Schindler Clara K, Shinoda Sachiko, Simon Roger P, Henshall David C
Robert S. Dow Neurobiology Laboratories, Legacy Clinical Research and Technology Center, 1225 NE 2nd Avenue, Portland, OR 97232, USA.
Neurosci Lett. 2004 Feb 19;356(3):163-6. doi: 10.1016/j.neulet.2003.11.048.
The molecular regulation of seizure-induced neuronal death may involve interactions between proteins of the Bcl-2 and 14-3-3 families. To further examine these pathways we performed subcellular fractionation on hippocampi obtained following a brief period of status epilepticus in the rat. Western blotting determined seizures induced caspase-8 cleavage and increased Bcl-w levels within the cytoplasm. Bax, Bad and Bid were largely present within the cytoplasm before and after seizures, although some Bax and, following seizures, truncated Bid was detected in mitochondria. Levels of 14-3-3 were significantly reduced in the cytoplasm and microsomal fractions. These data establish the expression and distribution profile of key Bcl-2 family proteins and the signaling chaperone 14-3-3 in the rat and provide additional evidence for the activation of programmed cell death pathways by seizures.
癫痫发作诱导的神经元死亡的分子调控可能涉及Bcl-2家族和14-3-3家族蛋白之间的相互作用。为了进一步研究这些途径，我们对大鼠短暂癫痫持续状态后获得的海马体进行了亚细胞分级分离。蛋白质免疫印迹法测定癫痫发作诱导了半胱天冬酶-8的切割，并增加了细胞质中Bcl-w的水平。癫痫发作前后，Bax、Bad和Bid主要存在于细胞质中，尽管在癫痫发作后，线粒体中检测到了一些Bax和截短的Bid。细胞质和微粒体组分中14-3-3的水平显著降低。这些数据确定了大鼠中关键Bcl-2家族蛋白和信号伴侣14-3-3的表达和分布情况，并为癫痫发作激活程序性细胞死亡途径提供了额外证据。
