Involvement of thio-, peroxi-, and glutaredoxins in cellular redox-dependent processes

Among the key antioxidant enzymes, thioredoxin and glutaredoxin systems play an important role in cell defense against oxidative stress and maintenance of redox homeostasis owing to the regulation of thiol-disulfide exchange. The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H 2O2, and peroxynitrite. NADPH-dependent thioredoxin reductase, which reduces a broad range of substrates including oxidized form of thioredoxin, can also directly reduce lipid hydroperoxides, H2O 2, and dehydroascorbic and lipoic acids. Glutaredoxin, whose major isoforms in mammals are Grx1, Grx2, and Grx5, as well as thioredoxin, catalyzes S-glutathionylation and deglutathionylation of proteins to protect SH-groups from oxidation and restore functionally active thiols. However, in contrast to thioredoxin, glutaredoxin reduces GSH-mixed disulfides and catalyzes the reaction not only via a dithiol mechanism but also via monothiol reduction. In addition to the role in cellular antioxidant defense, all of the reviewed redox proteins (thioredoxin, thioredoxin reductase, peroxiredoxin, and glutaredoxin) have a number of significant functions required for cell viability: they regulate transcription factor activities, play the role of growth factors, serve as enzyme cofactors, take part in regulation of cell cycle, and are involved in antiapoptotic mechanisms. © 2008 MAIK Nauka.

Authors
Kalinina E.V. 1, 2 , Chernov N.N. 3 , Saprin A.N.1
Number of issue
13
Language
English
Pages
1493-1510
Status
Published
Volume
73
Year
2008
Organizations
  • 1 Center for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, ul. Kosygina 4, Moscow 119991, Russian Federation
  • 2 Institute of Cytochemistry and Molecular Pharmacology, 6-ya Radial'naya ul. 24/14, Moscow 115404, Russian Federation
  • 3 Peoples' Friendship University of Russia, ul. Miklukho-Maklaya 8, Moscow 117198, Russian Federation
Keywords
Glutaredoxin; Oxidative stress; Peroxiredoxin; Redox-dependent processes; Thioredoxin; Thioredoxin reductase
Date of creation
19.10.2018
Date of change
19.10.2018
Short link
https://repository.rudn.ru/en/records/article/record/3037/
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