期刊
FEBS LETTERS
卷 593, 期 14, 页码 1799-1806出版社
WILEY
DOI: 10.1002/1873-3468.13454
关键词
apoptosis; glutaredoxins; glutathione; S-denitrosylation; thioredoxin
资金
- Karolinska Institutet Funding Source: Medline
- Swedish Cancer Society Funding Source: Medline
- Swedish Research Council Funding Source: Medline
Glutaredoxins (Grx) are involved in many reactions including defense against oxidative stress. However, the role of the Grx system under nitrosative stress has barely been investigated. In this study, we found that human Grxs denitrosylated both low and high molecular weight S-nitrosothiols. Some S-nitrosylated proteins, stable in the presence of a physiological concentration of glutathione (GSH), were denitrosylated by Grxs. Caspase 3 and cathepsin B were identified as substrates of Grx1-catalysed denitrosylation. In addition, mono-thiol Grxs, such as Grx5, exhibited denitrosylase activity coupled with GSH via a monothiol mechanism. Our study demonstrates the ability of Grxs to act as S-denitrosylases and pinpoint a new mechanism for denitrosylation.
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