Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging.

Jan Näslund(Karolinska Institutet), Angelika Schierhorn(NewYork–Presbyterian Hospital), Ulf Hellman(NewYork–Presbyterian Hospital), Lars Lannfelt(Karolinska Institutet), A.D. Roses(Karolinska Institutet), Lars O. Tjernberg(NewYork–Presbyterian Hospital), Jerzy Silberring(NewYork–Presbyterian Hospital), Sam Gandy(Karolinska Institutet), Bengt Winblad(Karolinska Institutet), Paul Greengard(Karolinska Institutet)
Proceedings of the National Academy of Sciences
August 30, 1994
Cited by 471Open Access

Abstract

The Alzheimer A beta amyloid peptide (A beta) is the principal proteinaceous component of amyloid associated with Alzheimer disease (AD). We have determined the relative abundance of A beta structural variants present in amyloid from brains of 10 individuals with sporadic AD, 2 individuals with familial AD carrying specific mutations in the Alzheimer amyloid precursor protein gene, and 5 nondemented elderly controls. A procedure of isolation based on the extreme insolubility of A beta amyloid was used. The purified, nondigested A beta was analyzed by N-terminal sequencing and electrospray-ionization mass spectrometry. Three principal A beta variants were detected--A beta-(1-40), A beta-(1-42), and A beta-(11-42)--in all brains analyzed. The predominant variant in sporadic AD was A beta-(1-40), whereas the principal A beta variant in nondemented elderly controls was A beta-(1-42). The ratio A beta-(1-40)/A beta-(1-42) differed by 10-fold between brains from nondemented controls and those with sporadic AD.


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