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Alzheimer's disease peptide β-amyloid interacts with fibrinogen and induces its oligomerization
Hyung Jin Ahn, Daria Zamolodchikov, Marta Cortes-Canteli, Erin H. Norris, J. Fraser Glickman, Sidney Strickland and Anthony Cerami
Proceedings of the National Academy of Sciences of the United States of America
Vol. 107, No. 50 (December 14, 2010), pp. 21812-21817
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25756966
Page Count: 6
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Increasing evidence supports a vascular contribution to Alzheimer's disease (AD), but a direct connection between AD and the circulatory system has not been established. Previous work has shown that blood clots formed in the presence of the β-amyloid peptide (Aβ), which has been implicated in AD, have an abnormal structure and are resistant to degradation in vitro and in vivo. In the present study, we show that Aβ specifically interacts with fibrinogen with a K d of 26.3 ± 6.7 mM, that the binding site is located near the C terminus of the fibrinogen β-chain, and that the binding causes fibrinogen to oligomerize. These results suggest that the interaction between Aβ and fibrinogen modifies fibrinogen's structure, which may then lead to abnormal fibrin clot formation. Overall, our study indicates that the interaction between Aβ and fibrinogen may be an important contributor to the vascular abnormalities found in AD.
Proceedings of the National Academy of Sciences of the United States of America © 2010 National Academy of Sciences