Neutrophil oxygen reduction: The enzymes and the products

Alfred I. Tauber , Bernard M. Babior
{"title":"Neutrophil oxygen reduction: The enzymes and the products","authors":"Alfred I. Tauber ,&nbsp;Bernard M. Babior","doi":"10.1016/8755-9668(85)90010-9","DOIUrl":null,"url":null,"abstract":"<div><p>The human neutrophil generates a non-mitochondrial respiratory burst by the activation of a NADPH-oxidase, whose electron source, NADPH, is generated in the hexose monophosphate shunt. The reduction product, <sub>2</sub><sup>−</sup>, is further reduced to H<sub>2</sub>O<sub>2</sub>, which upon the action of myeloperoxidase, oxidizes halide to form reactive chloramines and hypochlorous acid. The elusive hydroxyl radical, or kindred species, also appears as a product of the burst, but this chemistry has not been elucidated. NADPH-oxidase is a complex activity, comprised of at least two components: a low potential b cytochrome and a flavoprotein. Partial characterization and isolation of this electron transport system has been accomplished and serves as an intense focus of current research. The recent demonstration that the oxidase may be activated in a broken cell preparation should not only define mechanisms of burst activation, but this methodology should provide a powerful approach towards identifying the components of the NADPH-oxidase apparatus.</p></div>","PeriodicalId":100046,"journal":{"name":"Advances in Free Radical Biology & Medicine","volume":"1 2","pages":"Pages 265-307"},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/8755-9668(85)90010-9","citationCount":"82","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in Free Radical Biology & Medicine","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/8755966885900109","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 82

Abstract

The human neutrophil generates a non-mitochondrial respiratory burst by the activation of a NADPH-oxidase, whose electron source, NADPH, is generated in the hexose monophosphate shunt. The reduction product, 2, is further reduced to H2O2, which upon the action of myeloperoxidase, oxidizes halide to form reactive chloramines and hypochlorous acid. The elusive hydroxyl radical, or kindred species, also appears as a product of the burst, but this chemistry has not been elucidated. NADPH-oxidase is a complex activity, comprised of at least two components: a low potential b cytochrome and a flavoprotein. Partial characterization and isolation of this electron transport system has been accomplished and serves as an intense focus of current research. The recent demonstration that the oxidase may be activated in a broken cell preparation should not only define mechanisms of burst activation, but this methodology should provide a powerful approach towards identifying the components of the NADPH-oxidase apparatus.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
中性粒细胞氧还原:酶和产物
人中性粒细胞通过NADPH氧化酶的激活产生非线粒体呼吸爆发,其电子源NADPH在单磷酸己糖分流中产生。还原产物2−进一步还原为H2O2,在髓过氧化物酶的作用下,将卤化物氧化生成活性氯胺和次氯酸。难以捉摸的羟基自由基,或类似的物种,也作为爆发的产物出现,但这种化学反应尚未被阐明。nadph氧化酶是一种复杂的活性,由至少两种成分组成:低电位b细胞色素和黄素蛋白。该电子传递系统的部分表征和分离已经完成,并成为当前研究的热点。最近的研究表明,氧化酶可能在破碎的细胞中被激活,这不仅定义了破裂激活的机制,而且这种方法应该为识别nadph氧化酶装置的组成提供了有力的方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Glucose starvation induced upregulation of Prohibitin 1 via ROS generation causes mitochondrial dysfunction and apoptosis in breast cancer cells. Gender differences in albumin and ascorbic acid in the vitreous antioxidant system. A Comment on Free Radical Nomenclature Superoxide radical: A likely link between reperfusion injury and inflammation Free radicals in tumor promotion
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1