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Protein kinase C activators inhibit the antigen receptor‐coupled polyphosphoinositide phosphodiesterase in murine B lymphocytes
Author(s) -
Harnett M.M.,
Klaus G.G.B.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80934-7
Subject(s) - microbiology and biotechnology , protein kinase a , phosphodiesterase , receptor , protein kinase c , signal transduction , b cell receptor , antigen , gq alpha subunit , inositol phosphate , chemistry , biology , biochemistry , inositol , antibody , kinase , g protein , b cell , enzyme , immunology
Protein kinase C activators (e.g. PMA) inhibit the inositol phosphate release generated by crosslinking antigen receptors (sIgM and sIgD) on murine B lymphocytes with anti‐receptor antibodies. Unlike other Ca 2+ ‐mobilizing receptor systems, the antigen receptor signal transduction pathway in B cells is not interrupted by PMA at the level of receptor/G‐protein or G‐protein/polyphosphoinositide phosphodiesterase coupling. In these cells, PMA, presumably by activating protein kinase C, inhibits inositol phosphate release by direct effects on the polyphosphoinositide‐specific phosphodiesterase.