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IL‐4 secretion and histamine release by human basophils are differentially regulated by protein kinase C activation
Author(s) -
Schroeder John T.,
Howard Brian P.,
Jenkens M. Kathleen,
KageySobotka Anne,
Lichtenstein Lawrence M.,
MacGlashan Donald W.
Publication year - 1998
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.63.6.692
Subject(s) - ionomycin , protein kinase c , secretion , histamine , secretagogue , biology , phorbol , endocrinology , medicine , microbiology and biotechnology , kinase , stimulation
The role of protein kinase C (PKC) activation was investigated in the secretion of interleukin‐4 (IL‐4) protein by human basophils. Phorbol myristate acetate (PMA) induced little to no detectable IL‐4 protein in culture supernatants, despite being a potent secretagogue of histamine release by basophils. In fact, the secretion of IL‐4 by basophils stimulated with ionomycin alone was down‐regulated (30‐70%) with the simultaneous addition of PMA. In peripheral blood lymphocytes (PBL), however, the combination of ionomycin and PMA were highly synergistic, resulting in maximum IL‐4 release but at a slower rate. PKC inhibitors reversed these effects on IL‐4 secretion. In sharp contrast to its inhibitory effect on IL‐4 protein secretion, PMA did not block the accumulation of IL‐4 mRNA in basophils activated by ionomycin. These data suggest that there are marked differences in the regulatory processes for IL‐4 transcription, translation, or secretion between basophils and lymphocytes. J. Leukoc. Biol . 63: 692–698; 1998.