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CUTTING EDGE |
*
Division of Molecular Biology, Research Institute for Biological Sciences, Science University of Tokyo, Chiba, Japan;
First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan; and
Department of Molecular Genetics, Institute for Liver Research, Kansai Medical University, Moriguchi, Japan
Stimulation of the B cell Ag receptor (BCR) induces activation
of tyrosine kinases such as Lyn and Syk,
phosphorylation and activation of multiple signaling
components, and eventually, the expression of several genes including
c-myc. Syk is required for activation of phospholipase
C-
2 and the subsequent phosphatidylinositol hydrolysis, leading to
protein kinase C (PKC) activation and intracellular Ca2+
increase. In contrast, the function of Lyn remains obscure. Here, we
report that BCR-mediated induction of c-myc promoter
activity and of PKC activity, but not the expression level of
functional PKC, was markedly augmented in Lyn-deficient chicken B
cells. This enhancement was reversed to the level of wild-type cells by
the expression of exogenous Lyn of kinase-inactive form. These results
indicate that Lyn inhibits BCR-mediated activation of a large portion
of PKC isozymes in a kinase-independent fashion. This finding reveals a
novel role of Lyn in negative regulation of BCR signaling.
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