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作 者:张莉(综述)[1] 屈艺[1] 母得志(审校)[1]
出 处:《国际儿科学杂志》2010年第2期116-118,共3页International Journal of Pediatrics
基 金:国家自然科学基金资助项目(30825039,30770748);四川省青年科技基金项目(08ZQ026-069)
摘 要:缺氧诱导因子-1(hypoxia inducible factor-1, HIF-1)是机体氧平衡调节的重要转录因子,由α和β两种亚基组成,受氧分压调节的HIF-1α在蛋白质翻译后水平被多种方式修饰,如泛素化、磷酸化、羟基化、乙酰化、糖基化等,从而影响其蛋白稳定性、核转位以及对靶基因的转录调节等。小泛素相关修饰物(small ubiquitin-related modifier, SUMO)是一种参与真核生物可逆性蛋白质翻译后修饰的小分子蛋白,结构与泛素相似。SUMO化和去SUMO化修饰参与许多生物学过程的调节,包括细胞信号传导、转录调控、细胞周期进程及生物节律等。SUMO化修饰与低氧条件下HIF-1α的稳定性和转录活性相关,为了解HIF-1α的自身调控机制提供了新思路。Hypoxia-inducible factor-1 (HIF-1) is a key transciptional regulator of cellular and systemic oxygen homeostasis,composed of the two subunits, HIF-la and HIF-1β. HIF-1α is an inducible subunit regulated by hypoxia, which is posttranslationally modified by various ways, including ubiquitination, phosphorylation, hydroxylafion, aeetylation and glycation, accordingly affecting its protein' s stability, nuclear translocation and regulation of its target genes. Small ubiquitin-related modifier (SUMO) is an micromolecule protein participating in posttranslational modifications of proteins dynamiely in eukaryofic organism, which is similar in structure to ubiquitin. SUMOylafion and deSUMOylation are involved in multiple regulations of biologic processes, such as signal transduction, transcriptional regulation, cell cycle processes and biological rhythm. SUMOylation is related to HIF-1α stability and transcription activity in hypoxia, providing a newthread to study self-regulation mechanism of HIF-1α for us.
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