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Activation of multiple protein kinases induced by cross‐linking of Fc γ RII in human neutrophils
Author(s) -
Liang Li,
Huang ChiKuang
Publication year - 1995
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.57.2.326
Subject(s) - calphostin c , ask1 , mitogen activated protein kinase kinase , calphostin , map kinase kinase kinase , kinase , biology , map2k7 , c raf , microbiology and biotechnology , tyrosine kinase , protein kinase a , cyclin dependent kinase 9 , protein kinase c , cyclin dependent kinase 2 , protein kinase inhibitor , receptor tyrosine kinase , mitogen activated protein kinase , biochemistry , signal transduction
Several neutrophil protein kinases that undergo changes in activity during FC γ RII activation have been investigated. These kinases include calcium/calmodulin‐dependent protein kinase II (CAMPKII), mitogen‐activated protein kinase (MAPK), and histone H4 protein kinase (PKH4). They are rapidly and transiently activated in a dose‐dependent manner by the cross‐linking of FC γ RII. The activation of CAMPKII but neither PKH4 nor MAPK was inhibited by treating the cells with either a tyrosine kinase inhibitor, genistein, or an intracellular calcium chelator, BAPTA/AM. The superoxide production induced by cross‐linking FC γ RII can be inhibited partially by various protein kinase inhibitors: 33% by protein kinase C inhibitor calphostin C, 30% by CAMPKII inhibitor KN‐62, and 62% by tyrosine kinase inhibitor genistein. These results indicate that cross‐linking of FC γ RII induces multiple signaling pathways that lead to the activation of various protein kinases. The activation of these kinases may be involved directly or indirectly in the regulation of superoxide production. J. Leukoc. Biol. 57: 326–331; 1995.