Premium
Investigation of Cysteamine as a Potential Antioxidant Supplement in TRX1 Yeast Mutants
Author(s) -
Hendershot Allison,
MordanMcCombs Sarah
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.726.12
Subject(s) - thioredoxin , glutaredoxin , cysteamine , glutathione , oxidative stress , antioxidant , biochemistry , reactive oxygen species , chemistry , endogeny , microbiology and biotechnology , biology , enzyme
In 1957, the free radical theory of aging proposed that cellular aging and death are the result of accumulating oxygen‐derived free radicals within the cell. These free radicals, also referred to as reactive oxidative species (ROS), accrue as a result of mitochondrial metabolism and can damage DNA, lipids, and proteins. Studies suggest that ROS‐related damage is associated with diseases such as Alzheimer's and cancer. Cells combat the detrimental effects of ROS by producing endogenous antioxidants, such as the thiol antioxidant glutathione and its associated enzymes, which reduce free radicals to a more stable state. This research seeks to determine the relationship between endogenous and dietary antioxidants, using Saccharomyces cerevisiae as a model system. Here we investigate the role of the TRX1 protein and its involvement in the thioredoxin and glutaredoxin pathways, and the ability of the exogenous antioxidant, cysteamine, to interact with disrupted antioxidant signaling. We hypothesized that, due to the structural similarities between cysteamine and glutathione, cysteamine may be able to act as a surrogate in the glutaredoxin and thioredoxin pathways in the absence of functional glutathione. ΔTRX1 yeast strains were treated with cysteamine, and analyzed for growth, gene expression, and protein expression changes under oxidative stress from hydrogen peroxide. Results indicate alterations in endogenous antioxidant pathways in gene and protein expression levels with deletion of the TRX1 gene and subsequent treatment with cysteamine. This work is supported by the Biology Department at Franklin College and by a grant from the Indiana Academy of Science.