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The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain

Walsh, Dominic M., Tseng, Bertrand P., Rydel, Russell E., Podlisny, Marcia B., Selkoe, Dennis J.·2000·Biochemistry
DOI 10.1021/bi001048s
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Abstract

The progressive aggregation and deposition of amyloid beta-protein (Abeta) in brain regions subserving memory and cognition is an early and invariant feature of Alzheimer's disease, the most common cause of cognitive failure in aged humans. Inhibiting Abeta aggregation is therapeutically attractive because this process is believed to be an exclusively pathological event. Whereas many studies have examined the aggregation of synthetic Abeta peptides under nonphysiological conditions and concentrations, we have detected and characterized the oligomerization of naturally secreted Abeta at nanomolar levels in cultures of APP-expressing CHO cells [Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydell, R. E., Teplow, D. B., and Selkoe, D. J. (1995) J. Biol. Chem. 270, 9564-9570 (1); Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B., and Selkoe, D. J. (1998) Biochemistry 37, 3602-3611 (2)]. To determine whether similar species occur in vivo, we probed samples of human cerebrospinal fluid (CSF) and detected SDS-stable dimers of Abeta in some subjects. Incubation of CSF or of CHO conditioned medium at 37 degrees C did not lead to new oligomer formation. This inability to induce oligomers extracellularly as well as the detection of oligomers in cell medium very early during the course of pulse-chase experiments suggested that natural Abeta oligomers might first form intracellularly. We therefore searched for…

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  • The amyloid cascade hypothesis predicts that a gradual increase of Aβ-(1-42) levels in brain interstitial fluid may lead to Aβ oligomerization and eventually to Aβ fibrillization.

    “The amyloid cascade hypothesis predicts that a gradual increase of A␤-(1-42) levels in brain interstitial fluid (3,4) may lead to A␤ oligomerization and eventually to A␤ fibrillization (5).”

    From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [4]

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Metadata

Authors
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J.
Affiliations
Department of Neurology and Program in Neuroscience, Harvard Medical School and Center for Neurologic Diseases, Brigham and Women's Hospital, Boston, Massachusetts 02115, and Elan Pharmaceuticals, Inc., 800 Gateway Boulevard, San Francisco, California 94080
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2000-08-11
Volume
39
Issue
35
Pages
10831-10839
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi001048s
Cited by
401
References
4
Language
en

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