Glutathione is a Cysteine-Containing Tripeptide - Electrophile Scavenger and Antioxidant Glutathione S-transferase catalyzes the conjugation of glutathione.

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Presentation transcript:

Glutathione is a Cysteine-Containing Tripeptide - Electrophile Scavenger and Antioxidant Glutathione S-transferase catalyzes the conjugation of glutathione with foreign compounds and their metabolites. Conjugation reduces activity of xenobiotics and allows removal from body by increasing polarity and water solubility. Glutathione (GSH): glutamic acid-cysteine-glycine

Aflatoxin-B 1 Toxicity via DNA Alkylation Aflatoxin B1 Aspergillus flavus Fungus in contaminated nuts and grains Aflatoxin B1 epoxide Electrophilic metabolite Toxin bound to DNA Inhibition of DNA replication, RNA synthesis, mutagenesis liver DNA guanine residue Aflatoxin B1 epoxide Electrophilic metabolite

Glutathione Conjugation with Aflatoxin-B 1 Metabolite Allows its Removal From Body Aflatoxin B1 Glutathione Aflatoxin B1 epoxide Glutathione aflatoxin conjugate Detoxification via conjugation and removal from body

Glutathione (GSH) and Glutathione Disulfide (GSSG) Glutathione (GSH) Glutathione disulfide (GSSG) Oxidation Reduction

Glutathione is an Antioxidant Glutathione peroxidase (GSH peroxidase) Glutathione reductase (GSSG reductase) ROOH NADH Glutathione (GSH) Glutathione disulfide (GSSG) Oxidation of glutathione spares other endogenous substrates

Insulin Conversion of glucose to glycogen Oxytocin (Petocin®) Labor, lactation, pair bonding Disulfide Bridges in Peptide Hormones