Hunting for huntingtin associated factors: Identification and characterization of huntingtin expanded polyglutamine aggregate associated factors and their impact on Huntington disease model cellular toxicity
Abstract
Gene mutations resulting in the formation of insoluble protein aggregates, or amyloid-like structures, have been correlated with a number of pathological conditions. Huntington's disease (HD) is one of the most prevalent neurodegenerative diseases, characterized by movement, memory, behavioral, and cognitive difficulties, which become more severe as the disease progresses. Protein aggregation in HD is caused by expansion of the CAG repeat tract, also known as a polyglutamine (polyQ) expansion, in exon one of the Huntingtin protein (Htt). Research has shown that Huntingtin polyQ (HttpolyQ) mutant expansions beyond 35 repeats result in protein aggregation. These HttpolyQ aggregates form amyloid-like inclusions characterized by cross-beta structure and insolubility; and can result in loss of Huntingtin protein function or sequestration of essential cellular proteins that tightly interact with the aggregate.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 20, 2016
- Accession Number
- AD1036937
Entities
People
- Maggie P. Wear
Organizations
- Uniformed Services University of the Health Sciences