Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci)

Rendón, Juan L.; Mena, Irene Patricia del Arenal; Guevara-Flores, Alberto; Uribe, Aída; Plancarte, A.; Mendoza‐Hernández, Guillermo

doi:10.1016/j.molbiopara.2003.09.003

Cited by 76 publications

(98 citation statements)

References 38 publications

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“…The enzyme uses NADPH as electron donor for the reduction of GSSG. GR enables several vital functions of the cell such as the detoxification of free radicals and reactive oxygen species as well as protein and DNA biosynthesis by maintaining a high ratio of GSH/GSSG (Schirmer et al, 1989;Rendón et al, 2004). We observed that the activities of the enzymes decreased with increasing deltamethrin concentrations and exposure time.…”

Section: Modulation Of the Enzyme Activitymentioning

confidence: 49%

Interactions of Fungicides and Pesticides with Specific Enzymes

Ekinci¹,

Şentürk²

2010

Fungicides

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Section: Modulation Of the Enzyme Activitymentioning

confidence: 49%

Interactions of Fungicides and Pesticides with Specific Enzymes

Ekinci¹,

Şentürk²

2010

Fungicides

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“…C-terminal Cys, arises from the hysteretic behavior of the GR activity, first described for T. crassiceps TGR (44) and then observed in all platyhelminth TGRs characterized so far (9,21,26). The GR activity of these TGRs, but not their TR activity, is temporarily inhibited at high [GSSG], exhibiting a lag before achieving full activity (Fig.…”

Section: Hysteresis Is a Conspicuous Feature Of Platyhelminth Tgrsmentioning

confidence: 72%

“…Further, the hysteretic behavior persists after GSSG removal by size exclusion chromatography of a TGR sample treated with GSSG at conditions under which there is hysteresis (9). Taken together, these observations indicate that in all likelihood the phenomenon involves thiol-disulfide exchange reactions (9,44) (Fig. 7).…”

Section: Hysteresis Is a Conspicuous Feature Of Platyhelminth Tgrsmentioning

confidence: 74%

“…In contrast to their hosts, parasitic platyhelminthes lack conventional TR and GR (1,3,21,44). Instead, they rely exclusively on a linked Trx-GSH system in which TGR provides reducing equivalents to both pathways (Fig.…”

Section: Thioredoxin Glutathione Reductase Is the Sole Enzyme That Sumentioning

confidence: 99%

“…The higher the [GSH]/[GSSG] ratio the lower is the lag time. The lag is abolished not only by GSH, but also by Trx and dithiothreitol (DTT) (9,44); and there is evidence that GSH and Trx decrease hysteresis without the need of preincubation (9). Further, the hysteretic behavior persists after GSSG removal by size exclusion chromatography of a TGR sample treated with GSSG at conditions under which there is hysteresis (9).…”

Section: Hysteresis Is a Conspicuous Feature Of Platyhelminth Tgrsmentioning

confidence: 99%

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Thioredoxin Glutathione Reductase-Dependent Redox Networks in Platyhelminth Parasites

Williams

Bonilla²,

Gladyshev³

et al. 2013

Antioxidants & Redox Signaling

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Significance: Platyhelminth parasites cause chronic infections that are a major cause of disability, mortality, and economic losses in developing countries. Maintaining redox homeostasis is a major adaptive problem faced by parasites and its disruption can shift the biochemical balance toward the host. Platyhelminth parasites possess a streamlined thiol-based redox system in which a single enzyme, thioredoxin glutathione reductase (TGR), a fusion of a glutaredoxin (Grx) domain to canonical thioredoxin reductase (TR) domains, supplies electrons to oxidized glutathione (GSSG) and thioredoxin (Trx). TGR has been validated as a drug target for schistosomiasis. Recent Advances: In addition to glutathione (GSH) and Trx reduction, TGR supports GSH-independent deglutathionylation conferring an additional advantage to the TGR redox array. Biochemical and structural studies have shown that the TR activity does not require the Grx domain, while the glutathione reductase and deglutathionylase activities depend on the Grx domain, which receives electrons from the TR domains. The search for TGR inhibitors has identified promising drug leads, notably oxadiazole N-oxides. Critical Issues: A conspicuous feature of platyhelminth TGRs is that their Grx-dependent activities are temporarily inhibited at high GSSG concentrations. The mechanism underlying the phenomenon and its biological relevance are not completely understood. Future Directions: The functional diversity of Trxs and Grxs encoded in platyhelminth genomes remains to be further assessed to thoroughly understand the TGR-dependent redox network. Optimization of TGR inhibitors and identification of compounds targeting other parasite redox enzymes are good options to clinically develop relevant drugs for these neglected, but important diseases. Antioxid. Redox Signal. 19,[735][736][737][738][739][740][741][742][743][744][745]

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Selenoenzymes and Selenium Trafficking: An Emerging Target for Therapeutics

Self

Rosario

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Selenoproteins exist within all three domains of life. It is estimated that one‐third of prokaryotes utilize selenium for specific biological purposes, whereas the majority of microorganisms do not use or need selenium. Selenoproteins are unique proteins in which selenocysteine is inserted into the polypeptide chain by highly specialized translational machinery. Alternatively, some selenoproteins in which selenium is incorporated as a labile cofactor have been characterized, and this class of selenoproteins also contains either molybdenum or tungsten. Although several selenoproteins have been well characterized for several decades, the biological functions of these proteins are still being defined. The role of selenoproteins, particularly in human pathogens, has received little attention, yet there is evidence that targeting such proteins could play a major role in drug development. In addition, emerging evidence suggests that many well‐known cancer drugs target a specific class of selenoproteins in mammals, lending credence to the notion that selenoproteins may indeed already be substantial drug targets in the clinic.

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Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci)

Cited by 76 publications

References 38 publications

Interactions of Fungicides and Pesticides with Specific Enzymes

Interactions of Fungicides and Pesticides with Specific Enzymes

Thioredoxin Glutathione Reductase-Dependent Redox Networks in Platyhelminth Parasites

Selenoenzymes and Selenium Trafficking: An Emerging Target for Therapeutics

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