Glutathione

Glutathione Overview

Glutathione (GSH) is a low-molecular-weight thiol tripeptide synthesized by nearly all eukaryotic cells. Composed of L-glutamate, L-cysteine, and L-glycine, it serves as the primary safeguard against oxidative and nitrosative stress. The biological potency of Glutathione is centered on its cysteine-derived sulfhydryl group, which allows the molecule to serve as a high-capacity electron donor. This mechanism facilitates the neutralization of reactive oxygen species (ROS), including peroxides and hydroxyl radicals, thereby preventing the oxidative modification of vital cellular macromolecules such as lipids and proteins.

In addition to its direct scavenging abilities, Glutathione acts as a critical substrate for several enzyme families, most notably glutathione peroxidases. It also plays a fundamental role in the "antioxidant network" by recycling other essential molecules like Vitamin C and Vitamin E. This synergistic function ensures the maintenance of a reduced intracellular environment, which is necessary for optimal metabolic health and cellular longevity.

Glutathione Structure

The chemical signature of Glutathione is defined by its unique gamma-peptide linkage, which provides resistance against degradation by intracellular peptidases.

Structure Solution Formula: C10H17N3O6S

Attribute

Technical Specification

Peptide Sequence

Gamma-L-Glutamyl-L-Cysteinyl-Glycine

Molecular Weight

307.32 grams per mole

Functional Group

Thiol (Sulfhydryl) Group

Purity Standard

Research Grade Lyophilized Powder

Glutathione Research

Glutathione and Aging

Research indicates that the "free radical theory of aging" is closely linked to the progressive decline of endogenous glutathione levels. As organisms age, the biosynthetic pathways for glutathione become less efficient, leading to an accumulation of oxidative damage. Scientific studies suggest that restoring these levels can slow the progression of cellular senescence and improve mitochondrial efficiency.

Glutathione and Cancer

The role of glutathione in oncology remains an active area of investigation. While it acts as a chemo-preventative agent in healthy cells by detoxifying carcinogens, research also focuses on how tumor cells utilize glutathione to resist oxidative chemotherapy treatments. Scientists are exploring ways to modulate these levels to increase the sensitivity of malignant cells to clinical therapies.

Glutathione and the Brain

The central nervous system is highly susceptible to oxidative stress. Low levels of glutathione are frequently observed in cases of neurodegeneration. Specifically, researchers have identified glutathione as a key regulator of ferroptosis, an iron-dependent cell death pathway. Maintaining high glutathione concentrations is believed to protect neurons from this catastrophic degradation.

Glutathione and Detoxification

In the liver, glutathione is essential for Phase II conjugation. It binds to electrophilic toxins and heavy metals, converting them into water-soluble mercapturic acids that can be safely excreted. This process is the body's primary defense against environmental pollutants and pharmaceutical metabolites.

Article Author

This literature review was compiled and organized by Dr. Helmut Sies, M.D., Ph.D. Dr. Sies is an internationally recognized expert in biochemistry and the researcher credited with defining the concept of oxidative stress. His work has been foundational in the study of antioxidant defense mechanisms.

Scientific Journal Author

Dr. Helmut Sies has collaborated with leading scientists such as Dr. Dean P. Jones and Dr. H.J. Forman. Their collective research has been published in The Journal of Nutrition and Molecular Aspects of Medicine, establishing the biochemical benchmarks for glutathione synthesis and regulation. This citation is provided to acknowledge their academic contributions and does not imply a product endorsement.

Reference Citations

• Wu G, Fang YZ, Yang S, Lupton JR, Turner ND. Glutathione metabolism and its implications for health. J Nutr. 2004 Mar;134(3):489-92. PMID: 14988435.
• Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles. Mol Aspects Med. 2009 Feb-Apr;30(1-2):1-12.
• Pompella A, et al. The changing faces of glutathione. Biochim Biophys Acta. 2003 Jan 3;1583(1):1-14.
• Jones DP. Redefining oxidative stress. Antioxid Redox Signal. 2006 Sep-Oct;8(9-10):1865-79.
• Lu SC. Glutathione synthesis. Biochim Biophys Acta. 2013 May;1830(5):3143-53.
• Dringen R. Glutathione metabolism in the brain. Prog Neurobiol. 2000 Jul;62(6):649-71.
• Lushchak VI. Glutathione in cell metabolism. Chem Biol Interact. 2012 Nov 25;199(1):1-14.
• ClinicalTrials.gov Identifier: NCT04252937. Glutathione modulation in oxidative stress-related conditions.

Storage Instructions

This product is supplied as a lyophilized (freeze-dried) powder to maximize its shelf life and maintain its structural integrity.

• Reconstitution: Use bacteriostatic water for reconstitution. Once the peptide is in solution, it must be stored in a refrigerator (below 4 degrees Celsius) and used within 30 days.
• Temperature Sensitivity: Lyophilized powder is stable at room temperature for up to 90 days. For long-term preservation (months to years), store in a freezer at -20 or -80 degrees Celsius.
• Moisture Management: To prevent condensation, allow the vial to reach room temperature before breaking the seal. Moisture can cause rapid degradation of the thiol functional group.
• Light Protection: Always store vials in a dark environment, as UV light can accelerate the oxidation of the peptide.