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Review

Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants

1
Université de Tours, 37000 Tours, France
2
INSERM, UMR1100, Centre d’Etude des Pathologies Respiratoires, 37000 Tours, France
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(6), 1944; https://doi.org/10.3390/ijms21061944
Received: 20 February 2020 / Revised: 10 March 2020 / Accepted: 10 March 2020 / Published: 12 March 2020
(This article belongs to the Special Issue Biocatalysis: Mechanisms of Proteolytic Enzymes)
Besides their primary involvement in the recycling and degradation of proteins in endo-lysosomal compartments and also in specialized biological functions, cysteine cathepsins are pivotal proteolytic contributors of various deleterious diseases. While the molecular mechanisms of regulation via their natural inhibitors have been exhaustively studied, less is currently known about how their enzymatic activity is modulated during the redox imbalance associated with oxidative stress and their exposure resistance to oxidants. More specifically, there is only patchy information on the regulation of lung cysteine cathepsins, while the respiratory system is directly exposed to countless exogenous oxidants contained in dust, tobacco, combustion fumes, and industrial or domestic particles. Papain-like enzymes (clan CA, family C1, subfamily C1A) encompass a conserved catalytic thiolate-imidazolium pair (Cys25-His159) in their active site. Although the sulfhydryl group (with a low acidic pKa) is a potent nucleophile highly susceptible to chemical modifications, some cysteine cathepsins reveal an unanticipated resistance to oxidative stress. Besides an introductory chapter and peculiar attention to lung cysteine cathepsins, the purpose of this review is to afford a concise update of the current knowledge on molecular mechanisms associated with the regulation of cysteine cathepsins by redox balance and by oxidants (e.g., Michael acceptors, reactive oxygen, and nitrogen species). View Full-Text
Keywords: cathepsin; chronic obstructive pulmonary disease (COPD); cysteine; cysteine protease; lung inflammation; oxidation; proteolysis; thiol cathepsin; chronic obstructive pulmonary disease (COPD); cysteine; cysteine protease; lung inflammation; oxidation; proteolysis; thiol
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MDPI and ACS Style

Lalmanach, G.; Saidi, A.; Bigot, P.; Chazeirat, T.; Lecaille, F.; Wartenberg, M. Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants. Int. J. Mol. Sci. 2020, 21, 1944. https://doi.org/10.3390/ijms21061944

AMA Style

Lalmanach G, Saidi A, Bigot P, Chazeirat T, Lecaille F, Wartenberg M. Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants. International Journal of Molecular Sciences. 2020; 21(6):1944. https://doi.org/10.3390/ijms21061944

Chicago/Turabian Style

Lalmanach, Gilles, Ahlame Saidi, Paul Bigot, Thibault Chazeirat, Fabien Lecaille, and Mylène Wartenberg. 2020. "Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants" International Journal of Molecular Sciences 21, no. 6: 1944. https://doi.org/10.3390/ijms21061944

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