A comparison of reversible versus irreversible protein glutathionylation.

A comparison of reversible versus irreversible protein glutathionylation.
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DOI:
10.1016/b978-0-12-420117-0.00005-0
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发表时间:
2014
影响因子:
--
通讯作者:
Cooper AJ
Cooper AJ
中科院分区:
医学2区
文献类型:
--
作者:
Townsend DM;Lushchak VI;Cooper AJ

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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.