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Protein kinase C activation by interleukin (IL)‐1 limits IL‐1‐induced IL‐6 synthesis in osteoblast‐like cells: Involvement of phosphatidylcholine‐specific phospholipase C
Author(s) -
Kozawa Osamu,
Suzuki Atsushi,
Tokuda Haruhiko,
Kaida Takehiro,
Uematsu Toshihiko
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19971001)67:1<103::aid-jcb11>3.0.co;2-i
Subject(s) - protein kinase c , osteoblast , chemistry , phosphatidylcholine , microbiology and biotechnology , phospholipase d , kinase , enzyme , biochemistry , biology , phospholipid , in vitro , membrane
We investigated the regulatory mechanism of interleukin‐6 (IL‐6) synthesis induced by interleukin‐1 (IL‐1) in osteoblast‐like MC3T3‐E1 cells. IL‐1 stimulated the secretion of IL‐6 in a dose‐dependent manner in the range between 0.1 and 100 ng/ml. Staurosporine and calphostin C, inhibitors of protein kinase C (PKC), significantly enhanced the IL‐1‐induced secretion of IL‐6. The stimulative effect of IL‐1 was markedly amplified in PKC down‐regulated MC3T3‐E1 cells. IL‐1 produced diacylglycerol in MC3T3‐E1 cells. IL‐1 had little effect on the formation of inositol phosphates and choline. On the contrary, IL‐1 significantly stimulated the formation of phosphocholine dose‐dependently. D‐609, an inhibitor of phosphatidylcholine‐specific phospholipase C, suppressed the IL‐1‐induced diacylglycerol production. The IL‐1‐induced IL‐6 secretion was significantly enhanced by D‐609. These results indicate that IL‐1 activates PKC via phosphatidylcholine‐specific phospholipase C in osteoblast‐like cells, and the PKC activation then limits IL‐6 synthesis induced by IL‐1 itself. J. Cell. Biochem. 67:103–111, 1997. © 1997 Wiley‐Liss, Inc.