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Regulation of stimulated integrin surface expression in human neutrophils
by tyrosine phosphorylation
PH Naccache, N Jean, NW Liao, JM Bator, SR McColl and P Kubes
Centre de Recherche en Inflammation, Immunologie et Rhumatologie, CHUL,
Ste-Foy, Quebec, Canada.
The control of the adhesive properties of human neutrophils is an essential
element of their defense function. One level at which this control is
exerted involves the upregulation of the surface expression of beta
2-integrins. In this study, we have examined the potential involvement of
tyrosine phosphorylation in the latter process. Two inhibitors of tyrosine
kinases with differing modes of action, erbstatin and herbimycin A, were
found to inhibit the expression of CD11b and CD18 stimulated by chemotactic
factors (fMet-Leu-Phe or leukotriene B4) or growth factors (tumor necrosis
factor alpha). This inhibition was not shared by an inactive analog of
erbstatin or by the protein kinase C inhibitor Ro 31-8330. Erbstatin also
inhibited the unveiling of activation-specific neoepitopes detected by
antibody CBRM1/5. Pretreatment of neutrophils (but not of endothelial
cells) with erbstatin inhibited the stimulation of neutrophils' adherence
to endothelial cells induced by fMet-Leu-Phe. Augmentation of tyrosine
phosphorylation by inhibiting tyrosine phosphatases using
hydroperoxyvanadate led to an increased surface expression of CD11b and
CD18 and enhanced the adhesion of neutrophils to endothelial cells.
Finally, the leumedin NPC 15669, which had previously been shown to inhibit
stimulated CD11b expression and neutrophil adherence to endothelial cells
and to exhibit anti-inflammatory properties in various in vivo models of
inflammation, inhibited the stimulation of tyrosine, phosphorylation
induced by fMet-Leu-Phe. Taken together, these data establish a strong
correlation between tyrosine phosphorylation and integrin upregulation in
stimulated human neutrophils.
Volume 84,
Issue 2,
pp. 616-624,
07/15/1994
Copyright © 1994 by The American Society of Hematology
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