A Comparison of Reversible versus Irreversible Protein Glutathionylation

Authors

Danyelle M. Townsend, Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA.
Volodymyr I. Lushchak, Department of Biochemistry and Biotechnology, Vassyl Stefanyk Precarpathian National University, Ivano-Frankivsk, Ukraine.
Arthur J. Cooper, Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York, USA. Electronic address: arthur_cooper@nymc.edu.

Author Type(s)

Faculty

DOI

10.1016/B978-0-12-420117-0.00005-0

Journal Title

Advances in Cancer Research

First Page

177

Last Page

98

Document Type

Article

Publication Date

1-1-2014

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, 177-98. https://doi.org/10.1016/B978-0-12-420117-0.00005-0