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.
CITATION STYLE
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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