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Cited by 319

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Senile plaque neurites in Alzheimer disease accumulate amyloid precursor protein.

Open access
Cras, P, Kawai, M, Lowery, D, Gonzalez-DeWhitt, P, Greenberg, B, Perry, G·1991·Proceedings of the National Academy of Sciences

Abstract

Senile plaques are polymorphous beta-amyloid protein deposits found in the brain in Alzheimer disease and normal aging. This beta-amyloid protein is derived from a larger precursor molecule of which neurons are the principal producers in brain. We found that amyloid precursor protein (APP)-immunoreactive neurites were involved in senile plaques and that only a subset of these neurites showed markers for the abnormal filaments characteristic of neurofibrillary pathology. In the neocortex of nondemented individuals with senile plaques but spared of neurofibrillary pathology, dystrophic neurites in senile plaques showed only APP accumulation. In contrast, in the brains of Alzheimer patients, virtually all APP-immunoreactive neurites also showed immunoreactivity with ubiquitin, tau, and phosphorylated neurofilaments. The presence of tau and neurofilament epitopes in dystrophic neurites in senile plaques was correlated with the extent of neurofibrillary pathology in the surrounding brain tissue. Accumulation of APP and the formation of neurofibrillary pathology in senile plaque neurites are therefore distinct phenomena. Our findings suggest that APP accumulation in senile plaque neurites occurs prior to tau accumulation and is therefore more closely related to appearance of neuritic dystrophy.

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Crossref · 10.1073/pnas.88.17.7552

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Metadata

Authors
Cras, P., Kawai, M., Lowery, D., Gonzalez-DeWhitt, P., Greenberg, B., & Perry, G.
Venue
Proceedings of the National Academy of Sciences
Published
1991-09
Volume
88
Issue
17
Pages
7552-7556
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1976357608
Cited by
319
References
6
FWCI
7.02
Type
journal article
Language
en
Open access
green

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