The activity of recombinant human neuroglobin as an antioxidant and free radical scavenger
The activity of recombinant human neuroglobin as an antioxidant and free radical scavenger
复制标题
重组人神经球蛋白作为抗氧化剂和自由基清除剂的活性
DOI：
10.1002/prot.22863
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发表时间：
2011-01-01
影响因子：
2.9
通讯作者：
Zhang, Chenggang
中科院分区：
文献类型：
--
作者：
Li, Weiguang;Wu, Yonghong;Zhang, Chenggang
自由基是代谢的副产物，在体内以生成和清除之间的稳态存在。过量的自由基会导致各种疾病，包括神经系统疾病。脑红蛋白（Neuroglobin，Ngb）是一种神经系统特异性的氧结合蛋白，被认为是体内神经系统潜在的自由基清除剂，但其作用机制尚不清楚。在这项研究中，我们研究了重组人Ngb（rhNgb）在体外的抗氧化能力和自由基清除特性。有趣的是，我们发现rhNgb蛋白本身具有直接和独特的抗氧化能力，并且可以有效地清除各种自由基，包括[2，2 '-连氮基-二-（3-乙基-苯并噻唑啉-6-磺酸）]（ABTS）阳离子、超氧阴离子、过氧化氢和羟基自由基。rhNgb清除超氧阴离子和过氧化氢的能力甚至与维生素C相当。rhNgb具有螯合Fe ~（2+）的活性，而血红蛋白则没有。以上结果表明，rhNgb蛋白本身具有抗氧化和清除自由基的活性，为Ngb的神经保护功能提供了基础证据。这些数据为Ngb的神经保护和生理作用的起源提供了关键信息，并将促进使用这种新型氧结合球蛋白治疗活性氧（ROS）相关疾病。Proteins 2011; 79：115-125. (C)2010 Wiley-Liss，Inc.
Free radicals are by-products of metabolism and exist in a homeostasis between generation and scavenging in vivo. Excessive free radicals cause various diseases, including nervous system diseases. Neuroglobin (Ngb), a nervous system-specific oxygen-binding protein, has been suggested to be a potential free radical scavenger in the nervous system in vivo; however, its underlying mechanism remains unclear. In this study, we investigated the antioxidant potential and free radical scavenging properties of recombinant human Ngb (rhNgb) in vitro. Interestingly, we found that the rhNgb protein itself has a direct and distinct antioxidant capacity and can efficiently scavenge a variety of free radicals, including the [2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulfonic acid)] (ABTS) cation, superoxide anion, hydrogen peroxide, and hydroxyl radical. The capacity of rhNgb to scavenge the superoxide anion and hydrogen peroxide was even comparable to that of vitamin C. In addition, rhNgb had Fe2+ chelating activity but hemoglobin did not. In conclusion, our results indicated that the rhNgb protein itself has antioxidant and free radical scavenging activities, providing fundamental evidence for the neuroprotective function of Ngb. These data provide key information for the origin of the neuroprotective and physiological role of Ngb and will promote the treatment of reactive oxygen species (ROS)-related diseases using this novel oxygen-binding globin. Proteins 2011; 79: 115-125. (C) 2010 Wiley-Liss, Inc.