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Antioxidants
Volume 13
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10.3390/antiox13040444
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Article

A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia

by
Alberto Guevara-Flores
1,
Gabriela Nava-Balderas
2,*,
José de Jesús Martínez-González
1,
César Vásquez-Lima
1,
Juan Luis Rendón
1 and
Irene Patricia del Arenal Mena
1,*
1
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México (UNAM), Apartado Postal 70-159, Mexico City 04510, Mexico
2
Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México (UNAM), Apartado Postal 70-159, Mexico City 04510, Mexico
*
Authors to whom correspondence should be addressed.
Antioxidants 2024, 13(4), 444; https://doi.org/10.3390/antiox13040444
Submission received: 1 February 2024 / Revised: 2 April 2024 / Accepted: 4 April 2024 / Published: 10 April 2024
(This article belongs to the Section Antioxidant Enzyme Systems)
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Abstract

Peroxiredoxins (Prxs) and glutathione peroxidases (GPxs) are the main enzymes of the thiol-dependent antioxidant systems responsible for reducing the H2O2 produced via aerobic metabolism or parasitic organisms by the host organism. These antioxidant systems maintain a proper redox state in cells. The cysticerci of Taenia crassiceps tolerate millimolar concentrations of this oxidant. To understand the role played by Prxs in this cestode, two genes for Prxs, identified in the genome of Taenia solium (TsPrx1 and TsPrx3), were cloned. The sequence of the proteins suggests that both isoforms belong to the class of typical Prxs 2-Cys. In addition, TsPrx3 harbors a mitochondrial localization signal peptide and two motifs (-GGLG- and -YP-) associated with overoxidation. Our kinetic characterization assigns them as thioredoxin peroxidases (TPxs). While TsPrx1 and TsPrx3 exhibit the same catalytic efficiency, thioredoxin–glutathione reductase from T. crassiceps (TcTGR) was five and eight times higher. Additionally, the latter demonstrated a lower affinity (>30-fold) for H2O2 in comparison with TsPrx1 and TsPrx3. The TcTGR contains a Sec residue in its C-terminal, which confers additional peroxidase activity. The aforementioned aspect implies that TsPrx1 and TsPrx3 are catalytically active at low H2O2 concentrations, and the TcTGR acts at high H2O2 concentrations. These results may explain why the T. crassiceps cysticerci can tolerate high H2O2 concentrations.
Keywords: peroxiredoxins; Taenia crassiceps; thioredoxin–glutathione reductase; hydrogen peroxide peroxiredoxins; Taenia crassiceps; thioredoxin–glutathione reductase; hydrogen peroxide
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MDPI and ACS Style

Guevara-Flores, A.; Nava-Balderas, G.; de Jesús Martínez-González, J.; Vásquez-Lima, C.; Rendón, J.L.; del Arenal Mena, I.P. A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia. Antioxidants 2024, 13, 444. https://doi.org/10.3390/antiox13040444

AMA Style

Guevara-Flores A, Nava-Balderas G, de Jesús Martínez-González J, Vásquez-Lima C, Rendón JL, del Arenal Mena IP. A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia. Antioxidants. 2024; 13(4):444. https://doi.org/10.3390/antiox13040444

Chicago/Turabian Style

Guevara-Flores, Alberto, Gabriela Nava-Balderas, José de Jesús Martínez-González, César Vásquez-Lima, Juan Luis Rendón, and Irene Patricia del Arenal Mena. 2024. "A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia" Antioxidants 13, no. 4: 444. https://doi.org/10.3390/antiox13040444

APA Style

Guevara-Flores, A., Nava-Balderas, G., de Jesús Martínez-González, J., Vásquez-Lima, C., Rendón, J. L., & del Arenal Mena, I. P. (2024). A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia. Antioxidants, 13(4), 444. https://doi.org/10.3390/antiox13040444

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