中文摘要：

Necroptosis 是在各种各样的疾病被含有的调整房间死亡的一种类型。交往受体的蛋白质 3 (RIP3 ) ， RIP 家庭的一个成员，是 necroptotic 小径的一个重要调停人。在由 caspase-8 的 Asp328 的 RIP3 的劈开废除 RIP3 的 kinase 活动，它为 necroptosis 是批评的。而且， RIP3 是显著地 upregulated 在尖锐高 intra 眼睛的压力和氧葡萄糖剥夺的早阶段期间。在这研究， RIP3 的效果在提高的静水力学的压力(EHP ) 期间被调查， caspase-8 通过调整了 RIP3 劈开的可能的机制被探索。流动 cytometry 分析表明导致 EHP 的坏死的网膜的中心房间 5 的数字(RGC-5 ) 房间被减少在以后 RIP3 击倒。而且，在正常 RGC-5 房间的 malondialdehyde (MDA ) 层次和肝糖 phosphorylase (PYGL ) 活动比在在 EHP 以后的 RIP3 击倒的房间的那些高得多。导致 EHP 的 RGC-5 坏死显著地与 butylated hydroxyanisole (BHA ) 在处理以后被减少，反应的氧种类(ROS ) scavenger。MDA 层次和 PYGL 活动比在有在 EHP 以后的 caspase-8 抑制的房间的那些在正常 RGC-5 房间是更低的。西方的污点分析证明 RIP3 劈开产品是在有 caspase-8 抑制的房间的 upregulated。另外，流动 cytometry 分析表明导致 EHP 的坏死的 RGC-5 房间的数字在 caspase-8 抑制以后被增加。我们的结果建议 RGC-5 necroptosis 追随者 EHP 被 RIP3 通过 PYGL 活动和随后的 ROS 累积的正式就职调停。因此， caspase-8 可以经由 RIP3 劈开参予 RGC-5 necroptosis 的规定。

英文摘要：

Necroptosis is a type of regulated cell death that has been implicated in various diseases. Receptor-interacting protein 3 （RIP3）, a member of the RIP family, is an important mediator of the necroptotic pathway. Cleavage of RIP3 at Asp328 by caspase-8 abolishes the kinase activity of RIP3, which is critical for necroptosis. Moreover, RIP3 is significantly upregulated during the early stages of acute high intra-ocular pressure and oxygen glucose deprivation. In this study, the effects of RIP3 during elevated hydrostatic pressure （EHP） were investigated and the possible mechanism through which caspase-8 regulated RIP3 cleavage was explored. Flow cytometry ana- lysis revealed that the number of EHP-induced necrotic retinal ganglion cell 5 （RGC-5） cells was reduced after RIP3-knockdown. Furthermore, malondialdehyde （MDA） levels and glycogen phos- phorylase （PYGL） activity in normal RGC-5 cells were much higher than those in RIP3-knockdown cells after EHP. EHP-induced RGC-5 necrosis was significantly reduced after treatment with buty- lated hydroxyanisole （BHA）, a reactive oxygen species （ROS） scavenger. MDA levels and PYGL activity were lower in normal RGC-5 cells than those in cells with caspase-8 inhibition after EHP. Western blot analysis demonstrated that the RIP3 cleavage product was upregulated in cells with caspase-8 inhibition. Additionally, flow cytometry analysis revealed that the number of EHP- induced necrotic RGC-5 cells was increased after caspase-8 inhibition. Our results suggested that RGC-5 necroptosis following EHP was mediated by RIP3 through induction of PYGL activity and subsequent ROS accumulation, Thus, caspase-8 may participate in the regulation of RGC-5 necroptosis via RIP3 cleavage.