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Cited by 119

The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.

Deposition of Monomeric, Not Oligomeric, Aβ Mediates Growth of Alzheimer's Disease Amyloid Plaques in Human Brain Preparations

Tseng, Bertrand P., Esler, William P., Clish, Clary B., Stimson, Evelyn R., Ghilardi, Joseph R., Vinters, Harry V., Mantyh, Patrick W., Lee, Jonathan P., Maggio, John E.·1999·Biochemistry
DOI 10.1021/bi990718v
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Abstract

Senile plaques composed of the peptide Abeta contribute to the pathogenesis of Alzheimer's disease (AD), and mechanisms underlying their formation and growth may be exploitable as therapeutic targets. To examine the process of amyloid plaque growth in human brain, we have utilized size exclusion chromatography (SEC), translational diffusion measured by NMR, and in vitro models of Abeta amyloid growth to identify the oligomerization state of Abeta that is competent to add onto an existing amyloid deposit. SEC of radiolabeled and unlabeled Abeta over a concentration range of 10(-)(10)-10(-)(4) M demonstrated that the freshly dissolved peptide eluted as a single low molecular weight species, consistent with monomer or dimer. This low molecular weight Abeta species isolated by SEC was competent to deposit onto preexisting amyloid in preparations of AD cortex, with first-order kinetic dependence on soluble Abeta concentration, establishing that solution-phase oligomerization is not rate limiting. Translational diffusion measurements of the low molecular weight Abeta fraction demonstrate that the form of the peptide active in plaque deposition is a monomer. In deliberately aged (>6 weeks) Abeta solutions, a high molecular weight (>100 000 M(r)) species was detectable in the SEC column void. In contrast to the active monomer, assembled Abeta isolated from the column showed little or no focal association with AD tissue. These studies establish that, at least in vitro, Abeta exists as…

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Crossref · 10.1021/bi990718v

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16 of 16 references verified0 citation errors · 0 not checkable

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Citations

Cites

Show all 16 references

Research works printed but not linked: 52

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  52. Abbreviations Aβ, human β-amyloid peptide

Cited by

Metadata

Authors
Tseng, B. P., Esler, W. P., Clish, C. B., Stimson, E. R., Ghilardi, J. R., Vinters, H. V., Mantyh, P. W., Lee, J. P., & Maggio, J. E.
Affiliations
Department of Biological Chemistry & Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, Molecular Neurobiology Laboratory, Department of Preventive Sciences, University of Minnesota Dental School, Minneapolis, Minnesota 55417, Department of Chemistry, Boston University, Boston, Massachusetts 02215, and Department of Pathology & Laboratory Medicine (Neuropathology) and Brain Research Institute, University of California, Los Angeles Medical Center, Los Angeles, California 90095
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1999-07-27
Volume
38
Issue
32
Pages
10424-10431
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi990718v
Cited by
119
References
16
Language
en

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