Peroxiredoxins as multifunctional enzymes

Шарапов, М. Г.; Равин, В. К.; Новоселов, В. И.

doi:10.1134/s0026893314040128

Cited by 31 publications

(19 citation statements)

References 208 publications

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“…Peroxiredoxins are proteins that act as antioxidant enzymes and are widely distributed in living organisms. Six members of this family were found in mammals and were classi ed into 3 subgroups based on the number of conserved cysteine (Cys) residues in the PRDX6 monomer: typical 2-Cys (PRDX1-PRDX4), atypical 2-Cys (PRDX5), and 1-Cys (PRDX6) [36]. PRDX6 is similar to other PRDXs in being capable of reducing various peroxides.…”

Section: Resultsmentioning

confidence: 99%

“…It was also reported that PRDX6 is abundant in β-cells [38] and that muscle oxidative stress accelerates the shortening of telomeres, ultimately leading to cellular senescence [39]. PRDX6 can neutralize peroxides, peroxynitrites, and phospholipid hydroperoxides [36]. In addition, PRDX6 has a role in the repair of peroxidized cell membranes due to its ability to reduce peroxidized cell membrane phospholipids [37].…”

Section: Discussionmentioning

confidence: 99%

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PRDX6 Promotes the Differentiation of Human Mesenchymal Stem (Stromal) Cells to Insulin-Producing Cells

Gabr

Zakaria

Refaie

et al. 2020

BioMed Research International

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Mesenchymal stem cells (MSCs) can be differentiated in vitro to form insulin-producing cells (IPCs). However, the proportion of induced cells is modest. Extracts from injured pancreata of rodents promoted this differentiation, and three upregulated proteins were identified in these extracts. The aim of this study was to evaluate the potential benefits of adding these proteins to the differentiation medium alone or in combination. Our results indicate that the proportion of IPCs among the protein(s)-supplemented samples was significantly higher than that in the samples with no added proteins. The yield from samples supplemented with PRDX6 alone was 4-fold higher than that from samples without added protein. These findings were also supported by the results of fluorophotometry. Gene expression profiles revealed higher levels among protein-supplemented samples. Significantly higher levels of GGT, SST, Glut-2, and MafB expression were noted among PRDX6-treated samples. There was a stepwise increase in the release of insulin and c-peptide, as a function of increasing glucose concentrations, indicating that the differentiated cells were glucose sensitive and insulin responsive. PRDX6 exerts its beneficial effects as a result of its biological antioxidant properties. Considering its ease of use as a single protein, PRDX6 is now routinely used in our differentiation protocols.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

PRDX6 Promotes the Differentiation of Human Mesenchymal Stem (Stromal) Cells to Insulin-Producing Cells

Gabr

Zakaria

Refaie

et al. 2020

BioMed Research International

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“…Such segment-specific expression of Prx16—may be associated with the production of different types of hydroperoxides in various segments of the nephron in I/R. Peroxiredoxins are known to differ in the efficiency of neutralization of various types of hydroperoxides, and some Prxs are able to neutralize only a certain type of peroxide [ 57 ]. For instance, among mammalian peroxiredoxins, Prx2, Prx5 and Prx6 can reduce peroxynitrite, while phospholipids hydroperoxides can be reduced only by Prx6.…”

Section: Discussionmentioning

confidence: 99%

Comparative Study of Protective Action of Exogenous 2-Cys Peroxiredoxins (Prx1 and Prx2) Under Renal Ischemia-Reperfusion Injury

et al. 2020

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The pathogenesis of ischemia-reperfusion (I/R) injuries is based on oxidative stress caused by a sharp increase in the concentration of free radicals, reactive oxygen species (ROS) and secondary products of free radical oxidation of biological macromolecules during reperfusion. Application of exogenous antioxidants lowers the level of ROS in the affected tissues, suppresses or adjusts the course of oxidative stress, thereby substantially reducing the severity of I/R injury. We believe that the use of antioxidant enzymes may be the most promising line of effort since they possess higher efficiency than low molecular weight antioxidants. Among antioxidant enzymes, of great interest are peroxiredoxins (Prx1–6) which reduce a wide range of organic and inorganic peroxide substrates. In an animal model of bilateral I/R injury of kidneys (using histological, biochemical, and molecular biological methods) it was shown that intravenous administration of recombinant typical 2-Cys peroxiredoxins (Prx1 and Prx2) effectively reduces the severity of I/R damage, contributing to the normalization of the structural and functional state of the kidneys and an almost 2-fold increase in the survival of experimental animals. The use of recombinant Prx1 or Prx2 can be an efficient approach for the prevention and treatment of renal I/R injury.

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Section: Introductionmentioning

confidence: 99%

“…Prdx6′s peroxidase activity is mainly derived from a catalytically active C P –Cys 47 residue, located at the N-terminal part of the helix α2 of βαβ motif within thioredoxin fold 6 . The redox status of this peroxidatic cysteine regulates switching on/off of Prdx6′s peroxidase activity such that the enzyme with reduced Cys is active, oxidised Cys is reversibly inactive and hyperoxidised Cys is irreversibly inactive 6 . Redox cycling of Prdx6 to propel its peroxidase catalysis is believed to comprise of three steps—(i) self-oxidation and concurrent reduction of the peroxide substrate, (ii) glutathionylation of oxidised Prdx6 after hetero-dimerizing with pi-form of glutathione-S-transferase (πGST), and (iii) regeneration of catalytically active reduced Prdx6 and release of oxidised glutathione 7 .…”

Section: Introductionmentioning

confidence: 99%

Structural basis of peroxidase catalytic cycle of human Prdx6

Chowhan

Rahaman

Singh

2020

Sci Rep

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Peroxiredoxin 6 (Prdx6) is a ubiquitously expressed antioxidant non-selenium glutathione peroxidase that is known to play a major role in various physiological and pathological processes. It belongs to the family of peroxidases (referred to as Peroxiredoxins, Prdx’s) that work independently of any prosthetic groups or co-factors, and instead utilize a peroxidatic thiol residue for peroxide reduction. Mammalian Prdx’s are classified according to the number of Cys implicated in their catalytic activity by the formation of either inter-molecular (typical 2-Cys, Prdx1–4) or intra-molecular (atypical 2-Cys, Prdx5) disulfide bond, or non-covalent interactions (1-Cys, Prdx6). The typical and atypical 2-Prdx’s have been identified to show decamer/dimer and monomer/dimer transition, respectively, upon oxidation of their peroxidatic cysteine. However, the alterations in the oligomeric status of Prdx6 as a function of peroxidatic thiol’s redox state are still ambiguous. While the crystal structure of recombinant human Prdx6 is resolved as a dimer, the solution structures are reported to have both monomers and dimers. In the present study, we have employed several spectroscopic and electrophoretic probes to discern the impact of change in the redox status of peroxidatic cysteine on conformation and oligomeric status of Prdx6. Our study indicates Prdx6′s peroxidase activity to be a redox-based conformation driven process which essentially involves monomer–dimer transition.

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Peroxiredoxins as multifunctional enzymes

Cited by 31 publications

References 208 publications

PRDX6 Promotes the Differentiation of Human Mesenchymal Stem (Stromal) Cells to Insulin-Producing Cells

PRDX6 Promotes the Differentiation of Human Mesenchymal Stem (Stromal) Cells to Insulin-Producing Cells

Comparative Study of Protective Action of Exogenous 2-Cys Peroxiredoxins (Prx1 and Prx2) Under Renal Ischemia-Reperfusion Injury

Structural basis of peroxidase catalytic cycle of human Prdx6

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