... can inclusions bodies be good news for neurodegenerative diseases?
A potential new treatment for neurodegenerative disorders, which seems to be able to reduce the toxic protein aggregates characteristic of many of these diseases, is published online this week in the journal Proceedings of the National Academy of Sciences. Since it is believed that in most neurodegenerative disorders, like Parkinson and Huntington’s disease (PD and HD respectively), abnormal protein aggregates are major culprits associated with neurodegeneration, this research may have important implications for the lives of thousands of neurodegenerative patients all over the world.
Parkinson’s and Huntington’s diseases are incurable devastating brain disorders that result from the death of brain cells associated with muscle control. Both illnesses, like many other neurodegenerative diseases, result from the formation of misshaped/incorrectly folded versions of normal proteins (all proteins have a specific shape/folding associated with their normal function) that tend to clump together leading to the death of the cells in the neighbourhood.
Catarina Amorim | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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