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  Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation

Haapasalo, A., Viswanathan, J., Bertram, L., Soininen, H., Tanzi, R. E., & Hiltunen, M. (2010). Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation. Biochemical Society Transactions, 38, 150-155. doi:10.1042/BST0380150.

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Genre: Journal Article
Alternative Title : Biochem Soc Trans

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 Creators:
Haapasalo, A., Author
Viswanathan, J., Author
Bertram, L.1, Author           
Soininen, H., Author
Tanzi, R. E., Author
Hiltunen, M., Author
Affiliations:
1Neuropsychiatric Genetics (Lars Bertram), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479655              

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Free keywords: Alzheimer Disease/metabolism/pathology; Amyloid beta-Peptides/metabolism; Carrier Proteins/chemistry/genetics/metabolism; Cell Cycle Proteins/chemistry/genetics/metabolism; Endoplasmic Reticulum/metabolism; Humans; Inclusion Bodies/metabolism; Oxidative Stress; Presenilins/metabolism; Proteasome Endopeptidase Complex/metabolism; Protein Conformation; Protein Folding
 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.

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Language(s): eng - English
 Dates: 2010-02
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 554590
DOI: 10.1042/BST0380150
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Title: Biochemical Society Transactions
  Alternative Title : Biochem Soc Trans
Source Genre: Journal
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Pages: - Volume / Issue: 38 Sequence Number: - Start / End Page: 150 - 155 Identifier: ISSN: 1470-8752 (Electronic)