Abstract:
:Abnormal protein aggregation and intracellular or extracellular accumulation of misfolded and aggregated proteins are key events in the pathogenesis of different neurodegenerative diseases. Furthermore, endoplasmic reticulum stress and impairment of the ubiquitin-proteasome system probably contribute to neurodegeneration in these diseases. A characteristic feature of AD (Alzheimer's disease) is the abnormal accumulation of Abeta (amyloid beta-peptide) in the brain. Evidence shows that the AD-associated PS (presenilin) also forms aggregates under certain conditions and that another AD-associated protein, ubiquilin-1, controls protein aggregation and deposition of aggregated proteins. Here, we review the current knowledge of ubiquilin-1 and PS in protein aggregation and related events that potentially influence neurodegeneration.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Haapasalo A,Viswanathan J,Bertram L,Soininen H,Tanzi RE,Hiltunen Mdoi
10.1042/BST0380150subject
Has Abstractpub_date
2010-02-01 00:00:00pages
150-5issue
Pt 1eissn
0300-5127issn
1470-8752pii
BST0380150journal_volume
38pub_type
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