Work

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

Year: 2010

Type: review

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.

Source: Biochemical Society Transactions

DOI: 10.1042/bst0380150

Authors: Annakaisa Haapasalo, Jayashree Viswanathan, Lars Bertram, Hilkka Soininen, Rudolph E. Tanzi, Mikko Hiltunen

Institutions: Kuopio University Hospital, Harvard University, Massachusetts General Hospital, Max Planck Institute for Molecular Genetics

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Physiology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funder: Kuopion Yliopistollinen Sairaala