Open AccessAβ aggregation and possible implications in Alzheimer's disease pathogenesis
Author(s) -
Bharadwaj Prashant R.,
Dubey Ashok K.,
Masters Colin L.,
Martins Ralph N.,
Macreadie Ian G.
Publication year - 2009
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2009.00609.x
Subject(s) - pathogenesis , extracellular , disease , amyloid (mycology) , toxicity , protein aggregation , neuroscience , alzheimer's disease , amyloid beta , biology , microbiology and biotechnology , immunology , medicine , pathology , botany
• Introduction • Amyloid Structure • Mechanism of Amyloid aggregation • Aβ: a natively unfolded protein? • Ambiguities in synthetic Ab studies • Formation of Amyloid plaques • Role of Ab in AD Pathogenesis • ConclusionAbstract Amyloid β protein (Aβ) has been associated with Alzheimer's disease (AD) because it is a major component of the extracellular plaque found in AD brains. Increased Aβ levels correlate with the cognitive decline observed in AD. Sporadic AD cases are thought to be chiefly associated with lack of Aβ clearance from the brain, unlike familial AD which shows increased Aβ production. Aβ aggregation leading to deposition is an essential event in AD. However, the factors involved in Aβ aggregation and accumulation in sporadic AD have not been completely characterized. This review summarizes studies that have examined the factors that affect Aβ aggregation and toxicity. By necessity these are studies that are performed with recombinant‐derived or chemically synthesized Aβ. The studies therefore are not done in animals but in cell culture, which includes neuronal cells, other mammalian cells and, in some cases, non‐mammalian cells that also appear susceptible to Aβ toxicity. An understanding of Aβ oligomerization may lead to better strategies to prevent AD.