TY - JOUR
T1 - Synergistic action of protein kinase C and calcium for histamine release from rat peritoneal mast cells
AU - Katakami, Yuko
AU - Kaibuchi, Kozo
AU - Sawamura, Makoto
AU - Takai, Yoshimi
AU - Nishizuka, Yasutomi
N1 - Funding Information:
*/ This investigation was supported in part by research grants from the S&ntific Research Fund of the Ministry of Education, Science and Culture, Japan (1982-1984), the Intractable Diseases Division, Public Health Bureau, the Ministry of Health and Welfare, Japan (1982-1984), a Grant-in-Aid of New Drug Development from the Ministry of Health and Welfare, Japan (1983), the Science and Technology Agency (1983), and the Yamanouchi Foundation for Research on Metabolic Disorders (1982-1983). The data are taken in part from the dissertation that will be submitted by Y. Katakami to Kobe University School of Medicine in partial fulfilment of the requirement for the degree of Doctor of Medical Science. l/ Abbreviations used are: IgE, immunoglobulin phosphatidylinositol; OAG, 1-oleoyl-2-acetyl-glycerol; phorbol-13-acetate; EGTA, ethylene glycol bis(B-aminoethyl tetraacetic acid; PMSF, phenylmethylsulfonyl fluoride; sulfate; and PS, phosphatidylserine.
PY - 1984/6/15
Y1 - 1984/6/15
N2 - When rat mast cells were stimulated by concanavalin A, phosphatidylinositol turnover was induced. Concurrently, several cytosol proteins were phosphorylated and histamine was released. 1-Oleoyl-2-acetyl-glycerol (OAG) and 12-O-tetradecanoylphorbol-13-acetate (TPA), known as direct activators of protein kinase C in intact cells, induced phosphorylation of the same spectrum of proteins. These proteins also served in vitro as preferable substrates for protein kinase C. The simultaneous addition of OAG or TPA and A23187 synergistically enhanced histamine release from mast cells. It is suggestive that protein kinase C activation and Ca2+ mobilization play essential roles for this cellular response.
AB - When rat mast cells were stimulated by concanavalin A, phosphatidylinositol turnover was induced. Concurrently, several cytosol proteins were phosphorylated and histamine was released. 1-Oleoyl-2-acetyl-glycerol (OAG) and 12-O-tetradecanoylphorbol-13-acetate (TPA), known as direct activators of protein kinase C in intact cells, induced phosphorylation of the same spectrum of proteins. These proteins also served in vitro as preferable substrates for protein kinase C. The simultaneous addition of OAG or TPA and A23187 synergistically enhanced histamine release from mast cells. It is suggestive that protein kinase C activation and Ca2+ mobilization play essential roles for this cellular response.
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U2 - 10.1016/0006-291X(84)90220-1
DO - 10.1016/0006-291X(84)90220-1
M3 - Article
C2 - 6203533
AN - SCOPUS:0021253512
SN - 0006-291X
VL - 121
SP - 573
EP - 578
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -