Glutathione Overview

1) Conditions Studied for Glutathione

Glutathione has been studied for various conditions including but not limited to:

• Chronic diseases such as cancer, heart disease, and diabetes
• Neurodegenerative disorders like Alzheimer's and Parkinson's disease
• Respiratory diseases, including asthma and chronic obstructive pulmonary disease (COPD)
• Liver diseases, including hepatitis and fatty liver disease
• Immune system disorders
• Aging and associated conditions
• Oxidative stress and inflammation

2) Efficacy in Treating Conditions

The effectiveness of glutathione in treating these conditions varies. Some studies suggest potential benefits, whereas others do not show significant therapeutic effects. It is important to note that more research is needed to conclusively determine its efficacy in treating specific conditions.

3) Health Benefits of Glutathione

Glutathione is associated with several health benefits:

• Acts as a powerful antioxidant, neutralizing free radicals
• Supports the immune system
• Detoxifies harmful substances in the body
• May improve skin health
• Potentially improves insulin sensitivity in older individuals

4) Potential Downsides of Glutathione

While generally considered safe, glutathione can have downsides, including:

• Allergic reactions when taken intravenously
• Abdominal cramps and bloating
• Increased asthma symptoms if inhaled
• Potential interaction with medications

It is recommended to consult a healthcare provider before starting any glutathione supplementation.

5) Genetic Variations and Glutathione

Individual genetic variations can influence how beneficial or harmful glutathione is. For instance:

• People with certain genetic mutations affecting glutathione metabolism may benefit from supplementation.
• Conversely, certain genetic variations might cause an individual to experience adverse effects from glutathione supplementation.

Genetic testing and personalized medical advice can help determine if glutathione supplementation is appropriate for an individual.

Glutathione (GSH) in Health and Disease

Glutathione (GSH), a vital thiol-containing antioxidant, plays key roles in protecting against oxidative damage, aiding metabolism, and modulating cellular processes such as gene expression, growth, and immune response. Adequate protein nutrition and certain precursors can boost tissue GSH synthesis. GSH deficiency, linked to diseases like malnutrition, neurological disorders, and diabetes, increases oxidative stress and aging processes.

Redox Regulation and Cell Cycle

The balance between oxidizing and reducing agents is critical for cell survival. Shifts in redox balance can regulate nuclear transcription factors, influencing signaling pathways and cell cycle progression. The glutathione buffer system adjusts cellular responses to redox changes.

Thiol Metabolism and Signaling

Thiol-containing compounds like GSH are central to biochemical processes due to their oxidation and regeneration capabilities. GSH consumption, synthesis, and involvement in signaling pathways are complex and disruptions may contribute to various diseases.

Dietary Glutathione and Plasma Levels

Research on dietary glutathione intake and plasma levels reveals a complex regulation that is not directly proportional to diet or availability of precursor amino acids. Factors such as serum vitamin C levels may influence this relationship.

Glutathione Synthesis and Enzyme Regulation

Gamma-glutamylcysteine synthetase, key in GSH synthesis, is regulated by GSH feedback inhibition. Overexpression of this enzyme's subunits can influence resistance to chemotherapy and radiation in cancer cells.

Glutathione and DNA Deletions

Depletion of GSH induces DNA deletions, which can be prevented by antioxidant supplementation. This suggests a strategy to guard against carcinogenesis related to oxidative stress.

Glutathione and Chemotherapy Resistance

Drug-resistant cancer cells manage oxidative stress better due to higher activity of gamma-glutamylcysteine synthetase, contributing to their resistance to treatment.

Glutathione and Hemolytic Anemia

A case study shows a family with hemolytic anemia due to a deficiency in erythrocyte glutathione synthetase, leading to a concurrent deficiency of glutathione-S-transferase.

Glutathione Transport and Synthesis

Studies on glutathione synthetase, including its cloning and sequencing, help understand its role in GSH synthesis. Transport systems for GSH are significant for maintaining cellular health.

Glutathione S-Transferases and Disease Susceptibility

Glutathione S-transferases (GSTs) are crucial in detoxification and managing oxidative stress. Genetic variations in GSTs can affect disease susceptibility, including cancer and inflammatory conditions.

Glutathione and Benign Prostatic Hyperplasia

Low serum selenium, a factor in the body's antioxidant system, may increase the risk of developing benign prostatic hyperplasia (BPH), although further research is needed.

Glutathione and Aminochrome Toxicity

GSTM2 is essential for protecting against aminochrome-induced cell death by maintaining autophagic and lysosomal function.

Glutathione and Retinal Protection

GSTP1 levels in the retina increase with age and in response to light exposure, potentially serving as a defense against oxidative damage.

Glutathione Transferases and Cellular Detoxification

Theta class GSTs, the oldest and found across species, are involved in cellular detoxification and may influence cancer susceptibility.

Glutathione and Health

Glutathione is a critical molecule in protecting against oxidative stress. Its synthesis involves enzymes regulated by feedback inhibition. Strategies to increase GSH levels could have therapeutic benefits.

References:

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3. Cellular glutathione and thiols metabolism
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5. The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase
6. Glutathione depletion by buthionine sulfoximine induces DNA deletions in mice
7. Enhanced gamma-glutamylcysteine synthetase activity decreases drug-induced oxidative stress levels and cytotoxicity
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14. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution
15. Sequencing and expression of a cDNA for human glutathione synthetase
16. Identification of an essential cysteine residue in human glutathione synthase
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18. Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy
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20. Inhibition of glutathione disulfide reductase by glutathione
21. Glutathione transferases
22. Effects of selenium status, dietary glucosinolate intake and serum glutathione S-transferase α activity on the risk of benign prostatic hyperplasia
23. Glutathione transferase mu 2 protects glioblastoma cells against aminochrome toxicity by preventing autophagy and lysosome dysfunction
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29. Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases
30. Common structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
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48. The gamma-glutamyl cycle: a possible transport system for amino acids
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51. Effect of oxidant exposure on thiol status in the intestinal mucosa
52. Bidirectional glutathione transport by cultured human retinal pigment epithelial cells
53. Identification of a novel, sodium-dependent, reduced glutathione transporter in the rat lens epithelium
54. Analysis of glutathione: implication in redox and detoxification
55. Glutathione conjugation as a bioactivation reaction
56. Identification of the nonsubstrate steroid binding site of rat liver glutathione S-transferase, isozyme 1-1, by the steroid affinity label, 3beta-(iodoacetoxy)dehydroisoandrosterone
57. Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2, M1a-1a, and P1-1
58. Concise review of the glutathione S-transferases and their significance to toxicology
59. Glutathione supplementation and training increases myocardial resistance to ischemia-reperfusion in vivo
60. Glutathione supplementation improves macrophage functions in HIV
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65. Oxygen permeability of thylakoid membranes: electron paramagnetic resonance spin labeling study
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67. Chemistry and biochemistry of superoxide dismutases
68. Glutathione peroxidase family - an evolutionary overview
69. The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
70. Mitochondrial catalase and oxidative injury
71. Reversible inhibition and irreversible inactivation of catalase in presence of hydrogen peroxide
72. Determination of the kinetic parameters for the "suicide substrate" inactivation of bovine liver catalase by hydrogen peroxide
73. Glutathione peroxidase-catalase cooperativity is required for resistance to hydrogen peroxide by mature rat oligodendrocytes
74. Reactive oxygen species as intracellular messengers during cell growth and differentiation
75. Sequence-specific DNA cleavage by Fe2+-mediated fenton reactions has possible biological implications
76. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
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84. Nutrient supplementation: improving male fertility fourfold
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92. Age-related changes in the glutathione redox system
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94. Decreased synthetic capacity underlies the age-associated decline in glutathione content in Fisher 344 rats
95. Deficient synthesis of glutathione underlies oxidative stress in aging and can be corrected by dietary cysteine and glycine supplementation
96. Whole-body protein turnover in the healthy elderly
97. Protein requirements and ageing: metabolic demand and efficiency of utilization
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99. Blood glutathione synthesis rates in healthy adults receiving a sulfur amino acid-free diet
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106. Oxidative stress in autism
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109. A prospective study of transsulfuration biomarkers in autistic disorders
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120. Macrophages can convert citrulline into arginine
121. Combined L-citrulline and glutathione supplementation increases the concentration of markers indicative of nitric oxide synthesis

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