Gewählte Publikation:
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Neuro
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Kardio
Lipid
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Microb
Aigelsreiter, A; Janig, E; Stumptner, C; Fuchsbichler, A; Zatloukal, K; Denk, H.
How a cell deals with abnormal proteins. Pathogenetic mechanisms in protein aggregation diseases.
Pathobiology. 2007; 74(3): 145-158.
Doi: 10.1159/000103374
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PubMed
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- Führende Autor*innen der Med Uni Graz
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Aigelsreiter Ariane
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Denk Helmut
- Co-Autor*innen der Med Uni Graz
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Janig Elke
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Stumptner Cornelia
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Zatloukal Kurt
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- Abstract:
- Defective protein folding is responsible for many diseases. Although these diseases seem to be quite diverse at the first glance, there is evidence for common pathogenetic principles. The basis of the pathological changes is the cell's inability to prevent protein misfolding, to revert misfolded proteins to normal or to eliminate misfolded proteins by degradation. This could result in deposition of potentially cytotoxic protein aggregates (protein aggregation diseases). Chronic degenerative diseases of the central nervous system (e.g. Alzheimer's and Parkinson's disease), the amyloidoses, but also chronic liver diseases, for example alcoholic and nonalcoholic steatohepatitis, belong to this category of disorders. This review highlights general pathogenic principles of protein aggregation diseases based on immunohistochemical and biochemical studies as well as observations in a mouse model for protein aggregation in the context of alcoholic and nonalcoholic steatohepatitis. The cellular defense mechanisms involved in protein quality control as well as the pathogenesis of protein aggregation diseases will be discussed.
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Alzheimer Disease - metabolism
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Amyloidosis - metabolism
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Animals - metabolism
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Brain - metabolism
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Chronic Disease - metabolism
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Disease Models, Animal - metabolism
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Fatty Liver, Alcoholic - metabolism
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Humans - metabolism
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Mice - metabolism
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Molecular Chaperones - chemistry
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Neurodegenerative Diseases - metabolism
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Parkinson Disease - metabolism
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Protein Conformation - metabolism
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Protein Folding - metabolism
- Find related publications in this database (Keywords)
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protein folding
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protein aggregation
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chaperones
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amyloid
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Steatohepatitis
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(non) alcoholic
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Mallory body
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p62
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keratin