Monoclonal antibodies to 5'-deoxy-5' methylthioadenosine phosphorylase Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/z029p804m

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  • 5'-Deoxy-5'-methylthioadenosine phosphorylase catalyzes the phosphorolytic cleavage of 5'-deoxy-5'-methylthioadenosine to form 5'-deoxy-5'-methylthioribose-1-phosphate and adenine in mammalian cells and plays an important role in methionine and purine salvage. The enzyme is abundant in normal tissues and in cell lines derived from normal cells. However, several malignant tissues and cell lines have been shown to be devoid of detectable enzyme activity. Methylthioadenosine phosphorylase-deficient cells have no unique phenotype and are difficult to detect by means other than enzyme assays. Whether the lack of enzyme activity reflects a defective or absent protein is unknown. In an attempt to determine the nature of methylthioadenosine phosphorylase deficiency, I employed hybridoma technology to produce a series of monoclonal IgM anti-bovine methylthioadenosine phosphorylase antibodies which were used to detect the enzyme. Preliminary data demonstrated that the monoclonal antibodies strongly crossreact with the enzyme from both equine liver and human placenta, particularly the latter. The strongest responders were utilized for the immunodetection of methylthioadenosine phosphorylase in both enzyme-containing and deficient malignant cells and tissues. The data demonstrated that the antibodies not only reacted strongly with most malignant enzyme-containing samples, but also with some samples which lacked detectable enzyme activity. Western blot analysis revealed that the crossreactive material co-migrated with human placental methylthioadenosine phosphorylase. In conclusion, the monoclonal antibodies exhibited immunological specificity for methylthioadenosine phosphorylase in a variety of tissues and cells. For the first time, immunological evidence is provided suggesting that the phenotypic nature of methylthioadenosine ph-dsphorylase deficiency can arise from either a defective enzyme or the complete absence of the protein.
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