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  • Title: Involvement of tyrosine kinases in the activation of human peripheral blood neutrophils by granulocyte-macrophage colony-stimulating factor.
    Author: McColl SR, DiPersio JF, Caon AC, Ho P, Naccache PH.
    Journal: Blood; 1991 Oct 01; 78(7):1842-52. PubMed ID: 1717073.
    Abstract:
    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.
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