Neurodegenerative dementias involving aberrant protein aggregation

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Abstract

Inclusion bodies are common features of neurodegenerative disorders. Recently, it was shown that inclusion bodies are the result of aberrant protein aggregation. Thus, neurodegenerative diseases are classified into five categories: amyloidopathy, tauopathy, synucleinopathy, polyglutamine diseases, and prion diseases. Because the aggregated proteins are insoluble and highly ubiquitinated, the proteins that should have been metabolized by the ubiquitin-proteasome system (UPS) accumulate to form inclusion bodies. We propose the following mechanisms as a hypothesis for neurodegenerative dementia: (1) aberrant protein aggregation overloads the UPS, (2) the disturbed UPS affects endoplasmic reticulum-associated degradation (ERAD), (3) disturbed ERAD impairs the unfolded protein response (UPR), and (4) prolonged UPR causes ER-mediated apoptosis. © 2007 Springer-Verlag US.

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Kudo, T., & Takeda, M. (2007). Neurodegenerative dementias involving aberrant protein aggregation. In Handbook of Neurochemistry and Molecular Neurobiology: Neural Protein Metabolism and Function (pp. 345–353). Springer US. https://doi.org/10.1007/978-0-387-30379-6_11

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