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An atypical protein kinase C, PKC ζ, regulates human eosinophil effector functions
Author(s) -
Kato Masahiko,
Yamaguchi Takafumi,
Tachibana Atsushi,
Suzuki Masato,
Izumi Takashi,
Maruyama Kenichi,
Hayashi Yasuhide,
Kimura Hirokazu
Publication year - 2005
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1111/j.1365-2567.2005.02210.x
Subject(s) - protein kinase c , rottlerin , microbiology and biotechnology , eosinophil peroxidase , bisindolylmaleimide , eosinophil , nadph oxidase , biology , platelet activating factor , degranulation , chemistry , biochemistry , kinase , immunology , receptor , reactive oxygen species , asthma
Summary Protein kinase (PK) C comprises a family of isoenzymes that play key roles in downstream signalling and cell functions. We studied PKC ζ participation in the effector functions of human eosinophils stimulated with platelet‐activating factor (PAF) or complement (C) 5a. After pretreating eosinophils with a myristoylated specific PKC ζ inhibitor; bisindlolylmaleimide I ( Bis I), an inhibitor of conventional and novel PKCs; or rottlerin, a PKC δ inhibitor, we examined PAF‐ and C5a‐evoked functions. Induced PKC translocation was characterized by confocal laser scanning microscopy. The PKC ζ inhibitor blocked PAF‐ or C5a‐induced eosinophil superoxide anion generation as effectively as Bis I or rottlerin. The PKC ζ inhibitor also attenuated PAF‐ or C5a‐induced eosinophil degranulation and adhesion. In contrast, the PKC ζ inhibitor did not affect PAF‐ or C5a‐induced CD11b expression. Finally, both eosinophil shape changes and the translocation of PKC ζ and p47 phox , a component of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase, to the plasma membrane induced by PAF or C5a were completely inhibited by the PKC inhibitor. Thus, the atypical PKC ζ regulates human eosinophil adhesion and effector functions.