Abstract
Methylthioadenosine (MTA) phosphorylase is the enzyme involved in the metabolism of polyamines and purines.1 MTA, the substrate for this enzyme, is produced during the synthesis of spermine and spermidine and is cleaved to methylthioribose 1-phosphate and adenine, which are recycled to methionine and adenine nucleotide, respectively.1 This enzyme has been known to be deficient in human leukemias, lymphomas, and solid tumors.2,3,4 The gene locus for this enzyme (designated MTAP) has been mapped to human chromosome 9p.5 Enzyme deficient malignant cell lines are frequently found to have chromosome 9p abnormalities.6 Although cytogenetic analysis of human gliomas has demonstrated a very prevalent chromosomal abnormality involving deletions or translocations of chromosome 9p,7 these tumors have not been tested for MTAP deficiency. In this report, we screened eight human glioma cell lines and six primary brain tumors for MTA phosphorylase activities using the radiochemical method and immunoblot analysis. Of 14 cell lines and primary tumors, five cell lines and five primary tumors (70%) were found to be enzyme-deficient. To elucidate the molecular mechanism of this enzyme deficiency and its relevance to the genesis of human brain tumors, DNA analysis and pulsed field gel analysis were carried out.
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© 1991 Plenum Press, New York
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Wu, D.J., Reynolds, L., Carson, D.A., Nobori, T. (1991). Molecular Genetic Analysis of Chromosome 9p in Methylthioadenosine Phosphorylase Deficient Glioma Cell Lines. In: Harkness, R.A., Elion, G.B., Zöllner, N. (eds) Purine and Pyrimidine Metabolism in Man VII. Advances in Experimental Medicine and Biology, vol 309B. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-7703-4_47
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DOI: https://doi.org/10.1007/978-1-4615-7703-4_47
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