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Protein kinase C controls Fcγ receptor‐mediated endocytosis in human neutrophils
Author(s) -
Ion I. Moraru,
Mariana Laky,
T Stãnescu,
L Buzilă,
L. M. Popescu
Publication year - 1990
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(90)81337-n
Subject(s) - endocytosis , protein kinase c , microbiology and biotechnology , receptor mediated endocytosis , activator (genetics) , sphingosine , receptor , chemistry , phospholipase c , biology , kinase , signal transduction , biochemistry
The aim of this study is to clarify which signaling mechanism operates in Fcγ receptor‐mediated endocytosis in human neutrophils. Endocytosis of immune complexes was inhibited by antibodies directed to cell membrane phospholipase C (PLC) and A 2 (PLA 2 ) (maximal inhibition obtained was 57% and 28%, respectively), being almost abolished by these antibodies if used in combination (up to 91% inhibition). The protein kinase C (PKC) activator, phorbol 12,13‐dibutyrate, reversed this inhibitory effect. Four different PKC inhibitors (H‐7, palmitoylcarnitine, sphingosine. and tamoxifen) produced a dose‐dependent inhibition of endocytosis, up to over 80% in each case. H‐8 (1–10μM) which inhibits cyclic nucleotide protein kinases but not PKC had no effect upon endocytosis. It is concluded that Fcγ receptor‐induced activation of PLC and PLA 2 triggers endocytosis by activation of PKC.