Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-08

AUTHORS

D. Scheuner, C. Eckman, M. Jensen, X. Song, M. Citron, N. Suzuki, T.D. Bird, J. Hardy, M. Hutton, W. Kukull, E. Larson, L. Levy-Lahad, M. Viitanen, E. Peskind, P. Poorkaj, G. Schellenberg, R. Tanzi, W. Wasco, L. Lannfelt, D. Selkoe, S. Younkin

ABSTRACT

To determine whether the presenilin 1 (PS1), presenilin 2 (PS2) and amyloid beta-protein precursor (APP) mutations linked to familial Alzheimer's disease (FAD) increase the extracellular concentration of amyloid beta-protein (A beta) ending at A beta 42(43) in vivo, we performed a blinded comparison of plasma A beta levels in carriers of these mutations and controls. A beta 1-42(43) was elevated in plasma from subjects with FAD-linked PS1 (P < 0.0001), PS2N1411 (P = 0.009), APPK670N,M671L (P < 0.0001), and APPV7171 (one subject) mutations. A beta ending at A beta 42(43) was also significantly elevated in fibroblast media from subjects with PS1 (P < 0.0001) or PS2 (P = 0.03) mutations. These findings indicate that the FAD-linked mutations may all cause Alzhelmer's disease by increasing the extracellular concentration of A beta 42(43), thereby fostering cerebral deposition of this highly amyloidogenic peptide. More... »

PAGES

864

Journal

TITLE

Nature Medicine

ISSUE

8

VOLUME

2

From Grant

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nm0896-864

    DOI

    http://dx.doi.org/10.1038/nm0896-864

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1028210081

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8705854


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