Abstract
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease. J. Cell. Biochem. 114: 1962-1968, 2013.
Original language | English |
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Pages (from-to) | 1962-1968 |
Number of pages | 7 |
Journal | Journal of Cellular Biochemistry |
Volume | 114 |
Issue number | 9 |
DOIs | |
Publication status | Published - Sept 2013 |
Keywords
- GLUTAREDOXIN-1
- PROTEIN S-GLUTATHIONYLATION
- REDOX
- BIOTIN SWITCH
- DISULFIDE BOND FORMATION
- REDOX-BASED REGULATION
- ENDOPLASMIC-RETICULUM
- SIGNAL-TRANSDUCTION
- CYSTEINE DERIVATIZATION
- MOLECULAR-MECHANISMS
- PEROXIREDOXIN
- APOPTOSIS