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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1994 Aug 30;91(18):8368–8372. doi: 10.1073/pnas.91.18.8368

Transthyretin sequesters amyloid beta protein and prevents amyloid formation.

A L Schwarzman 1, L Gregori 1, M P Vitek 1, S Lyubski 1, W J Strittmatter 1, J J Enghilde 1, R Bhasin 1, J Silverman 1, K H Weisgraber 1, P K Coyle 1, et al.
PMCID: PMC44607  PMID: 8078889

Abstract

The cardinal pathological features of Alzheimer disease are depositions of aggregated amyloid beta protein (A beta) in the brain and cerebrovasculature. However, the A beta is found in a soluble form in cerebrospinal fluid in healthy individuals and patients with Alzheimer disease. We postulate that sequestration of A beta precludes amyloid formation. Failure to sequester A beta in Alzheimer disease may result in amyloidosis. When we added A beta to cerebrospinal fluid of patients and controls it was rapidly sequestered into stable complexes with transthyretin. Complexes with apolipoprotein E, which has been shown to bind A beta in vitro, were not observed in cerebrospinal fluid. Additional in vitro studies showed that both purified transthyretin and apolipoprotein E prevent amyloid formation.

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Selected References

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