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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1752-1757
Inhibition of degranulation and interleukin-6 production in mast
cells derived from mice deficient in protein kinase C
Hovav Nechushtan,
Michael Leitges,
Cellina Cohen,
Gillian Kay, and
Ehud Razin
From the Department of Biochemistry, Hebrew University-Hadassah
Medical School; and the Max-Planck-Institut fuer Immunbiologie
Stuebeweg, Freiburg, Germany.
The antigen-mediated activation of mast cells by means of IgE
antibodies bound to the cell surface leads to direct interactions between Fc RI receptor cytoplasmic domains and various intracellular proteins. These interactions initiate diverse signal-transduction pathways, and the activation of these pathways results in the immediate
release of proinflammatory agents. A delayed response also occurs and
includes the release of various cytokines. It is clear that the
activation of kinases is a requirement for the exocytosis observed in
mast cells. In addition to the tyrosine phosphorylation of the affected
system by soluble tyrosine kinases, activity of protein kinase C (PKC)
results in serine or threonine phosphorylation of multiple protein
substrates. In this study, we found that mast cells derived from
PKC -deficient mice produce less interleukin 6 in response to IgE-Ag.
The inhibition of exocytosis in the PKC-deficient mast cells
occurred whether the stimuli were due to the aggregation of the mast
cell surface FcRI or to the calcium ionophore, ionomycin. However,
no significant changes were observed in the proliferative response of
the mast cells to interleukin 3 (IL-3) or in their apoptotic rate after
IL-3 depletion.
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