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Signal Transduction during Platelet‐Activating Factor‐Induced Lymphocyte Binding to Endothelial Cells
Author(s) -
RENKONEN R.,
MATTILA P.,
USTINOV J.
Publication year - 1990
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1990.tb02800.x
Subject(s) - protein kinase c , signal transduction , platelet activating factor , activator (genetics) , protein kinase a , microbiology and biotechnology , biology , second messenger system , cgmp dependent protein kinase , intracellular , phorbol , lymphocyte , kinase , biochemistry , endocrinology , mitogen activated protein kinase kinase , immunology , receptor
Platelet‐activating factor (PAF) is a lipid mediator of inflammation. PAF pretreatment of cultured endothelial cells leads to an increase in lymphocyte binding. We have analysed the intracellular signal transduction during this PAF‐induced effect. The protein kinase C activator, phorbol 12‐myristate, 13‐acetate, mimicked PAF in the binding assay. Concomitantly, the protein kinase C (PKC) inhibitor H7 down‐regulated the PAF‐induced binding to nearly control level. Also dibutyryl‐cAMP treatment of endothelial cells increased lymphocyte binding, but the protein kinase A inhibitor HA1004 did not alter the PAF‐induced binding. Furthermore, PAF did not increase the level of cytosolic cAMP in the endothelial cells. Other second messengers. cGMPandCa 2+ , had no effect on lymphocyte binding. These fmdings suggest that protein kinase C, but no other signal transduction pathway, is essential in the PAF‐induced lymphocyte binding to endothelial cells.