Zhou Y, Kok K H, Chun A C, Wong C M, Wu H W, Lin M C, Fung P C, Kung H, Jin D Y
Institute of Molecular Biology, Division of Medical Physics, Department of Medicine, University of Hong Kong, Pokfulam, Hong Kong, China.
Biochem Biophys Res Commun. 2000 Feb 24;268(3):921-7. doi: 10.1006/bbrc.2000.2231.
We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling.
我们通过与酵母过氧化物酶体抗氧化酶PMP20的序列同源性鉴定出了人和小鼠的过氧化物氧还蛋白V（Prx-V）。Prx-V是哺乳动物过氧化物氧还蛋白目前已知的六个亚家族中的第五个。它是一种在细菌中具有直系同源物的新型细胞器酶。从生化角度来看，Prx-V是一种硫氧还蛋白过氧化物酶。p53在哺乳动物细胞中的一个重要功能方面涉及可能由氧化还原介导的细胞凋亡诱导。我们发现Prx-V的过表达可防止p53依赖的活性氧生成。同样，Prx-V抑制p53诱导的细胞凋亡。因此，Prx-V在细胞内氧化还原信号传导中起关键作用。
