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SHR Neuro Krebs Kardio Lipid Stoffw 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 [OPEN ACCESS]
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Führende Autor*innen der Med Uni Graz
Aigelsreiter Ariane
Denk Helmut
Co-Autor*innen der Med Uni Graz
Janig Elke
Stumptner Cornelia
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.
Find related publications in this database (using NLM MeSH Indexing)
Alzheimer Disease - metabolism
Amyloidosis - metabolism
Animals - metabolism
Brain - metabolism
Chronic Disease - metabolism
Disease Models, Animal - metabolism
Fatty Liver, Alcoholic - metabolism
Humans - metabolism
Mice - metabolism
Molecular Chaperones - chemistry
Neurodegenerative Diseases - metabolism
Parkinson Disease - metabolism
Protein Conformation - metabolism
Protein Folding - metabolism

Find related publications in this database (Keywords)
protein folding
protein aggregation
chaperones
amyloid
Steatohepatitis
(non) alcoholic
Mallory body
p62
keratin
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