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Submitted on July 13, 2005
Revised on October 7, 2005
Accepted on October 12, 2005

N, N-biotinyl glutathione disulfide: Studies demonstrating its utility in the study of protein S-glutathiolation

Jonathan P. Brennan, Jonathan I. A. Miller, William Fuller, Robin Wait, Shajna Begum, Michael J. Dunn, and Philip Eaton

Department of Cardiology, King's College London, The Rayne Institute, London SE1 7EH

Corresponding Author: philip.eaton{at}kcl.ac.uk

Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs during neurohormonal or metabolic stimulation, as well as in many disease states. Elevated GSSG promotes protein S-glutathiolation, a reversible post-translational modification, which can directly alter or regulate protein function. We have developed novel strategies for the study of protein S-glutathiolation, which involves the simple synthesis of N, N-biotinyl glutathione disulfide (biotin-GSSG). Biotin-GSSG treatment of cells mimics a defined component of oxidative stress, namely a shift in the glutathione redox couple to the oxidized disulfide state. This induces widespread protein S-glutathiolation, which was detected on non-reducing Western blots probed with streptavidin-HRP and imaged using confocal fluorescence microscopy and ExtrAvidin-FITC. S-glutathiolated proteins were purified using streptavidin-agarose and identified using proteomic methods. We conclude biotin-GSSG is a useful tool in the investigation of protein S-glutathiolation and offers significant advantages over conventional methods or antibody-based strategies. These novel approaches may find widespread utility in the study of disease or redox signaling models where GSSG accumulation occurs.


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