Phospholipid-sensitive, Ca2+-dependent protein kinase activity in rat embryo fibroblasts transformed by herpes simplex virus type 2.
Increased cytosolic phospholipid-sensitive, Ca2+-dependent protein kinase C (PK-C) activity is correlated with the highly tumorigenic potential of rat embryo fibroblasts transformed by herpes simplex virus type 2 (HSV-2). Treatment of the cells with 12-O-tetradecanoylphorbol-13-acetate (TPA) caused a decrease in the cytosolic PK-C with a concomitant increase in PK-C recovered in the membrane fraction. Translocation of the PK-C was dependent upon length of exposure to the phorbol diester. PK-C activity in the cytosolic fraction could be stimulated by TPA without the addition of phosphatidylserine and diacylglycerol. It is tempting to speculate that HSV-2 induction of cellular PK-C activity may be important in phosphorylation of proteins needed for promotion of HSV-2-induced carcinogenesis.
Roddick
V L
VL
Department of Biochemistry, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, N.C.
Krebs
C R
CR
Kucera
L S
LS
Daniel
L W
LW
Waite
M
M
D000818:Animals; D002471:Cell Transformation, Neoplastic / Q000201:enzymology*; D002472:Cell Transformation, Viral; D004622:Embryo, Mammalian; D004790:Enzyme Induction / Q000187:drug effects; D005347:Fibroblasts / Q000201:enzymology*; D009363:Neoplasm Proteins / Q000032:analysis*; D011493:Protein Kinase C / Q000032:analysis*; D051381:Rats; D011915:Rats, Inbred BUF; D018139:Simplexvirus / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D009363:Neoplasm Proteins; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate