An Etiological Role of Amyloidogenic Carboxyl‐Terminal Fragments of the β‐Amyloid Precursor Protein in Alzheimer's Disease

• Published in: Journal of neurochemistry Vol. 68; no. 5; pp. 1781 - 1791
• Main Author: Suh, Yoo‐Hun
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.05.1997; Blackwell
• Subjects: Alzheimer Disease - etiology; Alzheimer's disease; Amyloid - biosynthesis; Amyloid beta-Protein Precursor - metabolism; Amyloid beta-Protein Precursor - physiology; Amyloid precursor protein; Amyloid β protein; Animals; Biological and medical sciences; Carboxyl‐terminal peptide; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; Etiological role; Humans; Medical sciences; Neurology; Neurons - physiology; Peptide Fragments - metabolism; Peptide Fragments - physiology; C terminal-Sequence; Nervous system diseases; Alzheimer disease; Etiology; β Amyloid protein; Central nervous system disease; Degenerative disease; Review; Amyloid precursor protein; Cerebral disorder
• ISSN: 0022-3042; 1471-4159
• DOI: 10.1046/j.1471-4159.1997.68051781.x

: Amyloid β protein (Aβ), 39–43 amino acids long, is the principal constituent of the extracellular amyloid deposits in brain that are characteristic of Alzheimer's disease (AD). Several lines of evidence indicate that Aβ may play an important role in the pathogenesis of AD. However, there are several discrepancies between the production of Aβ and the development of the disease. Thus, Aβ may not be the sole active fragment of β‐amyloid precursor protein (βAPP) in the neurotoxicity associated with AD. Consequently, the possible effects of other cleaved products of βAPP need to be explored. The recent concentration on other potentially amyloidogenic products of βAPP has produced interesting candidates, the most promising of which are the amyloidogenic carboxyl‐terminal (CT) fragments of βAPP. This review discusses a possible etiological role of CT fragments of βAPP in AD.