NYMC Faculty Publications
A Comparison of Reversible Versus Irreversible Protein Glutathionylation
First Page
177
Last Page
198
Document Type
Article
Publication Date
6-25-2014
Department
Biochemistry and Molecular Biology
Abstract
Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as Michael acceptors. In turn, these can form Michael adducts with glutathione (GSH), resulting in the formation of a stable thioether conjugate, an irreversible process referred to as nonreducible glutathionylation. This is predicted to be prevalent in nature, particularly in more slowly turning over proteins. Such nonreducible glutathionylation can be distinguished from the more facile cycling signaling processes and is predicted to be of gerontological, toxicological, pharmacological, and oncological relevance. Here, we compare reversible and irreversible glutathionylation.
Recommended Citation
Townsend, D. M., Lushchak, V. I., & Cooper, A. J. (2014). A comparison of reversible versus irreversible protein glutathionylation. Advances in Cancer Research, 122, 177-198. doi:10.1016/B978-0-12-420117-0.00005-0
Publisher's Statement
Originally published in Advances in Cancer Research. https://doi.org/10.1016/B978-0-12-420117-0.00005-0
