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Published, Version of Record (VoR)Open Access via Drexel Libraries Read and Publish Program 2025CC BY V4.0, Open
Journal article
Dehydroglutathione, a glutathione derivative to introduce non-reversible glutathionylation
RSC chemical biology, v 6, pp 1156-1164
May 2025
Featured in Collection : Research Supported by Drexel Libraries' OA Programs
Abstract
Protein cysteine is susceptible to diverse oxidations, including disulfide, S-sulfenylation, S-nitrosylation, and S-glutathionylation, that regulate many biological processes in physiology and diseases. Despite evidence supporting distinct biological outcomes of individual cysteine oxoforms, the approach for examining functional effects resulting from a specific cysteine oxoform, such as S-glutathionylation, remains limited. In this report, we devised a dehydroglutathione (dhG)-mediated strategy, named G-PROV, that introduces a non-reducible glutathionylation mimic to protein with the subsequent delivery of the modified protein to cells to examine “phenotype” attributed to “glutathionylation”. We applied our strategy to fatty acid binding protein 5 (FABP5), demonstrating that dhG induces selective modification at C127 of FABP5, resembling S-glutathionylation. dhG-modified glutathionylation in FABP5 increases its binding affinity to linoleic acid, enhances its translocation to the nucleus for activating PPARβ/δ, and promotes MCF7 cell migration in response to linoleic acid. Our data report a facile chemical tool to introduce a glutathionylation mimic to protein for functional analysis of protein glutathionylation.
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Details
- Title
- Dehydroglutathione, a glutathione derivative to introduce non-reversible glutathionylation
- Creators
- Daniel Oppong - Drexel UniversityRayavarapu Padmavathi - Drexel UniversityDhanushika S. K. Kukulage - Drexel UniversityMadhu Chakkere Shivamadhu - Drexel UniversityElizabeth Aline Newberry - Drexel UniversityAnneliese M. Faustino - The Wistar InstituteHsin-Yao Tang - The Wistar InstituteYoung-Hoon Ahn (Corresponding Author) - Drexel University
- Publication Details
- RSC chemical biology, v 6, pp 1156-1164
- Publisher
- Royal Society of Chemistry
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Scopus ID
- 2-s2.0-105007813750
- Other Identifier
- 991022054115204721