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Amyloid Fragmentation and Disaggregation in Yeast and Animals.
Vitaly V Kushnirov1, Alexander A Dergalev1, Alexander I Alexandrov1
1Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, 119071 Moscow, Russia.
Biomolecules
|December 24, 2021
Summary
Chaperone proteins like Hsp104 can break down harmful amyloid aggregates. This mechanism, present in yeast and animals, shows potential for treating incurable amyloid diseases.
Area of Science:
- Molecular biology
- Neurodegenerative disease research
- Protein aggregation studies
Background:
- Amyloid aggregates cause incurable diseases (amyloidoses).
- Fungal prions propagate via chaperone Hsp104, which fragments amyloid fibrils.
- Animals lack Hsp104 but use similar chaperones (Hsp40, Hsp70, Hsp110) for disaggregation.
Purpose of the Study:
- To review chaperone mechanisms for disassembling protein aggregates in yeast and animals.
- To explore the therapeutic potential of these mechanisms for human amyloid diseases.
Main Methods:
- Comparative analysis of chaperone functions in yeast and animal models.
- Review of Hsp104's role in prion propagation and disaggregation.
- Examination of chaperone cooperation in amyloid disaggregation.
Main Results:
- Hsp104 fragments amyloid fibrils, promoting propagation at normal levels.
- Animal chaperones (Hsp40, Hsp70, Hsp110) perform disaggregation.
- Exogenous Hsp104 collaborates with animal chaperones, aiding disaggregation of large aggregates.
Conclusions:
- Chaperone-mediated disaggregation offers a potential therapeutic strategy for amyloid diseases.
- While promising, Hsp104 and variants may not fully resolve amyloid aggregates alone.
