Author: ["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"]
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Abstract
To determine whether the presenilin 1 (PS1), presenilin 2 (PS2) and amyloid β-protein precursor (APP) mutations linked to familial Alzheimer's disease (FAD) increase the extracellular concentration of amyloid β–protein (Aβ) ending at Aβ42(43) in vivo, we performed a blinded comparison of plasma Aβ levels in carriers of these mutations and controls. Aβ1 –42(43) was elevated in plasma from subjects with FAD–linked PS1 (P < 0.0001), PS2N141I (P = 0.009), APPK670N,M671L (P < 0.0001), and APPV717I (one subject) mutations. Aβ ending at Aβ42(43) was also significantly elevated in fibroblast media from subjects with PS1 (P < 0.0001) or P52 (P = 0.03) mutations. These findings indicate that the FAD–linked mutations may all cause Alzheimer's disease by increasing the extracellular concentration of Aβ42(43), thereby fostering cerebral deposition of this highly amyloidogenic peptide.Cite this article
Scheuner, D., Eckman, C., Jensen, M. et al. Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 2, 864–870 (1996). https://doi.org/10.1038/nm0896-864 