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An Etiological Role of Amyloidogenic Carboxyl‐Terminal Fragments of the β‐Amyloid Precursor Protein in Alzheimer's Disease
Author(s) -
Suh YooHun
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.68051781.x
Subject(s) - amyloid precursor protein , neurotoxicity , pathogenesis , p3 peptide , amyloid (mycology) , extracellular , amyloid β , chemistry , alzheimer's disease , disease , biochemistry , biochemistry of alzheimer's disease , senile plaques , amyloid precursor protein secretase , medicine , pathology , toxicity , inorganic chemistry , organic chemistry
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.