Structure and function of amyloid in Alzheimer's disease.
This review is focused on the structure and function of Alzheimer's amyloid deposits. Amyloid formation is a process in which normal well-folded cellular proteins undergo a self-assembly process that leads to the formation of large and ordered protein structures. Amyloid deposition, oligomerization, and higher order polymerization, and the structure adopted by these assemblies, as well as their functional relationship with cell biology are underscored. Numerous efforts have been directed to elucidate these issues and their relation with senile dementia. Significant advances made in the last decade in amyloid structure, dynamics and cell biology are summarized and discussed. The mechanism of amyloid neurotoxicity is discussed with emphasis on the Wnt signaling pathway. This review is focused on Alzheimer's amyloid fibrils in general and has been divided into two parts dealing with the structure and function of amyloid.
Morgan
Carlos
C
Centro FONDAP de Regulación Celular y Patología Joaquín V. Luco, MIFAB, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, P.O. Box 114-D, Santiago, Chile.
Colombres
Marcela
M
Nuñez
Marco Tulio
MT
Inestrosa
Nibaldo C
NC
D000544:Alzheimer Disease / Q000378:metabolism* / Q000503:physiopathology; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000633:toxicity; D000818:Animals; D017209:Apoptosis / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D009336:Necrosis / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000633:toxicity; D058225:Plaque, Amyloid / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
D000682:Amyloid; D010446:Peptide Fragments