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Involvement of tyrosine kinases in the activation of human peripheral blood
neutrophils by granulocyte-macrophage colony-stimulating factor
SR McColl, JF DiPersio, AC Caon, P Ho and PH Naccache
Centre de Recherche en Inflammation, Immunologie et Rhumatologie,
Universite Laval, Sainte-Foy, Quebec, Canada.
The aim of the present study is to evaluate the involvement of human
neutrophil tyrosine kinase(s) in the signal transduction mechanism of
granulocyte-macrophage colony-stimulating factor (GM-CSF). Stimulation of
neutrophils with GM-CSF resulted in a time- and dose-dependent
phosphorylation of several proteins having estimated molecular weights of
approximately 40, 55, 74, 97, 118, and 155 Kd, detected by immunoblot using
a monoclonal antibody directed against phosphotyrosine. GM-CSF-induced
tyrosine phosphorylation was inhibited in a dose- and time-dependent manner
by the tyrosine kinase inhibitor erbstatin. Using this inhibitor, we were
able to correlate tyrosine phosphorylation with several functional effects
of GM-CSF on human neutrophils. Pretreatment of neutrophils with erbstatin
before incubation with GM-CSF completely inhibited the GM-CSF-induced
intracellular alkalinization, downregulation of the leukotriene B4
receptor, enhancement of fMet-Leu-Phe-induced intracellular calcium
mobilization, as well as the accumulation of mRNA for the proto- oncogene
c-fos. Taken together, these data suggest that tyrosine kinase activation
in human neutrophils plays a critical regulatory role in both the
stimulation and priming of neutrophil function by GM-CSF.
Volume 78,
Issue 7,
pp. 1842-1852,
10/01/1991
Copyright © 1991 by The American Society of Hematology
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