蛋白激酶C的激活和前列腺素E2参与骨肉瘤源性细胞碱性磷酸酶活性的抑制。

The Journal of laboratory and clinical medicine Pub Date : 1995-09-01

K Fukuda, M Ueno, M Saitoh, S Nishioka, S Tanaka

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引用次数: 0

摘要

我们提供的证据表明，在骨肉瘤来源的(HT-3)细胞上存在特定的、高亲和力的12,13-二丁酸磷结合位点。磷酸酯激活蛋白激酶C可抑制碱性磷酸酶活性和前列腺素E2的积累。吲哚美辛阻断前列腺素E2的产生，增强碱性磷酸酶活性。这些数据表明，前列腺素E2通过蛋白激酶C的激活而增强，反过来，碱性磷酸酶活性降低。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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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.

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The Journal of laboratory and clinical medicine

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