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Altered protein acetylation in polyglutamine diseases
L Bodai1, J Pallos, L M Thompson
1Department of Developmental and Cell Biology, University of California, Irvine, Irvine, CA 92697, USA.
Current Medicinal Chemistry
|October 8, 2003
Summary
Polyglutamine diseases stem from expanded CAG repeats, causing neurodegeneration. Targeting Histone Deacetylases (HDACs) may restore protein acetylation balance and treat these disorders.
Area of Science:
- Neurodegenerative Diseases
- Molecular Biology
- Genetics
Background:
- Polyglutamine diseases are hereditary neurodegenerative disorders.
- Caused by expanded CAG repeats in disease genes, leading to protein aggregation.
- Aberrant protein interactions and cellular dysfunction are hallmarks.
Purpose of the Study:
- To investigate the role of Histone Acetyltransferases (HATs) in polyglutamine diseases.
- To explore the therapeutic potential of targeting Histone Deacetylases (HDACs).
Main Methods:
- Analysis of protein interactions involving polyglutamine domains.
- Studying the impact of polyglutamines on HAT activity.
- Investigating the effects of modulating HDACs on disease pathogenesis.
Main Results:
- Polyglutamines interact with and alter the activity of HATs.
- An imbalance in protein acetylation and deacetylation contributes to pathogenesis.
- Modulating HDACs shows potential for restoring cellular balance.
Conclusions:
- Restoring the balance between acetylation and deacetylation is crucial for treating polyglutamine diseases.
- HDAC inhibitors represent promising therapeutic candidates for these devastating conditions.