ACTIVATION OF PROTEIN-KINASE-C AND THE INVOLVEMENT OF PROSTAGLANDIN E(2) IN THE INHIBITION OF OSTEOSARCOMA-DERIVED CELL ALKALINE-PHOSPHATASE ACTIVITY
Citation
K. Fukuda et al., ACTIVATION OF PROTEIN-KINASE-C AND THE INVOLVEMENT OF PROSTAGLANDIN E(2) IN THE INHIBITION OF OSTEOSARCOMA-DERIVED CELL ALKALINE-PHOSPHATASE ACTIVITY, The Journal of laboratory and clinical medicine, 126(3), 1995, pp. 269-274
Categorie Soggetti
Medical Laboratory Technology","Medicine, General & Internal
SICI code
0022-2143(1995)126:3<269:AOPATI>2.0.ZU;2-S
Abstract
We present evidence for the presence of specific, high-affinity bindin
g sites for tritiated phorbol 12,13-dibutyrate on osteosarcoma-derived
(HT-3) cells. Activation of protein kinase C by a phorbol ester resul
ted in an inhibition of alkaline phosphatase activity and the accumula
tion of prostaglandin E(2). Indomethacin blocked prostaglandin E(2) pr
oduction and enhanced alkaline phosphatase activity, These data sugges
t that prostaglandin E(2) is enhanced by activation of protein kinase
C, and in turn, alkaline phosphatase activity is reduced.