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Protein S-glutathionylation: from current basics to targeted modifications
1Institute of Cellular Biology and Pathology "N. Simionescu" of the Romanian Academy , 8, B.P. Hasdeu Street, Bucharest 050568 , Romania.
Protein S-glutathionylation, a reversible modification, protects cells from oxidative stress. This redox switch regulates cell survival and death, offering potential therapeutic strategies for cardiovascular diseases.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Protein S-glutathionylation is a redox-dependent post-translational modification involving antioxidant glutathione and protein thiols.
- This modification is crucial for cellular homeostasis and plays a role in oxidative stress-related cardiovascular pathology due to redox imbalance.
Purpose of the Study:
- To review recent advancements in protein S-glutathionylation.
- Focus areas include its chemistry, cellular functions, quantification methods, and therapeutic potential.
Main Methods:
- Literature review of Medline and PubMed databases.
- Search terms included 'glutathionylation' for articles published between 2009 and 2014.
Main Results:
- Protein S-glutathionylation protects protein thiols from irreversible oxidation.
- It acts as a biological redox switch, influencing cell survival pathways (kinases, phosphatases) and cell death (apoptosis).
- This modification interacts with phosphorylation and S-nitrosylation.
Conclusions:
- Protein S-glutathionylation is a key regulator of cellular redox state.
- It serves as a valuable biomarker for oxidative stress.
- It holds significant potential for developing novel therapeutic strategies.
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