Scirè Andrea, Casari Giulia, Romaldi Brenda, de Bari Lidia, Antognelli Cinzia, Armeni Tatiana
Department of Life and Environmental Sciences (Di.S.V.A.), Università Politecnica delle Marche, 60131 Ancona, Italy.
Department of Odontostomatologic and Specialized Clinical Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.
Antioxidants (Basel). 2023 Nov 7;12(11):1976. doi: 10.3390/antiox12111976.
Hemoglobin is one of the proteins that are more susceptible to S-glutathionylation and the levels of its modified form, glutathionyl hemoglobin (HbSSG), increase in several human pathological conditions. The scope of the present review is to provide knowledge about how hemoglobin is subjected to S-glutathionylation and how this modification affects its functionality. The different diseases that showed increased levels of HbSSG and the methods used for its quantification in clinical investigations will be also outlined. Since there is a growing need for precise and reliable methods for markers of oxidative stress in human blood, this review highlights how HbSSG is emerging more and more as a good indicator of severe oxidative stress but also as a key pathogenic factor in several diseases.
血红蛋白是最易发生S-谷胱甘肽化的蛋白质之一,其修饰形式谷胱甘肽化血红蛋白(HbSSG)的水平在几种人类病理状况下会升高。本综述的目的是提供关于血红蛋白如何发生S-谷胱甘肽化以及这种修饰如何影响其功能的知识。还将概述临床研究中显示HbSSG水平升高的不同疾病以及用于其定量的方法。由于对人类血液中氧化应激标志物的精确可靠方法的需求日益增长,本综述强调了HbSSG如何越来越多地成为严重氧化应激的良好指标,同时也是几种疾病的关键致病因素。