Oishi K, Yamaguchi M
Laboratory of Metabolism and Endocrinology, Graduate School of Nutritional Sciences, University of Shizuoka, Japan.
J Cell Biochem. 1994 Jun;55(2):168-72. doi: 10.1002/jcb.240550203.
The effect of phorbol 12-myristate 13-acetate (PMA) on Ca(2+)-ATPase activity in rat liver nuclei was investigated. Ca(2+)-ATPase activity was calculated by subtracting Mg(2+)-ATPase activity from (Ca(2+)-Mg(2+)-ATPase activity. The nuclear Ca(2+)-ATPase activity was significantly increased by the presence of PMA (2-20 microM) in the enzyme reaction mixture; the maximum effect was seen at 10 microM. The PMA (10 microM)-increased Ca(2+)-ATPase activity was not blocked by the presence of staurosporine (2 microM) or dibucaine (2 and 10 microM), an inhibitor of protein kinase. Meanwhile, vanadate (20 and 100 microM) caused a significant reduction in the nuclear Ca(2+)-ATPase activity increased by PMA (10 microM). The present finding suggests that PMA has an activating effect on liver nuclear Ca(2+)-ATPase independent of protein kinase.
研究了佛波醇12 - 肉豆蔻酸酯13 - 乙酸酯(PMA)对大鼠肝细胞核中Ca(2 +)-ATP酶活性的影响。Ca(2 +)-ATP酶活性通过从(Ca(2 +)-Mg(2 +)-ATP酶活性中减去Mg(2 +)-ATP酶活性来计算。在酶反应混合物中存在PMA(2 - 20微摩尔)时,细胞核Ca(2 +)-ATP酶活性显著增加;在10微摩尔时观察到最大效应。PMA(10微摩尔)增加的Ca(2 +)-ATP酶活性不受星形孢菌素(2微摩尔)或二丁卡因(2和10微摩尔,一种蛋白激酶抑制剂)的存在的阻断。同时,钒酸盐(20和100微摩尔)使PMA(10微摩尔)增加的细胞核Ca(2 +)-ATP酶活性显著降低。目前的发现表明,PMA对肝细胞核Ca(2 +)-ATP酶具有独立于蛋白激酶的激活作用。