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Glutamine repeats and neurodegeneration
1Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA. hzoghbi@bcm.tmc.edu
Annual Review of Neuroscience
|June 9, 2000
Summary
Expanded trinucleotide repeats cause neurodegenerative diseases by making proteins toxic to neurons. This review details these polyglutamine disorders and proposes a unifying model for their pathogenesis.
Area of Science:
- Neuroscience
- Genetics
- Molecular Biology
Background:
- Neurodegenerative diseases are increasingly linked to unstable trinucleotide repeat expansions.
- The toxic mechanism of expanded polyglutamine tracts in neurons is under active investigation.
Purpose of the Study:
- To review the clinicopathologic features of polyglutamine disorders.
- To describe the genes and protein products involved.
- To discuss model systems and propose a unifying pathogenesis model.
Main Methods:
- Literature review of clinicopathologic features.
- Analysis of genetic and protein product information.
- Synthesis of data from various model systems.
Main Results:
- Detailed summary of spinobulbar muscular atrophy, Huntington disease, and spinocerebellar ataxias.
- Identification of key genes and their polyglutamine tract expansions.
- Insights from model systems into disease mechanisms.
Conclusions:
- A unifying model for polyglutamine disorder pathogenesis is presented.
- This model highlights common features across these neurodegenerative conditions.
- The proposed model may offer insights into other neurodegenerative diseases.