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Previous Article | Next Article
Volume 16, Number 20, Issue of October 15, 1996 pp. 6394-6401
Copyright ©1996 Society for NeuroscienceThe Role of Monoamine Metabolism in Oxidative Glutamate Toxicity
Received May 10, 1996; revised July 24, 1996; accepted July 31, 1996.
Pamela Maher1 and John B. Davis2 1 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, and 2 The Salk Institute for Biological Studies, San Diego, California 92186-5800
Glutamate kills neuronal cells by either a receptor-mediated pathway or the inhibition of cystine uptake, the ``oxidative pathway.'' Antioxidants can block cell death initiated by either pathway, suggesting that toxicity is dependent on the production of free radicals. We provide evidence that in a neuronal cell line, glutamate toxicity via the oxidative pathway requires monoamine metabolism as a source of free radicals. Glutamate toxicity is inhibited by monoamine oxidase (MAO) type-A-specific inhibitors, but only at concentrations much higher than those required to inhibit classical type-A MAO. Toxicity is not inhibited by MAO type-B-specific inhibitors at any concentration. Furthermore, treatment of cells with agents that block monoamine uptake inhibits glutamate toxicity. These results suggest that an enzyme distinct from MAO is involved in monoamine metabolism and demonstrate a relationship between glutamate toxicity and monoamine metabolism. These data also have implications for the understanding and treatment of neurodegenerative disorders in which glutamate toxicity is thought to be involved.
Key words: glutamate toxicity; free radicals; monoamine oxidase; neuronal cells; Parkinson's disease; hydrogen peroxide; dopamine
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