Effect of phorbol 12-myristate 13-acetate on Ca2+-ATPase activity in rat liver nuclei
β Scribed by Kimiko Oishi; Masayoshi Yamaguchi
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 426 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0730-2312
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β¦ Synopsis
The effect of phorbol 12-myristate 13-acetate (PMA) on Ca2+-ATPase activity in rat h e r nuclei was investigated. Ca2 +-ATPase activity was calculated by subtracting Mg2+ -ATPase activity from (Ca2 +-Mg2 +)-ATPase activity. The nuclear Ca2+-ATPase activity was significantly increased by the presence of PMA (2-20 pM) in the enzyme reaction mixture; the maximum effect was seen at 10 pM. The PMA (10 pM)-increased Ca2+-ATPase activity was not blocked by the presence of staurosporine (2 pM) or dibucaine (2 and 10 pM), an inhibitor of protein kinase. Meanwhile, vanadate (20 and 100 FM) caused a significant reduction in the nuclear Ca*+-ATPase activity increased by PMA (10 pM). The present finding suggests that PMA has an activating effect on liver nuclear Ca2+-ATPase independent of protein kinase.
π SIMILAR VOLUMES
The effect of Ca 2Ο© -binding protein regucalcin on Ca 2Ο© -ATPase activity in isolated rat liver mitochondria was investigated. The presence of regucalcin (0.1, 0.25, and 0.5 M) in the enzyme reaction mixture led to a significant increase in Ca 2Ο© -ATPase activity. Regucalcin significantly stimulated