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Tyrosine-specific protein phosphorylation during activation of human
neutrophils
RL Berkow and RW Dodson
Department of Pediatrics, University of Alabama, Birmingham.
The activation of human neutrophils by a variety of receptor-dependent and
receptor-independent agonists induces the phosphorylation of a large number
of proteins. Since we have previously shown that human neutrophils have at
least two distinct tyrosine kinase activities, we examined protein tyrosine
phosphorylation in human neutrophils stimulated with a variety of agonists.
Using a monoclonal antibody specific for phosphotyrosine, the present study
shows that the chemotactic peptides FMLP and leukotriene B4, the phorbol
ester phorbol myristate acetate (PMA), and the calcium ionophore A23187
induce an increase in tyrosine phosphorylation of a number of neutrophil
proteins. This increased protein tyrosine phosphorylation was dependent on
the concentration of the agonist, as well as on the time of exposure to the
agonist. Fractionation experiments showed that both a 150,000 g cytosolic
and a particulate preparation showed increases in protein tyrosine
phosphorylation with stimulation by FMLP or PMA, and showed that the
pattern of protein tyrosine phosphorylation was slightly different in the
FMLP- and PMA-stimulated cells. These data indicate that protein tyrosine
phosphorylation is an early event in the activation of human neutrophils by
a variety of receptor-dependent and receptor-independent agonists.
Volume 75,
Issue 12,
pp. 2445-2452,
06/15/1990
Copyright © 1990 by The American Society of Hematology
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