ИСТИНА

During the development of polyglutamine neurodegenerative disorders such as Huntington disease the abnormal protein expression occurs in the neural tissues causing aggregate formation and neuron death. These mutant proteins comprise in its sequence elongated polyglutamine tracts (from 6-35 to 36-306 glutamine residues) capable to form extended intermolecular secondary structure. It is believed that long polyglutamine tracts cannot be completely hydrolyzed into small peptides by the proteasome. This can result in the accumulation of poorly soluble peptides in the cells, the formation of inclusion bodies, which adversely affect neuronal function manifesting itself in the symptoms of these diseases. It is also possible that the mutant elongated poly-Q proteins inhibiting the proteasome, preventing degradation of other cellular proteins, thereby causing cell apoptosis. The aim of our work is to study the mechanisms of proteasomal degradation of peptides containing polyglutamine sequences.