Transthyretin sequesters amyloid β protein and prevents amyloid formation. Schwarzman, A., Gregori, L., Vitek, M., Lyubski, S., Strittmatter, W., Enghilde, J., Bhasin, R., Silverman, J., Weisgraber, K., Coyle, P., Zagorski, M., Talafous, J., Eisenberg, M., Saunders, A., Roses, A., & Goldgaber, D. Proceedings of the National Academy of Sciences of the United States of America, 91(18):8368-8372, National Academy of Sciences, 1994. cited By 290![Transthyretin sequesters amyloid β protein and prevents amyloid formation [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The cardinal pathological features of Alzheimer disease are depositions of aggregated amyloid β protein (Aβ) in the brain and cerebrovasculature. However, the Aβ is found in a soluble form in cerebrospinal fluid in healthy individuals and patients with Alzheimer disease. We postulate that sequestration of Aβ precludes amyloid formation. Failure to sequester Aβ in Alzheimer disease may result in amyloidosis. When we added Aβ 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 Aβ in vitro, were not observed in cerebrospinal fluid. Additional in vitro studies showed that both purified transthyretin and apolipoprotein E prevent amyloid formation.
@ARTICLE{Schwarzman19948368,
author={Schwarzman, A.L. and Gregori, L. and Vitek, M.P. and Lyubski, S. and Strittmatter, W.J. and Enghilde, J.J. and Bhasin, R. and Silverman, J. and Weisgraber, K.H. and Coyle, P.K. and Zagorski, M.G. and Talafous, J. and Eisenberg, M. and Saunders, A.M. and Roses, A.D. and Goldgaber, D.},
title={Transthyretin sequesters amyloid β protein and prevents amyloid formation},
journal={Proceedings of the National Academy of Sciences of the United States of America},
year={1994},
volume={91},
number={18},
pages={8368-8372},
doi={10.1073/pnas.91.18.8368},
note={cited By 290},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027999030&doi=10.1073%2fpnas.91.18.8368&partnerID=40&md5=d600d8db8de320883e0a4aea9f18ab74},
affiliation={Department of Psychiatry, School of Medicine, State Univ. New York at Stony Brook, Stony Brook, NY 11794, United States; Department of Pathology, School of Medicine, State Univ. New York at Stony Brook, Stony Brook, NY 11794, United States; Department of Neurology, School of Medicine, State Univ. New York at Stony Brook, Stony Brook, NY 11794, United States; Department of Pharmacology, School of Medicine, State Univ. New York at Stony Brook, Stony Brook, NY 11794, United States; Picower Inst. for Medical Research, Manhasset, NY 11030, United States; Department of Medicine (Neurology), Joseph Kathleen Bryan Alzheimer's R., Durham, NC 27710, United States; Department of Pathology, Duke University Medical Center, Durham, NC 27710, United States; Department of Pathology, J. David Gladstone Inst. C., University of California, San Francisco, CA 94110, United States; Department of Chemistry, Case Western Reserve University, Cleveland, OH 44106, United States},
abstract={The cardinal pathological features of Alzheimer disease are depositions of aggregated amyloid β protein (Aβ) in the brain and cerebrovasculature. However, the Aβ is found in a soluble form in cerebrospinal fluid in healthy individuals and patients with Alzheimer disease. We postulate that sequestration of Aβ precludes amyloid formation. Failure to sequester Aβ in Alzheimer disease may result in amyloidosis. When we added Aβ 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 Aβ in vitro, were not observed in cerebrospinal fluid. Additional in vitro studies showed that both purified transthyretin and apolipoprotein E prevent amyloid formation.},
author_keywords={sequestration},
correspondence_address1={Goldgaber, D.; Department of Psychiatry, School of Medicine, State University of New York, Stony Brook, NY 11794, United States},
publisher={National Academy of Sciences},
issn={00278424},
coden={PNASA},
pubmed_id={8078889},
language={English},
abbrev_source_title={PROC. NATL. ACAD. SCI. U. S. A.},
document_type={Article},
source={Scopus},
}
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