Structure, gene expression, and evolution of primate glutathione peroxidases

Fukuhara, Ryoji; Kageyama, Takashi

doi:10.1016/j.cbpc.2005.05.002

Cited by 20 publications

(21 citation statements)

References 28 publications

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“…Among lung peroxidases, Prdx6 has the unique ability to reduce PL-OOH, as other PL-OOH reductase enzymes have limited or no activity in this tissue [39] [40] [41]. It was therefore expected that this antioxidant would be basally activated in Cftr −/− cells.…”

Section: Discussionmentioning

confidence: 99%

Peroxiredoxin 6 Fails to Limit Phospholipid Peroxidation in Lung from Cftr-Knockout Mice Subjected to Oxidative Challenge

et al. 2009

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Oxidative stress plays a prominent role in the pathophysiology of cystic fibrosis (CF). Despite the presence of oxidative stress markers and a decreased antioxidant capacity in CF airway lining fluid, few studies have focused on the oxidant/antioxidant balance in CF cells. The aim of the current study was to investigate the cellular levels of reactive oxygen species (ROS), oxidative damage and enzymatic antioxidant defenses in the lung of Cftr-knockout mice in basal conditions and as a response to oxidative insult.The results show that endogenous ROS and lipid peroxidation levels are higher in Cftr −/− lung when compared to wild-type (Cftr +/+) in basal conditions, despite a strong enzymatic antioxidant response involving superoxide dismutases, glutathione peroxidases and peroxiredoxin 6 (Prdx6). The latter has the unique capacity to directly reduce membrane phospholipid hydroperoxides (PL-OOH). A dramatic increase in PL-OOH levels in Cftr −/− lung consecutive to in vivo oxidative challenge by paraquat (PQ) unmasks a susceptibility to phospholipid peroxidation. PQ strongly decreases Prdx6 expression in Cftr −/− mice compared to Cftr +/+. Similar results were obtained after P. aeruginosa LPS challenge. Two-dimensional gel analysis of Prdx6 revealed one main molecular form in basal conditions and a PQ-induced form only detected in Cftr +/+ lung. Mass spectrometry experiments suggested that, as opposed to the main basal form, the one induced by PQ is devoid of overoxidized catalytic Cys47 and could correspond to a fully active form that is not induced in Cftr −/− lung. These results highlight a constitutive redox imbalance and a vulnerability to oxidative insult in Cftr −/− lung and present Prdx6 as a key component in CF antioxidant failure. This impaired PL-OOH detoxification mechanism may enhance oxidative damage and stress-related signaling, contributing to an exaggerated inflammatory response in CF lung.

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Section: Discussionmentioning

confidence: 99%

Peroxiredoxin 6 Fails to Limit Phospholipid Peroxidation in Lung from Cftr-Knockout Mice Subjected to Oxidative Challenge

et al. 2009

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“…Tissue specific expression varies with the type of GPx isozymes. GPx1 is known to distribute ubiquitously in various tissues; however, expression of other GPx isozymes is more tissue specific than GPx1 [14,30]. Liu et al [23] showed wide distribution of GPx mRNA in gill, muscle, hepatopancreas, digestive tract, and hemocytes of white shrimp (L. vannamei), and its role as an antioxidant.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional up-regulation of disk abalone selenium dependent glutathione peroxidase by H2O2 oxidative stress and Vibrio alginolyticus bacterial infection

Zoysa¹,

Pushpamali²,

Oh³

et al. 2008

Fish & Shellfish Immunology

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“…The only protein besides Prdx6 for which significant PHGPx activity has been demonstrated is GSH peroxidase 4 (GPx4) [56,57] and none of the 2-cys Prdx enzymes have been shown to express this activity. (In this review, I have used PHGPx to describe the activity potentially shared by other enzymes and GPx4 as the name of a specific protein.)…”

Section: Enzymatic Activites Of Prdx6mentioning

confidence: 99%

Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling

Fisher

2017

Archives of Biochemistry and Biophysics

142

127

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Peroxiredoxin 6 represents a widely distributed group of peroxiredoxins that contain a single conserved cysteine in the protein monomer (1-cys Prdx). The cys when oxidized to the sulfenic form is reduced with glutathione (GSH) catalyzed by the π isoform of GSH-S-transferase. Three enzymatic activities of the protein have been described:1) peroxidase with H2O2, short chain hydroperoxides, and phospholipid hydroperoxides as substrates; 2) phospholipase A2 (PLA2); and 3) lysophosphatidylcholine acyl transferase (LPCAT). These activities have important physiological roles in antioxidant defense, turnover of cellular phospholipids, and the generation of superoxide anion via initiation of the signaling cascade for activation of NADPH oxidase (type 2). The ability of Prdx6 to reduce peroxidized cell membrane phospholipids (peroxidase activity) and also to replace the oxidized sn-2 fatty acyl group through hydrolysis/reacylation (PLA2 and LPCAT activities) provides a complete system for the repair of peroxidized cell membranes.

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Structure, gene expression, and evolution of primate glutathione peroxidases

Cited by 20 publications

References 28 publications

Peroxiredoxin 6 Fails to Limit Phospholipid Peroxidation in Lung from Cftr-Knockout Mice Subjected to Oxidative Challenge

Peroxiredoxin 6 Fails to Limit Phospholipid Peroxidation in Lung from Cftr-Knockout Mice Subjected to Oxidative Challenge

Transcriptional up-regulation of disk abalone selenium dependent glutathione peroxidase by H2O2 oxidative stress and Vibrio alginolyticus bacterial infection

Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling

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