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Science 18 April 2003:
Vol. 300. no. 5618, pp. 486 - 489
DOI: 10.1126/science.1079469
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Reports

Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

Rakez Kayed,1 Elizabeth Head,2 Jennifer L. Thompson,1 Theresa M. McIntire,3 Saskia C. Milton,1 Carl W. Cotman,2 Charles G. Glabe1*

Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Aß peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.

1 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697–3900, USA.
2 Institute for Brain Aging & Dementia, University of California, Irvine, CA 92697–4540, USA.
3 Department of Chemistry, University of California, Irvine, CA 92697–2025, USA.

* To whom correspondence should be addressed. E-mail: cglabe{at}uci.edu

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J. Neurosci. 26, 10536-10541
   Abstract »    Full Text »    PDF »
Neuroserpin Binds Abeta and Is a Neuroprotective Component of Amyloid Plaques in Alzheimer Disease.
K. J. Kinghorn, D. C. Crowther, L. K. Sharp, C. Nerelius, R. L. Davis, H. T. Chang, C. Green, D. C. Gubb, J. Johansson, and D. A. Lomas (2006)
J. Biol. Chem. 281, 29268-29277
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Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins.
N. Slepko, A. M. Bhattacharyya, G. R. Jackson, J. S. Steffan, J. L. Marsh, L. M. Thompson, and R. Wetzel (2006)
PNAS 103, 14367-14372
   Abstract »    Full Text »    PDF »
Calcitonin Forms Oligomeric Pore-Like Structures in Lipid Membranes.
M. Diociaiuti, L. Z. Polzi, L. Valvo, F. Malchiodi-Albedi, C. Bombelli, and M. C. Gaudiano (2006)
Biophys. J. 91, 2275-2281
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Cytocidal Actions of Parasporin-2, an Anti-tumor Crystal Toxin from Bacillus thuringiensis.
S. Kitada, Y. Abe, H. Shimada, Y. Kusaka, Y. Matsuo, H. Katayama, S. Okumura, T. Akao, E. Mizuki, O. Kuge, et al. (2006)
J. Biol. Chem. 281, 26350-26360
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Dynamics of yeast prion aggregates in single living cells..
S. Kawai-Noma, S. Ayano, C.-G. Pack, M. Kinjo, M. Yoshida, K. Yasuda, and H. Taguchi (2006)
Genes Cells 11, 1085-1096
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Toxicity of recombinant {beta}-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus.
R. Carrotta, M. Di Carlo, M. Manno, G. Montana, P. Picone, D. Romancino, and P. L. San Biagio (2006)
FASEB J 20, 1916-1917
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Distinct Early Folding and Aggregation Properties of Alzheimer Amyloid-beta Peptides Abeta40 and Abeta42: STABLE TRIMER OR TETRAMER FORMATION BY Abeta42.
Y.-R. Chen and C. G. Glabe (2006)
J. Biol. Chem. 281, 24414-24422
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Endoplasmic Reticulum Stress Associated with Extracellular Aggregates: EVIDENCE FROM TRANSTHYRETIN DEPOSITION IN FAMILIAL AM