IRMA-International.org: Creator of Knowledge
Information Resources Management Association
Advancing the Concepts & Practices of Information Resources Management in Modern Organizations

Aß Monomer, Oligomer and Fibril in Alzheimer's Disease

Aß Monomer, Oligomer and Fibril in Alzheimer's Disease
View Sample PDF
Author(s): Hiroshi Mori (Department of Neuroscience, Osaka City University Medical School, Japan)
Copyright: 2011
Pages: 7
Source title: Early Detection and Rehabilitation Technologies for Dementia: Neuroscience and Biomedical Applications
Source Author(s)/Editor(s): Jinglong Wu (Okayama University, Japan)
DOI: 10.4018/978-1-60960-559-9.ch016

Purchase

View Aß Monomer, Oligomer and Fibril in Alzheimer's Disease on the publisher's website for pricing and purchasing information.

Abstract

Alzheimer’s disease (AD), the most prevalent disease of aged people, is a progressive neurodegenerative disorder with dementia. Amyloid-ß (also known as ß-protein and referred to here as Aß) is a well-established, seminal peptide in AD that is produced from the amyloid precursor protein (APP) by consecutive digestion with the ß secretase of BACE (beta-site amyloid cleaving enzyme) and gamma secretase of the presenilin complex. Abnormal cerebral accumulation of Abeta in the form of insoluble fibrils in senile plaques and cerebral amyloid angiopathy (CAA) is a neuropathological hallmark of AD. In contrast to insoluble fibrillary Aß, a soluble oligomeric complex, ADDL, consists of low-n oligomers of Aß, such as Aß*56. Despite their different names, it is currently proposed that oligomeric Aß is directly involved in synaptic toxicity and cognitive dysfunction in the early stages of AD. This chapter identifies a novel APP mutation (E693delta; referred to as the Osaka mutation) in a pedigree with probable AD, resulting in a variant Aß lacking glutamate at position 22. Based on theoretical predictions and in vitro studies on synthetic mutant Aß peptides, the mutated Aß peptide showed a unique and enhanced oligomerization activity without fibrillization. This was further confirmed by PiB-PET analysis on the proband patient. Collectively, the chapter concludes that the Osaka mutation is the first human evidence for the hypothesis that oligomeric Aß is involved in AD.

Related Content

David Edson Ribeiro, Valter Augusto de Freitas Barbosa, Clarisse Lins de Lima, Ricardo Emmanuel de Souza, Wellington Pinheiro dos Santos. © 2021. 15 pages.
Juliana Carneiro Gomes, Maíra Araújo de Santana, Clarisse Lins de Lima, Ricardo Emmanuel de Souza, Wellington Pinheiro dos Santos. © 2021. 12 pages.
Maíra Araújo de Santana, Jessiane Mônica Silva Pereira, Clarisse Lins de Lima, Maria Beatriz Jacinto de Almeida, José Filipe Silva de Andrade, Thifany Ketuli Silva de Souza, Rita de Cássia Fernandes de Lima, Wellington Pinheiro dos Santos. © 2021. 19 pages.
Jessiane Mônica Silva Pereira, Maíra Araújo de Santana, Clarisse Lins de Lima, Rita de Cássia Fernandes de Lima, Sidney Marlon Lopes de Lima, Wellington Pinheiro dos Santos. © 2021. 25 pages.
Adriel dos Santos Araujo, Roger Resmini, Maira Beatriz Hernandez Moran, Milena Henriques de Sousa Issa, Aura Conci. © 2021. 35 pages.
Abir Baâzaoui, Walid Barhoumi. © 2021. 21 pages.
Marcus Costa de Araújo, Luciete Alves Bezerra, Kamila Fernanda Ferreira da Cunha Queiroz, Nadja A. Espíndola, Ladjane Coelho dos Santos, Francisco George S. Santos, Rita de Cássia Fernandes de Lima. © 2021. 44 pages.
Body Bottom