Removals of Hydrogen Peroxide and Hydroxyl Radical by Thiol-Specific Antioxidant Protein as a Possible Role in Vivo

Lim, Yongseok; Cha, Mee‐Kyung; Kim, H.K.; Uhm, Tai-Boong; Park, J.W.; Kim, K.; Kim, I.H.

doi:10.1006/bbrc.1993.1410

Cited by 176 publications

(80 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mouse insulinoma cells βTC6-F7 (passages [15][16][17][18][19][20] were propagated in DMEM medium containing 5.5 mmol/l glucose, supplemented with 10% heat-inactivated FCS, 100 U/ml penicillin and 100 µg/ml streptomycin. Rat insulinoma cells INS-1 (passages [13][14][15][16][17][18][19][20] were propagated in RPMI-1640 medium containing 11 mmol/l glucose, supplemented with 10% heat-inactivated FCS, 100 U/ml penicillin, 100 µg/ml streptomycin, 10 mmol/l HEPES-buffer, 2 mmol/l L-glutamine, 1 mmol/l sodium pyruvate, 50 µmol/l β-mercaptoethanol. All cells were cultured at 37°C in a humidified atmosphere containing 95% air and 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

“…19] and catalyse reduction of both hydrogen peroxide and alkyl peroxides to water or to the corresponding alcohol using thioredoxin (Tx) as their physiological hydrogen donor [20,21,22,23,24]. Additionally it has been shown that the bacterial peroxiredoxin AhpC (alkylhydroperoxide reductase subunit C) is able to protect against nitrogen radicals [25].…”

mentioning

confidence: 99%

“…It is also named thiol-specific antioxidant (TSA) [38,39], protector protein (PRP) [11,26], human natural killer cell-enhancing factor-B (NKEF-B) [33,41,40], calpromotin [19,42,43] and torin [44]. Prx II is important in erythroid cell differentiation [11,26] and protects red blood cell membranes from peroxidation [20,45]. It also regulates signal transduction pathways that directly relate to apoptotic cell death [23,27,28,29,46].…”

mentioning

confidence: 99%

See 2 more Smart Citations

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

View full text Add to dashboard Cite

Aims/hypothesis. Insulin-producing beta cells are destroyed by oxidative and nitrosative stress during the pathogenesis of Type I (insulin-dependent) diabetes mellitus. These cells are more sensitive than others due to their deficiency of well known antioxidant enzymes like superoxide dismutase, glutathione peroxidase and catalase. However the peroxiredoxins discovered in the past decade form a large family of highly conserved thioredoxin-dependent peroxide reductases, which are present in most tissues. We investigated whether peroxiredoxins I and II are present in pancreatic beta cells and if they are inducible by oxidative and nitrosative stress. Methods. To detect these enzymes in insulin-producing beta cells we used semiquantitative RT-PCR, western blots and immunohistochemistry. The expression of peroxiredoxins I and II was analysed after treatment with cytokines, hydrogen peroxide, alloxan or streptozotocin in the rat insulinoma cells INS-1 using RT-PCR and western blots. Results. We show that peroxiredoxins I and II are present in the cytoplasm of pancreatic islet cells as well as in insulinoma cell lines βTC6-F7 and INS-1. Peroxiredoxins I and II were up-regulated by all stress agents used. Conclusion/interpretation. Beta cells, undersupplied with well characterized antioxidant enzymes, possess an additional antioxidant system which is inducible by oxidative as well as nitrosative stress. [Diabetologia (2002) 45:867-876]

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

View full text Add to dashboard Cite

show abstract

“…Assays were performed as described previously [18,19] with the following modifications: reaction mixtures contained 16.5 μM FeCl 3 , 1.0 mM DTT and concentrations of Ov-TPx-1 ranging from 6-200 μg/ml were incubated at 37°C. After 30 min, 300 ng of pUC19 supercoiled plasmid was added and the reaction tubes incubated at 37°C for 2.5 h. The mixtures were then examined by agarose gel electrophoresis for evidence of DNA nicking.…”

Section: Antioxidant Activity Assaymentioning

confidence: 99%

Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini

Suttiprapa

Loukas

Laha

et al. 2008

Molecular and Biochemical Parasitology

View full text Add to dashboard Cite

The human liver fluke, Opisthorchis viverrini, induces inflammation of the hepatobiliary system. Despite being constantly exposed to inimical oxygen radicals released from inflammatory cells, the parasite survives for many years. The mechanisms by which it avoids oxidative damage are unknown. In this study, thioredoxin peroxidase (TPx), a member of the peroxiredoxin superfamily, was cloned from an O. viverrini cDNA library. O. viverrini TPx cDNA encoded a polypeptide of 212 amino acid residues, of molecular mass 23.57 kDa. The putative amino acid sequence shared 60-70% identity with TPXs from other helminths and from mammals, and phylogenetic analysis revealed a close relationship between TPxs from O. viverrini and other trematodes. Recombinant O. viverrini TPx was expressed as soluble protein in Escherichia coli.The recombinant protein dimerized, and its antioxidant activity was deduced by observing protection of nicking of supercoiled plasmid DNA by hydroxyl radicals. Antiserum raised against O. viverrini TPx recognized native proteins from egg, metacercaria and adult developmental stages of the liver fluke and excretory-secretory products released by adult O. viverrini. Immunolocalization studies revealed ubiquitous expression of TPx in O. viverrini organs and tissues. TPx was also detected in bile fluid and bile duct epithelial cells surrounding the flukes two weeks after infection of hamsters with O. viverrini. In addition, TPx was observed in the secondary (small) bile ducts where flukes cannot reach due to their large size. These results suggested that O. viverrini TPx plays a significant role in protecting the parasite against damage induced by reactive oxygen species from inflammation.

show abstract

“…In common with GPxs, Prxs are able to reduce hydrogen peroxide and alkyl hydroperoxides (of the form ROOH) to water or the corresponding alcohol (ROH), respectively (Jacobson et al, 1989; Lim et al, 1993;Chae et al, 1994a;Cha & Kim, 1995;Tsuji et al, 1995;Poole and Ellis, 1996;Bruchhaus et al, 1997;Jin et al, 1997;Nogoceke et al, 1997;Shau et al, 1997; Reprint requests to: Chris P. Ponting, University of Oxford, The Old Observatory, Fibrinolysis Research Unit, South Parks Road, Oxford, OX1 3RH, United Kingdom; e-mail: Ponting@bioch.ox.ac.uk. 1998b).…”

mentioning

confidence: 99%

Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

Schröder

Ponting

1998

Protein Science

View full text Add to dashboard Cite

Abstract:Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence-and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.

show abstract

Removals of Hydrogen Peroxide and Hydroxyl Radical by Thiol-Specific Antioxidant Protein as a Possible Role in Vivo

Cited by 176 publications

References 0 publications

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini

Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

Contact Info

Product

Resources

About