| Autor: |
Nussbaum-Krammer CI; Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University; c.nussbaum@zmbh.uni-heidelberg.de., Neto MF; Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University., Brielmann RM; Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University., Pedersen JS; Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University., Morimoto RI; Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of visualized experiments : JoVE [J Vis Exp] 2015 Jan 08 (95), pp. 52321. Date of Electronic Publication: 2015 Jan 08. |
| DOI: |
10.3791/52321 |
| Abstrakt: |
Prions are unconventional self-propagating proteinaceous particles, devoid of any coding nucleic acid. These proteinaceous seeds serve as templates for the conversion and replication of their benign cellular isoform. Accumulating evidence suggests that many protein aggregates can act as self-propagating templates and corrupt the folding of cognate proteins. Although aggregates can be functional under certain circumstances, this process often leads to the disruption of the cellular protein homeostasis (proteostasis), eventually leading to devastating diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Amyotrophic lateral sclerosis (ALS), or transmissible spongiform encephalopathies (TSEs). The exact mechanisms of prion propagation and cell-to-cell spreading of protein aggregates are still subjects of intense investigation. To further this knowledge, recently a new metazoan model in Caenorhabditis elegans, for expression of the prion domain of the cytosolic yeast prion protein Sup35 has been established. This prion model offers several advantages, as it allows direct monitoring of the fluorescently tagged prion domain in living animals and ease of genetic approaches. Described here are methods to study prion-like behavior of protein aggregates and to identify modifiers of prion-induced toxicity using C. elegans. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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