Chaperoning brain diseases

Article Abstract:

The proteins involved in Parkinson's and Alzheimer's disease can be further affected by genetic mutation. This mutation causes harmful, insoluble protein to form in the brain and normal protein then copies the abnormal formation. The failure of prion-related disorders to cross over into other species suggests that another factor must be involved. A molecular chaperone may interact with proteins and provide stability during the protein folding process. Research into brain disease needs to focus on the change of soluble proteins into insoluble aggregates.

Research and Development in the Physical, Engineering, and Life Sciences, Research and Testing Services, Neurological R&D, Parkinson's disease, Parkinson disease, Neurological research

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The prolylisomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Article Abstract:

Pin1, a highly conserved and essential mitotic regulator, binds to only one pT-P motif in tau and copurifies with paired helical filaments (PHFs), leading to a depletion of soluble Pin1 in the brains of people suffering from Alzheimer's disease. As depletion of Pin1 prompts mitotic arrest and apoptosis, Pin1 may be needed to prevent abnormal activation of mitotic events in neurons and to regulate the function of phosphoproteins, such as tau. Both depletion of Pin1 and formation of PHFs could play a role in neuronal loss in Alzheimer's disease.

Causes of, Cell cycle

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