eats. Because patients with OPMD show more effects on their eyes and throat as compared to their legs, hip and shoulders, protein binding for the latter three muscle tissues will be less than that of the former two. We would still expect an increase in protein binding for leg, hip, and shoulder muscles with increasing alanine repeats. However, this increase is slower than that of eye/throat muscles. Table 1 also shows that for tests with normal repeats (6), there would not be binding if indeed there is protein binding for expanded repeats, no matter which muscle type. If these results occur, there will be a need for further characterizations of the newly found mutant PABP2-binding proteins. Table 1 shows a situation where a specific protein is binding to extended Ala repeats and more of it binds with increasing repeat size. There may however, be different proteins that bind to the different repeats. This possibility will nonetheless still affirm the hypothesis. The protein(s) that bind to the extended poly A stretches will be involved in the progressive destruction of muscle tissue over time (a characteristic of muscular dystrophies). They will also lead to weakness and loss of muscular function. Because of this senescence phenotype, it can be predicted that the extended poly-A-binding protein(s) may affect(s) proper functioning of telomerases. The protein may also alter the proper functioning of PABP2 and initiate a cascade which results in degradation of muscle tissues. The other possible outcome would be that the decrease in protein binding leads to OPMD (Table 2). The two controls (tests with smooth muscles and tests with 6 Ala repeats) will show significant protein binding. With the onset of the disease, under this scenario, there will be less binding of the particular protein. For experiments with eye or throat muscles, binding is decreased as the number of extended repeats increase. That same pertains to leg, hip ...
