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Interleukin-12 induces tyrosine phosphorylation and activation of 44-kD
mitogen-activated protein kinase in human T cells
C Pignata, JS Sanghera, L Cossette, SL Pelech and J Ritz
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA
02115.
Interleukin-12 (IL-12) is a novel cytokine that enhances numerous
functional activities of human T cells and natural killer (NK) cells. The
present studies were undertaken to characterize some of the early signaling
events following IL-12 stimulation of mitogen-activated normal T cells. In
these cells, IL-12 induces rapid tyrosine phosphorylation of proteins of
21, 44, and 54 kD. However, IL-12 does not induce tyrosine phosphorylation
in normal resting T cells. In conjunction with increased tyrosine
phosphorylation of several substrates, IL-12 stimulation resulted in
increased in vitro kinase activity of immunoprecipitated tyrosine
phosphorylated proteins. The 44- kD protein has been characterized as one
isoform of the mitogen- activated protein (MAP) kinase family. Increased
tyrosine phosphorylation of MAP kinase following IL-12 stimulation was also
associated with enhanced enzymatic activity of this protein in vitro as
measured by myelin basic protein phosphotransferase assay. These studies
identify MAP kinase as one of the intracellular elements of the IL-12
signaling pathway in human T cells.
Volume 83,
Issue 1,
pp. 184-190,
01/01/1994
Copyright © 1994 by The American Society of Hematology
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