Transthyretin sequesters amyloid beta protein and prevents amyloid formation.

A. L. Schwarzman, Luisa Gregori, Michael P. Vitek, S Lyubski, Warren J. Strittmatter, J J Enghilde, R Bhasin, Judith M. Silverman, Karl H. Weisgraber, Patricia K. Coyle

Proceedings of the National Academy of Sciences · 1994 · 415 citations · 30 references

Concepts

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.

References

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