addition, erbstatin affected neither the release
of elastase stimulated by these agonists nor the release of
beta-glucosaminidase, lysozyme or vitamin B12-binding protein induced by
fMet-Leu-Phe. These results indicate that tyrosine protein kinases are
involved in the signaling pathways employed by chemotactic factors in the
stimulation of selective functional responses (and superoxide production in
particular) in human neutrophils.
Volume 76,
Issue 10,
pp. 2098-2104,
11/15/1990
Copyright © 1990 by The American Society of Hematology
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