蛋白激酶C的激活以及前列腺素E2在骨肉瘤来源细胞碱性磷酸酶活性抑制中的作用。
Activation of protein kinase C and the involvement of prostaglandin E2 in the inhibition of osteosarcoma-derived cell alkaline phosphatase activity.
作者信息
Fukuda K, Ueno M, Saitoh M, Nishioka S, Tanaka S
机构信息
Department of Orthopaedic Surgery, Kinki University School of Medicine, Osaka, Japan.
出版信息
J Lab Clin Med. 1995 Sep;126(3):269-74.
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.
我们提供了氚标记的佛波醇12,13 - 二丁酸酯在骨肉瘤衍生的（HT - 3）细胞上存在特异性、高亲和力结合位点的证据。佛波酯激活蛋白激酶C导致碱性磷酸酶活性受到抑制以及前列腺素E2的积累。吲哚美辛阻断前列腺素E2的产生并增强碱性磷酸酶活性。这些数据表明，蛋白激酶C的激活会增强前列腺素E2的生成，进而降低碱性磷酸酶的活性。
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