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Antioxidants
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Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family
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Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Antioxidant Enzyme Systems".

Deadline for manuscript submissions: closed (31 October 2018) | Viewed by 48021

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Prof. Dr. Aron B. Fisher

E-Mail Website
Guest Editor
Department of Physiology and the Institute for Environmental Medicine, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA
Interests: oxidant stress; anti-oxidants; reactive oxygen species; lipid peroxidation; GSH peroxidase; phospholipase A2; cell signalling; endothelial shear stress; mechanotransduction; lung surfactant; acute lung injury

Special Issue Information

Dear Colleagues,

Peroxiredoxin 6 is truly a unique member of the peroxiredoxin family. While it is similar to other peroxiredoxins in its peroxidase activity towards small peroxides, such as H2O2, it exhibits several important characteristics that distinguish it from other peroxiredoxins. These characteristics of Peroxiredoxin 6 include: a catalytic mechanism for peroxidase activity that depends on a single conserved Cys in contrast to the 2-Cys mechanisms for most other peroxiredoxins; the use of GSH as the primary physiological reductant for peroxidase activity in contrast to the thioredoxin that is the primary reductant for other peroxiredoxins; the ability to bind phospholipids; the activity to reduce phospholipid hydroperoxides to the corresponding alcohol, i.e., phospholipid hydroperoxide glutathione peroxidase activity; the activity to hydrolyze the sn-2 fatty acyl bond of phospholipids, i.e.,phospholipase A2 activity (PLA2); and activity to transfer a fatty acyl CoA into the sn-2 position of lysophosphatidylcholine, i.e., lysoPC acyl transferase activity. The binding of phospholipids and the associated lipid-related enzymatic activities of Peroxiredoxin 6 are not expressed by other members of the peroxiredoxin family. Thus, Prdx6 is a unique multifunctional protein.

Peroxiredoxin 6 has been demonstrated to play specific and important roles in normal physiology. Well-documented roles include: Anti-oxidant defense and the repair of peroxidized cell membranes, the turnover of lung surfactant phospholipids,and cellular signaling such as in mechanotransduction and the activation of NADPH oxidase. Although less well documented, Peroxiredoxin 6 has been postulated to be important in the pathophysiology of acute lung injury and inflammation, cancer and carcinogenesis, various chronic diseases of the CNS, cataracts and retinal disease, type 2 diabetes, and male infertility, among others. Thus, there is important depth and breadth to the study of Prdx6.

While Peroxiredoxin 6 has been included in published forums dealing with peroxiredoxins in general, there has not been, to date, a forum dealing specifically with this protein. I believe that the time is ripe. This Special Issue welcomes submission of reviews or original research addressing any aspect of Peroxiredoxin 6 structure/function relationships and the physiological/pathophysiological roles of its unique enzymatic activities.

Dr. Aron B. Fisher
Guest Editor

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antioxidants is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Peroxiredoxin
  • GSH peroxidase
  • Phospholipase A2
  • Thiol reactions
  • SDH catalytic triad
  • Cellular signaling
  • Oxidant stress
  • Phospholipid turnover
  • Inflammation
  • Carcinogenesis

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Published Papers (11 papers)

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Editorial

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5 pages, 162 KiB  
Editorial
Antioxidants Special Issue: Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family
by Aron B. Fisher
Antioxidants 2019, 8(4), 107; https://doi.org/10.3390/antiox8040107 - 19 Apr 2019
Cited by 10 | Viewed by 2712
Abstract
The peroxiredoxins, first discovered about 30 years ago, are the most recently described family of ubiquitously expressed antioxidant enzymes [...] Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)

Research

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17 pages, 1964 KiB  
Article
Non-Mammalian Prdx6 Enzymes (Proteins with 1-Cys Prdx Mechanism) Display PLA2 Activity Similar to the Human Orthologue
by Renata Bannitz-Fernandes, Rogério Aleixo-Silva, João Paulo Silva, Chandra Dodia, Jose Pablo Vazquez-Medina, Jian-Qin Tao, Aron Fisher and Luis Netto
Antioxidants 2019, 8(3), 52; https://doi.org/10.3390/antiox8030052 - 01 Mar 2019
Cited by 11 | Viewed by 3884
Abstract
Mammalian peroxiredoxin class 6 (Prdx6) are bifunctional enzymes. Non-mammalian Prdx6 enzymes display Cys-based peroxidase activity, but to date their putative phospholipase A2 (PLA2 activities) has not been experimentally investigated. Initially, we observed that five non-mammalian Prdx6 enzymes (enzymes from Arabidopsis thaliana [...] Read more.
Mammalian peroxiredoxin class 6 (Prdx6) are bifunctional enzymes. Non-mammalian Prdx6 enzymes display Cys-based peroxidase activity, but to date their putative phospholipase A2 (PLA2 activities) has not been experimentally investigated. Initially, we observed that five non-mammalian Prdx6 enzymes (enzymes from Arabidopsis thaliana (AtPER1), Triticum aestivum (TaPER1), Pseudomonas aeruginosa (PaLsfA) and Aspergillus fumigatus (AfPrx1 and AfPrxC)) present features compatible with PLA2 activities in mammalian Prdx6 by amino acid sequences alignment and tertiary structure modeling. Employing unilamellar liposomes with tracer amounts of [3H]-1,2-Dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and thin layer chromatography, all the tested non-mammalian Prdx6 enzymes displayed PLA2 activities, with values ranging from 3.4 to 6.1 nmol/min/mg protein. It was previously shown that Thr177 phosphorylation of human Prdx6 increases its PLA2 activity, especially at neutral pH. Therefore, we investigated if human Erk2 kinase could also phosphorylate homologous Thr residues in non-mammalian Prdx6 proteins. We observed phosphorylation of the conserved Thr in three out of the five non-mammalian Prdx enzymes by mass spectrometry. In the case of the mitochondrial Prdx6 from A. fumigatus (AfPrxC), we also observed phosphorylation by western blot, and as a consequence, the PLA2 activity was increased in acidic and neutral conditions by the human Erk2 kinase treatment. The possible physiological meanings of these PLA2 activities described open new fields for future research. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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14 pages, 2511 KiB  
Article
Hyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State
by Sharifun Shahnaj, Rimpy Kaur Chowhan, Potshangbam Angamba Meetei, Pushpa Kakchingtabam, Khundrakpam Herojit Singh, Laishram Rajendrakumar Singh, Potshangbam Nongdam, Aron B. Fisher and Hamidur Rahaman
Antioxidants 2019, 8(2), 33; https://doi.org/10.3390/antiox8020033 - 02 Feb 2019
Cited by 11 | Viewed by 4626
Abstract
Peroxiredoxins(Prdx), the family of non-selenium glutathione peroxidases, are important antioxidant enzymes that defend our system from the toxic reactive oxygen species (ROS). They are thiol-based peroxidases that utilize self-oxidation of their peroxidatic cysteine (Cp) group to reduce peroxides and peroxidized biomolecules. [...] Read more.
Peroxiredoxins(Prdx), the family of non-selenium glutathione peroxidases, are important antioxidant enzymes that defend our system from the toxic reactive oxygen species (ROS). They are thiol-based peroxidases that utilize self-oxidation of their peroxidatic cysteine (Cp) group to reduce peroxides and peroxidized biomolecules. However, because of its high affinity for hydrogen peroxide this peroxidatic cysteine moiety is extremely susceptible to hyperoxidation, forming peroxidase inactive sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) derivatives. With the exception of peroxiredoxin 6 (Prdx6), hyperoxidized sulfinic forms of Prdx can be reversed to restore peroxidase activity by the ATP-dependent enzyme sulfiredoxin. Interestingly, hyperoxidized Prdx6 protein seems to have physiological significance as hyperoxidation has been reported to dramatically upregulate its calcium independent phospholipase A2 activity. Using biochemical studies and molecular dynamic (MD) simulation, we investigated the roles of thermodynamic, structural and internal flexibility of Prdx6 to comprehend the structural alteration of the protein in the oxidized state. We observed the loosening of the hydrophobic core of the enzyme in its secondary and tertiary structures. These changes do not affect the internal dynamics of the protein (as indicated by root-mean-square deviation, RMSD and root mean square fluctuation, RMSF plots). Native-PAGE and dynamic light scattering experiments revealed the formation of higher oligomers of Prdx6 under hyperoxidation. Our study demonstrates that post translational modification (like hyperoxidation) in Prdx6 can result in major alterations of its multimeric status. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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14 pages, 1135 KiB  
Article
Oxidation of Peroxiredoxin 6 in the Presence of GSH Increases its Phospholipase A2 Activity at Cytoplasmic pH
by Suiping Zhou, Chandra Dodia, Sheldon I. Feinstein, Sandra Harper, Henry J. Forman, David W. Speicher and Aron B. Fisher
Antioxidants 2019, 8(1), 4; https://doi.org/10.3390/antiox8010004 - 24 Dec 2018
Cited by 10 | Viewed by 4222
Abstract
The expression of the phospholipase A2 activity (aiPLA2) of peroxiredoxin 6 (Prdx6) in the cell cytoplasm is physiologically relevant for the repair of peroxidized cell membranes, but aiPLA2 assay in vitro indicates that, unlike assay at pH 4, activity [...] Read more.
The expression of the phospholipase A2 activity (aiPLA2) of peroxiredoxin 6 (Prdx6) in the cell cytoplasm is physiologically relevant for the repair of peroxidized cell membranes, but aiPLA2 assay in vitro indicates that, unlike assay at pH 4, activity at cytosolic pH is essentially absent with non-oxidized substrate. However, the addition of glutathione (GSH) to the assay medium significantly increased aiPLA2 activity at cytosolic pH, while oxidized GSH (GSSG) and several other thiols had no effect. By mass spectroscopy (ESI MS), the addition of GSH to Prdx6 paradoxically led to oxidation of its conserved Cys47 residue to a sulfinic acid. The effect of GSH on PLA2 activity was abolished by incubation under anaerobic conditions, confirming that auto-oxidation of the protein was the mechanism for the GSH effect. Analysis by circular dichroism (CD) and tryptophan fluorescence showed alterations of the protein structure in the presence of GSH. Independently of GSH, the oxidation of Prdx6 by exposure to H2O2 or the presence of oxidized phospholipid as substrate also significantly increased aiPLA2 activity at pH 7. We conclude that the oxidation of the peroxidatically active Cys47 of Prdx6 results in an increase of aiPLA2 activity at pH 7 without effect on the activity of the enzyme at pH 4. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Graphical abstract

13 pages, 1189 KiB  
Article
Identification of Small Peptides that Inhibit NADPH Oxidase (Nox2) Activation
by Aron B. Fisher, Chandra Dodia and Sheldon I. Feinstein
Antioxidants 2018, 7(12), 181; https://doi.org/10.3390/antiox7120181 - 05 Dec 2018
Cited by 10 | Viewed by 3289
Abstract
Nicotinamide adenine phosphate (NADPH) oxidase type 2 (Nox2), a major source of reactive oxygen species in lungs, plays an important role in tissue damage associated with acute inflammatory diseases. The phospholipase A2 (PLA2) activity of peroxiredoxin 6 (Prdx6), called aiPLA [...] Read more.
Nicotinamide adenine phosphate (NADPH) oxidase type 2 (Nox2), a major source of reactive oxygen species in lungs, plays an important role in tissue damage associated with acute inflammatory diseases. The phospholipase A2 (PLA2) activity of peroxiredoxin 6 (Prdx6), called aiPLA2, is required for Nox2 activation through its role in the cellular generation of Rac, a key cytosolic component of the activation cascade. Lung surfactant protein A (SP-A) binds to Prdx6, inhibits its aiPLA2 activity, and prevents activation of Nox2. Based on protein docking software, we previously identified a 16 amino acid (aa) peptide derived from rat SP-A as the Prdx6 binding motif. We now identify the minimal effective sequences of rat/mouse and human SP-A as 9-aa sequences that we have called PLA2-inhibitory peptide (PIP).These sequences are PIP-1, rat/mouse; PIP-2, human; and PIP-3, a hybrid of PIPs 1&2. aiPLA2 activity in vitro was inhibited by 50% with ~7–10 µg PIP/µg Prdx6. Inhibition of the aiPLA2 activity and Nox2 activation of lungs in vivo was similar for intratracheal (IT) and intravenous (IV) administration of PIP-2, but required its incorporation into liposomes as a delivery vehicle; tissue ½ time for decrease of the in vivo inhibition of aiPLA2 activity after PIP-2 administration was ~50 h. These properties suggest that PIP-2 could be an effective therapeutic agent to prevent tissue injury associated with lung inflammation. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Graphical abstract

12 pages, 1701 KiB  
Article
Regulation of Oxidative Stress in Corneal Endothelial Cells by Prdx6
by Matthew Lovatt, Khadijah Adnan, Gary S. L. Peh and Jodhbir S. Mehta
Antioxidants 2018, 7(12), 180; https://doi.org/10.3390/antiox7120180 - 04 Dec 2018
Cited by 13 | Viewed by 4093
Abstract
The inner layer of the cornea, the corneal endothelium, is post-mitotic and unable to regenerate if damaged. The corneal endothelium is one of the most transplanted tissues in the body. Fuchs’ endothelial corneal dystrophy (FECD) is the leading indication for corneal endothelial transplantation. [...] Read more.
The inner layer of the cornea, the corneal endothelium, is post-mitotic and unable to regenerate if damaged. The corneal endothelium is one of the most transplanted tissues in the body. Fuchs’ endothelial corneal dystrophy (FECD) is the leading indication for corneal endothelial transplantation. FECD is thought to be an age-dependent disorder, with a major component related to oxidative stress. Prdx6 is an antioxidant with particular affinity for repairing peroxidised cell membranes. To address the role of Prdx6 in corneal endothelial cells, we used a combination of biochemical and functional studies. Our data reveal that Prdx6 is expressed at unusually high levels at the plasma membrane of corneal endothelial cells. RNAi-mediated knockdown of Prdx6 revealed a role for Prdx6 in lipid peroxidation. Furthermore, following induction of oxidative stress with menadione, Prdx6-deficient cells had defective mitochondrial membrane potential and were more sensitive to cell death. These data reveal that Prdx6 is compartmentalised in corneal endothelial cells and has multiple functions to preserve cellular integrity. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Review

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10 pages, 207 KiB  
Review
Mouse Models of Genetically Altered Peroxiredoxin 6
by Sheldon I. Feinstein
Antioxidants 2019, 8(4), 77; https://doi.org/10.3390/antiox8040077 - 27 Mar 2019
Cited by 12 | Viewed by 2654
Abstract
Peroxiredoxin 6 (Prdx6) has been shown to have three enzymatic activities: peroxidase, phospholipase A2 (PLA2) and acyl transferase. The peroxidase activity is unusual, as it is capable of reducing phospholipid hydroperoxides (as well as hydrogen peroxide and short chain organic [...] Read more.
Peroxiredoxin 6 (Prdx6) has been shown to have three enzymatic activities: peroxidase, phospholipase A2 (PLA2) and acyl transferase. The peroxidase activity is unusual, as it is capable of reducing phospholipid hydroperoxides (as well as hydrogen peroxide and short chain organic peroxides). Knockout and overexpressing mice have been produced that demonstrate the effect that eliminating or overproducing Prdx6 has on the animals’ physiology. In addition, mutations in various amino acids of Prdx6 have been identified that interfere with different enzymatic functions as well as protein transport. These mutations were originally characterized biochemically; subsequently, several knock-in mouse strains have been produced, each containing one mutation. These mice include the S32T knock-in that affects protein transport, the C47S knock-in that inactivates the peroxidase enzymatic activity, the D140A knock-in that inactivates the PLA2 enzymatic activity and the H26A knock-in that inactivates the peroxidase and blocks binding to phospholipids. This review summarizes the properties of these mice based upon studies conducted with the knockout, overexpressing and knock-in mice and the effect of the genetic changes on the biochemistry and physiology of these mice. The availability of these mice is also briefly discussed. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
12 pages, 1287 KiB  
Review
Peroxiredoxin6 in Endothelial Signaling
by Priyal Patel and Shampa Chatterjee
Antioxidants 2019, 8(3), 63; https://doi.org/10.3390/antiox8030063 - 13 Mar 2019
Cited by 18 | Viewed by 4202
Abstract
Peroxiredoxins (Prdx) are a ubiquitous family of highly conserved antioxidant enzymes with a cysteine residue that participate in the reduction of peroxides. This family comprises members Prdx1–6, of which Peroxiredoxin 6 (Prdx6) is unique in that it is multifunctional with the ability to [...] Read more.
Peroxiredoxins (Prdx) are a ubiquitous family of highly conserved antioxidant enzymes with a cysteine residue that participate in the reduction of peroxides. This family comprises members Prdx1–6, of which Peroxiredoxin 6 (Prdx6) is unique in that it is multifunctional with the ability to neutralize peroxides (peroxidase activity) and to produce reactive oxygen species (ROS) via its phospholipase (PLA2) activity that drives assembly of NADPH oxidase (NOX2). From the crystal structure, a C47 residue is responsible for peroxidase activity while a catalytic triad (S32, H26, and D140) has been identified as the active site for its PLA2 activity. This paradox of being an antioxidant as well as an oxidant generator implies that Prdx6 is a regulator of cellular redox equilibrium (graphical abstract). It also indicates that a fine-tuned regulation of Prdx6 expression and activity is crucial to cellular homeostasis. This is specifically important in the endothelium, where ROS production and signaling are critical players in inflammation, injury, and repair, that collectively signal the onset of vascular diseases. Here we review the role of Prdx6 as a regulator of redox signaling, specifically in the endothelium and in mediating various pathologies. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Graphical abstract

23 pages, 5637 KiB  
Review
Radioprotective Role of Peroxiredoxin 6
by Mars G. Sharapov, Vladimir I. Novoselov and Sergey V. Gudkov
Antioxidants 2019, 8(1), 15; https://doi.org/10.3390/antiox8010015 - 05 Jan 2019
Cited by 44 | Viewed by 6662
Abstract
Peroxiredoxin 6 (Prdx6) is a member of an evolutionary ancient family of peroxidase enzymes with diverse functions in the cell. Prdx6 is an important enzymatic antioxidant. It reduces a wide range of peroxide substrates in the cell, thus playing a leading role in [...] Read more.
Peroxiredoxin 6 (Prdx6) is a member of an evolutionary ancient family of peroxidase enzymes with diverse functions in the cell. Prdx6 is an important enzymatic antioxidant. It reduces a wide range of peroxide substrates in the cell, thus playing a leading role in the maintenance of the redox homeostasis in mammalian cells. Beside peroxidase activity, Prdx6 has been shown to possess an activity of phospholipase A2, an enzyme playing an important role in membrane phospholipid metabolism. Moreover, Prdx6 takes part in intercellular and intracellular signal transduction due to its peroxidase and phospholipase activity, thus facilitating the initiation of regenerative processes in the cell, suppression of apoptosis, and activation of cell proliferation. Being an effective and important antioxidant enzyme, Prdx6 plays an essential role in neutralizing oxidative stress caused by various factors, including action of ionizing radiation. Endogenous Prdx6 has been shown to possess a significant radioprotective potential in cellular and animal models. Moreover, intravenous infusion of recombinant Prdx6 to animals before irradiation at lethal or sublethal doses has shown its high radioprotective effect. Exogenous Prdx6 effectively alleviates the severeness of radiation lesions, providing normalization of the functional state of radiosensitive organs and tissues, and leads to a significant elevation of the survival rate of animals. Prdx6 can be considered as a potent and promising radioprotective agent for reducing the pathological effect of ionizing radiation on mammalian organisms. The radioprotective properties and mechanisms of radioprotective action of Prdx6 are discussed in the current review. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Graphical abstract

9 pages, 418 KiB  
Review
Peroxiredoxin 6: The Protector of Male Fertility
by Cristian O’Flaherty
Antioxidants 2018, 7(12), 173; https://doi.org/10.3390/antiox7120173 - 24 Nov 2018
Cited by 38 | Viewed by 4661
Abstract
The spermatozoon is a terminal cell with the unique purpose of delivering the paternal genome to the oocyte during fertilization. Once spermatozoa enter into the female reproductive tract, they count on only the antioxidant protection that they received during spermatogenesis and epididymal maturation. [...] Read more.
The spermatozoon is a terminal cell with the unique purpose of delivering the paternal genome to the oocyte during fertilization. Once spermatozoa enter into the female reproductive tract, they count on only the antioxidant protection that they received during spermatogenesis and epididymal maturation. Peroxiredoxins (PRDXs), particularly PRDX6, are important players in the antioxidant protection and regulation of reactive oxygen species (ROS) levels in spermatozoa. PRDX6, through its peroxidase and calcium-independent phospholipase A2 activities, plays a major role in the regulation of ROS to maintain viability and motility and allow the spermatozoon to achieve fertilizing ability during the complex process of capacitation. The absence of PRDX6 is sufficient to promote abnormal reproductive outcomes in mice that resemble what we observe in infertile men. Indeed, Prdx6−/− spermatozoa display low motility and severe DNA damage, which is translated into reduced ability to fertilize oocytes in vitro or produce a low number of pups compared to wild-type controls. This review focuses on the role of PRDX6 as the primary antioxidant enzyme that protects the spermatozoon from oxidative-stress-associated damages to protect the paternal genome and assure fertility. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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Graphical abstract

12 pages, 238 KiB  
Review
The Role of Peroxiredoxin 6 in Cell Signaling
by José A. Arevalo and José Pablo Vázquez-Medina
Antioxidants 2018, 7(12), 172; https://doi.org/10.3390/antiox7120172 - 24 Nov 2018
Cited by 66 | Viewed by 5767
Abstract
Peroxiredoxin 6 (Prdx6, 1-cys peroxiredoxin) is a unique member of the peroxiredoxin family that, in contrast to other mammalian peroxiredoxins, lacks a resolving cysteine and uses glutathione and π glutathione S-transferase to complete its catalytic cycle. Prdx6 is also the only peroxiredoxin capable [...] Read more.
Peroxiredoxin 6 (Prdx6, 1-cys peroxiredoxin) is a unique member of the peroxiredoxin family that, in contrast to other mammalian peroxiredoxins, lacks a resolving cysteine and uses glutathione and π glutathione S-transferase to complete its catalytic cycle. Prdx6 is also the only peroxiredoxin capable of reducing phospholipid hydroperoxides through its glutathione peroxidase (Gpx) activity. In addition to its peroxidase activity, Prdx6 expresses acidic calcium-independent phospholipase A2 (aiPLA2) and lysophosphatidylcholine acyl transferase (LPCAT) activities in separate catalytic sites. Prdx6 plays crucial roles in lung phospholipid metabolism, lipid peroxidation repair, and inflammatory signaling. Here, we review how the distinct activities of Prdx6 are regulated during physiological and pathological conditions, in addition to the role of Prdx6 in cellular signaling and disease. Full article
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
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