Activation of protein kinase C and the involvement of prostaglandin E2 in the inhibition of osteosarcoma-derived cell alkaline phosphatase activity.
We present evidence for the presence of specific, high-affinity binding sites for tritiated phorbol 12,13-dibutyrate on osteosarcoma-derived (HT-3) cells. Activation of protein kinase C by a phorbol ester resulted in an inhibition of alkaline phosphatase activity and the accumulation of prostaglandin E2. Indomethacin blocked prostaglandin E2 production and enhanced alkaline phosphatase activity. These data suggest that prostaglandin E2 is enhanced by activation of protein kinase C, and in turn, alkaline phosphatase activity is reduced.
Fukuda
K
K
Department of Orthopaedic Surgery, Kinki University School of Medicine, Osaka, Japan.
Ueno
M
M
Saitoh
M
M
Nishioka
S
S
Tanaka
S
S
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D004247:DNA / Q000096:biosynthesis; D015232:Dinoprostone / Q000096:biosynthesis* / Q000494:pharmacology; D004789:Enzyme Activation; D007213:Indomethacin / Q000494:pharmacology; D007700:Kinetics; D012516:Osteosarcoma / Q000201:enzymology*; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D015240:Phorbol 12,13-Dibutyrate; D004247:DNA; D011493:Protein Kinase C; D000469:Alkaline Phosphatase; D015232:Dinoprostone; D007213:Indomethacin