Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells.
Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells.
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DOI：
10.1006/bbrc.2001.4700
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发表时间：
2001-04
影响因子：
3.1
通讯作者：
Masato Matsuoka;H. Igisu
中科院分区：
文献类型：
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作者：
Masato Matsuoka;H. Igisu
当MCF-7细胞与10或20 μ M CdCl（2）孵育18小时后，p53蛋白水平增加。在CdCl（2）处理的细胞免疫沉淀的p53蛋白中，只有Ser 15被磷酸化。在Ser 6、9、20、37和392上没有发现明显的磷酸化。暴露18 h后，在Ser 15处磷酸化的p53蛋白也被发现积累。虽然在CdCl处理的细胞中发现了细胞外信号调节蛋白激酶、c-Jun NH 2-末端激酶和p38的磷酸化（2），但U 0126、LL-Z1640-2或SB 203580处理不能抑制Ser 15磷酸化。另一方面，wortmannin或咖啡因处理抑制CdCl（2）诱导的Ser 15磷酸化和p53蛋白的积累。本研究结果表明，镉诱导MCF-7细胞中p53丝氨酸15的磷酸化依赖于磷脂酰肌醇3-激酶相关激酶，但不依赖于丝裂原活化蛋白激酶。
When MCF-7 cells were incubated with 10 or 20 microM CdCl(2), p53 protein level increased after 18 h. Among serines in p53 protein immunoprecipitated from cells treated with CdCl(2), only Ser 15 was phosphorylated. No clear phosphorylation was found on Ser 6, 9, 20, 37, and 392. Accumulation of p53 protein phosphorylated at Ser 15 was also found after 18 h exposure. While phosphorylation of extracellular signal-regulated protein kinase, c-Jun NH2-terminal kinase and p38 was found in cells treated with CdCl(2), treatment with U0126, LL-Z1640-2, or SB203580 did not suppress Ser 15 phosphorylation. On the other hand, treatment with wortmannin or caffeine suppressed CdCl(2)-induced Ser 15 phosphorylation and accumulation of p53 protein. The present results showed that cadmium induces phosphorylation of p53 at Ser 15 in MCF-7 cells depending on phosphatidylinositol 3-kinase related kinases, but not on mitogen-activated protein kinases.