The exploitation of methylthioadenosine phosphorylase deficiency in cancer therapy Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/h989r5906

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  • Methylthioadenosine (MTA) is a naturally occuring nucleoside formed during the synthesis of polyamines in mammalian cells. MTA is rapidly catabolised by MTA phosphorylase (MTAase), eventually yielding methionine and adenine. MTAase has been shown to be active in all normal cells, but deficient in some cells and tissues of malignant origin. A protocol has been developed which potentially exploits this metabolic difference between normal and malignant cells, focussing on MTA as the sole methionine source in a methionine deficient rodent chow. All normal cells in a rodent on this diet would possess MTAase and be able to catabolise MTA to obtain methionine. Introduced MTAase negative tumor cells would not be able to scavenge methionine from the MTA in the diet and would be selectively starved for methionine. MTA as a replacement for methionine in the diet of mice could only partially support their growth, and could not selectively starve MTAase deficient tumors present in those mice. MTA as a replacement for methionine in the diet of rats could support an average of 35% of normal weight gain, and could not selectively starve MTAase negative tumors present in those rats. The effect of tumor on methionine metabolism is discussed in relation to the inability of MTA to provide selective starvation.
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