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Updated: Jan 16, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
An In Vitro Study of Protein S-Glutathionylation by Members of the CLIC Protein Family
Wendy El Khoury1, Khondker Rufaka Hossain1, Amani Alghalayini1
1School of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.
Abstract:
Increasing evidence points to members of the chloride intracellular ion channel (CLIC) protein family performing a variety of functions within cells-classifying them as moonlighting proteins-and serving as natural cellular antioxidant protective agents. Apart from their role as membrane-inserting ion channels, members of the CLIC family also possess enzymatic oxidoreduction activity in their soluble form. The current study is the first to specifically examine the S-glutathionylation catalytic activity of several purified recombinant CLIC protein members (rCLIC1, rCLIC3, and rCLIC4) by directly measuring their ability to deglutathionylate and glutathionylate a synthetic model peptide via an in vitro tryptophan fluorescence quenching assay. Effects of pH and temperature on this activity were also assessed. Our findings provide insights into a likely previously uncharacterised mechanism by which CLIC proteins serve as cellular antioxidant protective enzymes via their S-glutathionylation capabilities.
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