TY - JOUR
T1 - The role of Aβ42 in Alzheimer's disease
AU - Younkin, Steven G.
PY - 1998
Y1 - 1998
N2 - Our recent studies of plasma, fibroblasts, transfected cells and transgenic mice show that a fundamental effect of the mutations linked to familial Alzheimer's disease (FAD) is to increase the extracellular concentration of Aβ42. This effect of the FAD-linked mutations is likely to be directly related to the pathogenesis of Alzheimer's disease (AD) because Aβ42 is deposited early and selectively in the senile plaques that are an invariant feature of all forms of AD. Thus our results provide strong evidence that the FAD-linked mutations all cause AD by increasing the extracellular concentration of Aβ42 (43), thereby fostering Aβ deposition, and they support the hypothesis that cerebral Aβ deposition is an essential early event in the pathogenesis of all forms of AD. Interactions between the basal forebrain cholinergic system and Aβ that could influence AD pathogenesis are discussed.
AB - Our recent studies of plasma, fibroblasts, transfected cells and transgenic mice show that a fundamental effect of the mutations linked to familial Alzheimer's disease (FAD) is to increase the extracellular concentration of Aβ42. This effect of the FAD-linked mutations is likely to be directly related to the pathogenesis of Alzheimer's disease (AD) because Aβ42 is deposited early and selectively in the senile plaques that are an invariant feature of all forms of AD. Thus our results provide strong evidence that the FAD-linked mutations all cause AD by increasing the extracellular concentration of Aβ42 (43), thereby fostering Aβ deposition, and they support the hypothesis that cerebral Aβ deposition is an essential early event in the pathogenesis of all forms of AD. Interactions between the basal forebrain cholinergic system and Aβ that could influence AD pathogenesis are discussed.
UR - http://www.scopus.com/inward/record.url?scp=0032105394&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032105394&partnerID=8YFLogxK
U2 - 10.1016/S0928-4257(98)80035-1
DO - 10.1016/S0928-4257(98)80035-1
M3 - Article
C2 - 9789825
AN - SCOPUS:0032105394
SN - 0928-4257
VL - 92
SP - 289
EP - 292
JO - Journal of Physiology Paris
JF - Journal of Physiology Paris
IS - 3-4
ER -