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Updated: Aug 9, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
Published on: January 7, 2013
Effect of phorbol 12-myristate 13-acetate on Ca2+-ATPase activity in rat liver nuclei
1Laboratory of Metabolism and Endocrinology, Graduate School of Nutritional Sciences, University of Shizuoka, Japan.
Abstract:
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.
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