TUMOR NECROSIS FACTOR-ALPHA-DEPENDENT ACTIVATION OF A RELA HOMODIMER IN ASTROCYTES - INCREASED PHOSPHORYLATION OF RELA AND MAD-3 PRECEDE ACTIVATION OF RELA
TUMOR NECROSIS FACTOR-ALPHA-DEPENDENT ACTIVATION OF A RELA HOMODIMER IN ASTROCYTES - INCREASED PHOSPHORYLATION OF RELA AND MAD-3 PRECEDE ACTIVATION OF RELA
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DOI：
10.1074/jbc.270.6.2703
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发表时间：
1995-02-10
影响因子：
4.8
通讯作者：
HANNINK, M
中科院分区：
文献类型：
--
作者：
DIEHL, JA;TONG, W;HANNINK, M
Rel 蛋白是细胞因子诱导的信号转导的重要细胞内介质。为了了解细胞因子如何影响大脑中不同的细胞群，我们对星形胶质细胞中的 Rel 激活进行了表征。 RelA 同二聚体在细胞因子刺激的星形胶质细胞中被独特地激活。 RelA 抑制剂 MAD-3 在从 RelA 解离之前发生在离散肽上的细胞因子依赖性磷酸化。还诱导了 RelA 的短暂过度磷酸化。抗氧化剂治疗抑制RelA激活和RelA(.)MAD-3复合物的磷酸化。这些结果证明RelA同二聚体的细胞因子依赖性激活涉及RelA及其相关抑制剂的磷酸化。 RelA 同二聚体的唯一激活表明细胞因子将激活星形胶质细胞中一组独特的 Rel 调节基因。
Rel proteins are important intracellular mediators of cytokine-induced signal transduction. To understand how cytokines affect different cell populations in the brain, we have characterized Rel activation in astrocytes. A RelA homodimer is uniquely activated in cytokine-stimulated astrocytes. Cytokine-dependent phosphorylation of the RelA inhibitor MAD-3 occurred on discrete peptides prior to its dissociation from RelA. A transient hyperphosphorylation of RelA was also induced. Antioxidant treatment inhibited both RelA activation and phosphorylation of the RelA(.)MAD-3 complex, These results demonstrate that cytokine-dependent activation of the RelA homodimer involves phosphorylation of both RelA and its associated inhibitor. The sole activation of a RelA homodimer suggests that cytokines will activate a unique set of Rel-regulated genes in astrocytes.