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Induction of protein kinase C activation and Ca 2+ mobilization by fibroblast growth factor in Swiss 3T3 cells
Author(s) -
Tsuda Terutaka,
Kaibuchi Kozo,
Kawahara Yasuhiro,
Fukuzaki Hisashi,
Takai Yoshimi
Publication year - 1985
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(85)80009-0
Subject(s) - diacylglycerol kinase , protein kinase c , second messenger system , dna synthesis , fibroblast growth factor , protein kinase a , growth factor , biology , microbiology and biotechnology , fibroblast , phorbol , phosphatidylinositol , epidermal growth factor , endocrinology , kinase , chemistry , signal transduction , biochemistry , dna , receptor , in vitro
Addition of fibroblast growth factor (FGF) to quiescent cultures of Swiss 3T3 cells rapidly induced diacylglycerol formation, protein kinase C activation and Ca 2+ mobilization. Protein kinase C‐activating agents such as 12‐ O ‐tetradecanoylphorbol‐13‐acetate (TPA) and 1‐oleoyl‐2‐acetylglycerol (OAG) mimicked the action of FGF and stimulated DNA synthesis in the presence of insulin. Prolonged treatment of the cells with phorbol‐12,13‐dibutyrate (PDBu) led to the down‐regulation and complete disappearance of protein kinase C. In these cells, TPA and OAG did not induce DNA synthesis any more. FGF still elicited Ca 2+ mobilization and DNA synthesis, but the magnitude of DNA synthesis was reduced to almost half as compared with that in the control cells. These results clearly indicate that both diacylglycerol and Ca 2+ may serve as second messengers for FGF and suggest that these messengers may be involved in the mitogenic action of this growth factor.