Oxidation of cathepsin S by major chemicals of cigarette smoke

Wartenberg, Mylène; Andrault, Pierre-Marie; Saidi, Ahlame; Bigot, Paul; Nadal-Desbarats, Lydie; Lecaille, Fabien; Lalmanach, Gilles

doi:10.1016/j.freeradbiomed.2020.02.013

Cited by 16 publications

(19 citation statements)

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“…Both reactive aldehydes and carbonyl-containing proteins inhibit papain and cathepsins B and L by glycation of Cys25 of the active site [163]. Nevertheless, spectral analysis by circular dichroism supported that oxidation by CSE does not alter the overall structure of CatS, despite an increase of carbonylation [77]. Acrolein (Figure 4b), which is known to react with thiolate by forming a highly-stable Michael addition adduct, and in a lesser extent formaldehyde (Figure 4c), inactivated human cathepsins B, L, S and K in a concentration-dependent manner.…”

Section: Carbonylation Of Cysteine Cathepsinsmentioning

confidence: 93%

“…Also, despite a significantly higher oxidative stress index (OSI) in current smokers compared to nonsmokers, an increase of CatS activity was found in lung tissue of smokers [76]. Addition of N-acetyl cysteine or GSH led to a partial recovery of CatS activity following incubation with CSE, H2O, and ONOO − [77]. A decrease in the inactivation rate by oxidized glutathione (GSSG) was observed for human CatK in the presence of a peptide substrate, suggesting that the latter has a partial protective…”

Section: Redox Regulationmentioning

confidence: 93%

“…On the other hand, following the addition of H 2 O 2 , Cys25 of CatK was found either in the form of sulfonic acid (~70% of -SO 3 H), either in the form of sulfenic acid (~30% of -SOH), which suggested that CatK activity could be partially recovered [141]. Also, analysis by redox sensing probes of the inactivation of CatS by H 2 O 2 supported the formation of Cys25 sulfenic acid followed by a slower conversion to sulfinic acid [77]. This protective mechanism may explain the maintenance of cysteine cathepsin activity during emphysema [76] and inflammatory phenomena such as silicosis [43].…”

Section: Inactivation By Reactive Oxygen Speciesmentioning

confidence: 93%

“…Exposure of primary human bronchial epithelial cells to cigarette smoke extract (CSE) triggers the activation of purinergic P2X7 receptors, which in turn drive CatS upregulation [76]. Despite a marked increase of oxidants associated with cigarette smoke and a subsequent oxidant/antioxidant imbalance, overall data suggest that CatS may contribute, in conjunction with other proteases, to elastinolysis and subsequent parenchymal destruction in emphysema [77].…”

Section: Cysteine Cathepsins In Pulmonary Diseasesmentioning

confidence: 99%

“…Both GSNO and H 2 O 2 inhibit the autocatalytic maturation of procathepsin K and inactivate the activity of the mature form in a time-and dose-dependent manner [102,133]. H 2 O 2 , but not ONOO − , hinders the autocatalytic maturation of procathepsin S [77]. Additionally, ROS impair the automaturation of procathepsin L and may disrupt its pro-autophagic function, while the processing of CatB zymogen is not blocked by ROS [143].…”

Section: Inactivation By Reactive Oxygen Speciesmentioning

confidence: 99%

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Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants

Lalmanach

Saidi

Bigot

et al. 2020

IJMS

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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).

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Section: Carbonylation Of Cysteine Cathepsinsmentioning

confidence: 93%

Section: Redox Regulationmentioning

confidence: 93%