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Nutrients
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Glutathione and Its Related Enzymes in Health and Diseases
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Glutathione and Its Related Enzymes in Health and Diseases

A special issue of Nutrients (ISSN 2072-6643). This special issue belongs to the section "Proteins and Amino Acids".

Deadline for manuscript submissions: closed (5 September 2024) | Viewed by 12125

Special Issue Editor

Prof. Dr. Yi-Chia Huang

E-Mail Website
Guest Editor
Department of Nutrition, Chung Shan Medical University, Taichung 40201, Taiwan
Interests: oxidative stress; antioxidant capacity and nutrition; critical care and nutrition

Special Issue Information

Dear Colleagues,

High oxidative stress and increased inflammatory responses might have potential adverse impacts on human health, and further lead to disease development. Adequate antioxidant capacities are thus indispensable for humans to overcome the threats of high oxidative stress and inflammation, and further prevent or slow disease progression.

Glutathione (GSH) is a thiol and tripeptide molecule synthesized using cysteine, glycine, and glutamate in the liver. The thiol group of cysteine is a major limiting substrate for the GSH synthesis within cells. GSH and its related enzymes (i.e., glutathione peroxidase and glutathione S-transferase) constitute an important endogenous antioxidant system in the human body. Glutathione peroxidase acts as the first line of the antioxidant defense system, while GSH and glutathione S-transferase are situated in the second line. In addition, GSH might have an anti-inflammatory role in different diseases. Consequently, GSH and its related antioxidant enzymes might have important roles in human health and disease. However, the influences of GSH and its related antioxidant enzymes on human health and disease have not been deeply investigated.

This Special Issue, entitled “Glutathione and Its Related Enzymes in Health and Diseases”, will focus on the role of GSH and its related antioxidant enzymes in human health and all kinds of disease. We are interested in exploring how GSH and its related antioxidant enzymes regulate oxidative stress or inflammatory responses before, during and after disease development. In addition, any factors affecting GSH and its related antioxidant enzyme capacities will be also discussed in this Special Issue. 

Prof. Dr. Yi-Chia Huang
Guest Editor

Manuscript Submission Information

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Keywords

  • glutathione
  • glutathione peroxidase
  • glutathione S-transferase
  • oxidative stress
  • antioxidant capacity
  • inflammation
  • health and diseases

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Published Papers (3 papers)

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Research

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11 pages, 611 KiB  
Article
Oxidative Stress Induced by Chemotherapy: Evaluation of Glutathione and Its Related Antioxidant Enzyme Dynamics in Patients with Colorectal Cancer
by Feng-Fan Chiang, Shih-Chien Huang, Pei-Ting Yu, Te-Hsin Chao and Yi-Chia Huang
Nutrients 2023, 15(24), 5104; https://doi.org/10.3390/nu15245104 - 14 Dec 2023
Cited by 12 | Viewed by 2882
Abstract
One of the mechanisms of chemotherapy is to increase the oxidative stress of cancer cells, leading to their apoptosis. Glutathione (GSH) and its related antioxidant enzymes might be stimulated to cope with increased oxidative stress during chemotherapy. Here, we studied the fluctuation in [...] Read more.
One of the mechanisms of chemotherapy is to increase the oxidative stress of cancer cells, leading to their apoptosis. Glutathione (GSH) and its related antioxidant enzymes might be stimulated to cope with increased oxidative stress during chemotherapy. Here, we studied the fluctuation in oxidative stress and GSH-related antioxidant capacities before tumor resection, after tumor resection, and after resection either with or without chemotherapy in patients with colorectal cancer (CRC). This was a cross-sectional and follow-up design. We followed patients before having tumor resection (pre-resection), one month after tumor resection (post-resection), and after the first scheduled chemotherapy (post-chemo). If patients were required to receive chemotherapy after tumor resection, they were assigned to the chemotherapy group. Eligible patients were scheduled to undergo six to twelve cycles of chemotherapy at 2-week intervals and received single, double, or triple chemotherapeutic drugs as required. Those patients who did not require chemotherapy were assigned to the non-chemotherapy group. Indicators of oxidative stress and GSH-related antioxidant capacities were determined at the above three time points. We found in 48 patients of the chemotherapy group and in 43 patients of the non-chemotherapy group different fluctuations in levels of oxidative stress indicators and GSH-related antioxidant capacities starting from pre-resection, post-resection through the post-chemo period. Both groups showed significantly or slightly increased levels of advanced oxidation protein products (AOPP), GSH, and its related enzymes in tumor tissues compared to adjacent normal tissues. Patients in the chemotherapy group had significantly lower plasma levels of GSH and glutathione disulfide (GSSG), but had significantly higher plasma glutathione peroxidase and glutathione reductase activities than patients in the non-chemotherapy group post-chemo. Plasma levels of malondialdehyde and AOPP were positively or negatively associated with GSH and GSSG levels post-chemo after adjustment for age, sex, and histological grading in patients receiving chemotherapy. These significant associations were, however, not seen in patients without chemotherapy. Patients with CRC may require higher GSH demands to cope with a greater oxidative stress resulting from chemotherapy. Full article
(This article belongs to the Special Issue Glutathione and Its Related Enzymes in Health and Diseases)
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Review

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22 pages, 1339 KiB  
Review
The Role of S-Glutathionylation in Health and Disease: A Bird’s Eye View
by Luca Federici, Michele Masulli, Vincenzo De Laurenzi and Nerino Allocati
Nutrients 2024, 16(16), 2753; https://doi.org/10.3390/nu16162753 - 18 Aug 2024
Cited by 3 | Viewed by 2101
Abstract
Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays a role in the regulation of several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains [...] Read more.
Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays a role in the regulation of several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains redox homeostasis, and shields several proteins from irreversible oxidative stress. Aberrant GS-ylation patterns are thus implicated in various diseases, particularly those associated with oxidative stress and inflammation, such as cardiovascular diseases, neurodegenerative disorders, cancer, and many others. Research in the recent years has highlighted the potential to manipulate protein GS-ylation for therapeutic purposes with strategies that imply both its enhancement and inhibition according to different cases. Moreover, it has become increasingly evident that monitoring the GS-ylation status of selected proteins offers diagnostic potential in different diseases. In this review, we try to summarize recent research in the field with a focus on our current understanding of the molecular mechanisms related to aberrant protein GS-ylation. Full article
(This article belongs to the Special Issue Glutathione and Its Related Enzymes in Health and Diseases)
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15 pages, 346 KiB  
Review
Nebulized Glutathione as a Key Antioxidant for the Treatment of Oxidative Stress in Neurodegenerative Conditions
by João Vitor Lana, Alexandre Rios, Renata Takeyama, Napoliane Santos, Luyddy Pires, Gabriel Silva Santos, Izair Jefthé Rodrigues, Madhan Jeyaraman, Joseph Purita and Jose Fábio Lana
Nutrients 2024, 16(15), 2476; https://doi.org/10.3390/nu16152476 - 31 Jul 2024
Cited by 24 | Viewed by 6469
Abstract
Glutathione (GSH), a tripeptide synthesized intracellularly, serves as a pivotal antioxidant, neutralizing reactive oxygen species (ROS) and reactive nitrogen species (RNS) while maintaining redox homeostasis and detoxifying xenobiotics. Its potent antioxidant properties, particularly attributed to the sulfhydryl group (-SH) in cysteine, are crucial [...] Read more.
Glutathione (GSH), a tripeptide synthesized intracellularly, serves as a pivotal antioxidant, neutralizing reactive oxygen species (ROS) and reactive nitrogen species (RNS) while maintaining redox homeostasis and detoxifying xenobiotics. Its potent antioxidant properties, particularly attributed to the sulfhydryl group (-SH) in cysteine, are crucial for cellular health across various organelles. The glutathione-glutathione disulfide (GSH-GSSG) cycle is facilitated by enzymes like glutathione peroxidase (GPx) and glutathione reductase (GR), thus aiding in detoxification processes and mitigating oxidative damage and inflammation. Mitochondria, being primary sources of reactive oxygen species, benefit significantly from GSH, which regulates metal homeostasis and supports autophagy, apoptosis, and ferroptosis, playing a fundamental role in neuroprotection. The vulnerability of the brain to oxidative stress underscores the importance of GSH in neurological disorders and regenerative medicine. Nebulization of glutathione presents a novel and promising approach to delivering this antioxidant directly to the central nervous system (CNS), potentially enhancing its bioavailability and therapeutic efficacy. This method may offer significant advantages in mitigating neurodegeneration by enhancing nuclear factor erythroid 2-related factor 2 (NRF2) pathway signaling and mitochondrial function, thereby providing direct neuroprotection. By addressing oxidative stress and its detrimental effects on neuronal health, nebulized GSH could play a crucial role in managing and potentially ameliorating conditions such as Parkinson’s Disease (PD) and Alzheimer’s Disease (AD). Further clinical research is warranted to elucidate the therapeutic potential of nebulized GSH in preserving mitochondrial health, enhancing CNS function, and combating neurodegenerative conditions, aiming to improve outcomes for individuals affected by brain diseases characterized by oxidative stress and neuroinflammation. Full article
(This article belongs to the Special Issue Glutathione and Its Related Enzymes in Health and Diseases)
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