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Structure and function of amyloid in Alzheimer's disease |
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| Authors: | Morgan Carlos Colombres Marcela Nuñez Marco Tulio Inestrosa Nibaldo C |
| Affiliation: | aCentro 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 bLaboratorio de Bioinformática y Expresión Génica, Instituto de Nutrición y Tecnología de los Alimentos, Universidad de Chile, Chile cLaboratorio del Hierro y Biología del Envejecimiento, Departamento de Biología, Instituto Milenio CBB, Facultad de Ciencias, Universidad de Chile, Chile |
| Abstract: | 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. |
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