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Introduction Glutathione (GSH) is mainly present in the cytosol, and its distribution between the intracellular compartments is crucial to regulate redox homeostasis, gene expression, cell signaling and proliferation ( Sies 1999 ). The
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Character and function Glutathione peroxidase 1 GPxl, GPXl KO mouse shows highly sensitive to oxidative stress Glutathione peroxidase 2 GPx2, GPX2 Protein levels are maintained under selenium deficiency Glutathione peroxidase 3
Laboratory of Comparative Neurobiology, Cavanilles Institute of Biodiversity and Evolutionary Biology, University of Valencia, Valencia, Spain
INSERM UMR1141, Université Paris Diderot, Sorbonne Paris Cité, Paris, France
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Division of Neonatology, University and Polytechnic Hospital La Fe, Valencia, Spain
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Department of Physiology, University of Valencia, Burjassot, Spain
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of catalytic transition metals especially iron in some regions of the brain plus a low activity of antioxidant enzymes such as glutathione peroxidase (GPx) and catalase (CAT), and a high aerobic metabolic rate with high oxygen consumption undoubtedly
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ascorbic acid or glutathione ( Buettner 1993 ). Thus, under ‘normal’ conditions, neither the accumulation of oxidized lipids nor oxidized tocopherol (tocopheryl quinone – the two-electron oxidation product) occurs. By contrast, α-tocopherol deficiency, when
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Department of Clinical Nutrition, Faculty of Applied Medical Sciences, Umm Al-Qura University, Makkah, KSA
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sex hormone in females, are reported to possess antioxidative properties, notably through their ability to increase antioxidative proteins, such as glutathione peroxidases (GPX), reduced glutathione, and manganese-dependent superoxide dismutases
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Objective: This work characterized fluctuations in cell components involved in the regulation of cell redox homeostasis during Caco-2 cell differentiation into enterocytes.
Methods: Caco-2 cells were differentiated for 10 days. Gene expression of NADPH oxidases; enzymes that metabolize superoxide anion and hydrogen peroxide, proteins involved in the production and/or regeneration of glutathione, thioredoxin, and in NADPH production, and Nrf2-dependent genes were measured by qPCR at 0, 1, 4, 7, and 10 days post-confluence.
Results: NADPH oxidase 1 mRNA levels decreased with Caco-2 cell differentiation, in agreement with its role in regulating cell proliferation. NADPH oxidase 4, DUOX2, superoxide dismutase 1 and catalase mRNA levels increased with differentiation. Nrf2 mRNA levels increased with differentiation up to day 4 post-confluence, reaching a plateau until day 10. A similar pattern was observed for the Nrf2-regulated genes: NAD(P)H quinone dehydrogenase 1, glutathione reductase 1, and thioredoxin reductase 1. On the contrary, glutamate-cysteine ligase catalytic subunit mRNA levels decreased after reaching a maximum 4 days post-confluence. This and the finding of a correlation between glutathione reductase 1 and thioredoxin reductase 1 mRNA levels, suggest that recycling of glutathione and thioredoxin is more relevant than their synthesis during Caco-2 cell differentiation.
Conclusion: Results support the relevance of redox homeostasis for cell fate decisions and in preparing enterocytes to interact with their environment.
Significance statement: Current findings resemble changes in redox components previously characterized in vivo. This stresses the concept that Caco-2 cells are an appropriate model to be used to evaluate redox-regulated mechanisms in human enterocytes.
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Department of Environmental Health Science, Ajayi Crowther University, Oyo, Nigeria
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), sulfosalicyclic acid, di-potassium orthophosphate, potassium di-hydrogen orthophosphate, BSA, thiobarbituric acid (TBA), glutathione and 1-chloro-2,4-dinitrobenzene and all additional reagents were purchased from Sigma–Aldrich and were of analytical grade
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is a precursor of glutathione, this finding suggests persistent oxidative stress in these patients ( Sitole et al. 2022 ). Antioxidant approaches to HIV infection The control of imbalanced redox status by antioxidants might be beneficial for
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Department of Pharmacology and Toxicology, Virginia Commonwealth University, Richmond, Virginia, USA
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Department of Pharmacology and Toxicology, Virginia Commonwealth University, Richmond, Virginia, USA
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Department of Pharmacology, College of Graduate Studies, Midwestern University, Downers Grove, Illinois, USA
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) acts as the major co-factor in glutathione reductase enzyme activity. Glutathione could effectively perform its antioxidant capacity in its reduced form and lack or deprivation of riboflavin could lead to a reduced glutathione status disrupting cellular
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homeostasis including the regulation of the vascular tone, blood flow and vessel vasodilation. NO may diffuse to adjacent cells to promote smooth muscle cell (SMC) relaxation and inhibit their proliferation ( Fig. 1 ). NO and NO-derived species such as S-nitroso-glutathione
