Induction of Akt phosphorylation in rat primary astrocytes by H2O2 occurs upstream of phosphatidylinositol 3-kinase: no evidence for oxidative inhibition of PTEN.
Induction of Akt phosphorylation in rat primary astrocytes by H2O2 occurs upstream of phosphatidylinositol 3-kinase: no evidence for oxidative inhibition of PTEN.
复制标题
H2O2 在大鼠原代星形胶质细胞中诱导 Akt 磷酸化发生在磷脂酰肌醇 3-激酶的上游：没有证据表明 PTEN 的氧化抑制。
DOI：
10.1006/abbi.2000.2202
复制
发表时间：
2001
影响因子：
3.9
通讯作者：
Hensley,K
中科院分区：
文献类型：
--
作者：
Salsman,S;Felts,N;Pye,QN;Floyd,RA;Hensley,K
Phosphorylation of the serine/threonine kinase Akt has previously been shown to be increased by treatment of cells with H2O2; the target of H2O2has not been clearly identified. Here we show that treatment of rat primary astrocytes with H2O2resulted in increased Akt phosphorylation that was blocked by wortmannin. The thiol-reducing agent N-acetylcysteine had only a slight inhibitory effect. Treatment with rotenone or antimycin A also resulted in increased wortmannin-sensitive Akt phosphorylation, probably by increasing intracellular H2O2generation by blocking mitochondrial electron transport. Addition of phosphatidylinositol 3,4-bisphosphate to cells also resulted in an increase in Akt phosphorylation. This increase was additive to that induced by H2O2and was also blocked by wortmannin. These results suggest that activation of Akt by H2O2occurs upstream of phosphatidylinositol 3-kinase (PI 3-K) activity in astrocytes. The data indicate that major oxidative effects do not occur at the level of the PI 3-K-antagonizing phosphatase PTEN.
