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(Received for publication, April 29, 1996, and in revised form, June 10, 1996)
From the In the course of analyzing the chemical
composition of Alzheimer's disease neuritic and vascular amyloid, we
have purified stable dimeric and trimeric components of A
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20631-20635
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-(1-42) Dimer Derived from
Neuritic and Vascular Amyloid Deposits of Alzheimer's Disease
,
,
,
,
,
,
,
,
Haldeman Laboratory for Alzheimer's Disease
Research, Sun Health Research Institute, Sun City, Arizona 85372,
¶ Biotechnology Core, Eli Lilly Research Laboratories,
Indianapolis, Indiana 46285, the 
Department of Cellular and
Microscopic Research, Abbott Laboratories, Abbott Park,
Illinois 60064, the '' Alzheimer's Disease Research Center, Department
of Neurology, Baylor College of Medicine, Houston, Texas 77030, the
Department of Pharmacology and Molecular
Sciences, The Johns Hopkins University School of Medicine, Baltimore,
Maryland 21205, the Department of Molecular
Pharmacology and Biological Sciences, Northwestern University Medical
School, Chicago, Illinois 60611, the # Department of
Zoology, Arizona State University, Tempe, Arizona 85287, and the
Parke Davis Co., Ann Arbor, Michigan 48106
peptides.
These peptides (molecular mass 9.0 and 13.5 kDa) were separated by size
exclusion chromatography in the presence of 80% formic acid or 5 M guanidine thiocyanate, pH 7.4. The average ratio of
monomers, dimers, and trimers was 55:30:15, respectively. Similar
structures were produced over time upon incubation of synthetic
A-(1-42) at pH 7.4. The stability of these oligomeric forms was
also demonstrated by Western blot and mass spectrometry. Atomic force
microscopy and electron microscopy rotary shadowing revealed that the
monomers polymerized into 8-10-nm filaments, whereas the dimers
generated prolate ellipsoids measuring 3-4 nm in diameter. The
pathogenic effects of the dimeric A-(1-40/42) were tested in
cultures of rat hippocampal neuron glia cells. Only in the presence of
microglia did the dimer elicit neuronal killing. It is possible that
these potentially pathogenic A-(1-40/42) dimers and trimers from
Alzheimer's disease amyloid represent the soluble oligomers of A
recently described in Alzheimer's disease brains (Kuo, Y.-M.,
Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick,
J. B., Murdoch, G. H., Ball, M. J., and Roher, A. E. (1996)
J. Biol. Chem., 271, 4077-4081).
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