An In Vitro Study of Protein S-Glutathionylation by Members of the CLIC Protein Family.

Wendy El Khoury, Khondker Rufaka Hossain, Amani Alghalayini, Hala M Ali, Stella M Valenzuela

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Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

5 authors.

Wendy El KhourySchool of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.

Khondker Rufaka HossainSchool of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.ORCID 0000-0003-4506-1491

Amani AlghalayiniSchool of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.ORCID 0000-0002-2308-0256

Hala M AliSchool of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.

Stella M ValenzuelaSchool of Life Sciences, University of Technology Sydney, Sydney, NSW 2007, Australia.ORCID 0000-0001-5934-6047

Funding

Bod Science Pty Ltd ACN 601225441 PRO19-9510

6 · The paper itself

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.

Indexed as

Chloride ChannelsGlutathioneHumansHydrogen-Ion ConcentrationRecombinant ProteinsChloride ChannelsGlutathioneRecombinant ProteinsCLIC proteinsdeglutathionylationglutathioneS-glutathionylationtryptophan quenching assay

Identifiers

PMID41008519

DOI10.3390/biom15091213

PMCPMC12467487

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LicenceCC BY

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