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New Biochemical Insights to Unravel the Pathogenesis of Alzheimer's Lesions

Published online by Cambridge University Press:  18 September 2015

Alex E. Roher*
Affiliation:
Department of Anatomy and Cell Biology, Oregon Health Sciences University, Portland
Kenneth C. Palmer
Affiliation:
Department of Pathology, Oregon Health Sciences University, Portland
John Capodilupo
Affiliation:
Department of Anatomy and Cell Biology, Oregon Health Sciences University, Portland
Arun R. Wakade
Affiliation:
Department of Pharmacology, Oregon Health Sciences University, Portland
Melvyn J. Ball
Affiliation:
Wayne State University School of Medicine, Detroi and Division of Neuropathology, Oregon Health Sciences University, Portland
*
Department of Anatomy and Cell Biology, Wayne State University School of Medicine, 540 E. Canfield Ave., Detroi, Michigan, U.S.A. 48201
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Abstract:

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Purification of amyloid plaque core proteins (APCP) from Alzheimer's disease brains to complete homogeneity and in high yield permitted its chemical fractionation and characterization of its components. APCP is mainly made of β-amyloid (βA) and an assortment of glycoproteins (accounting for 20%) rich in carbohydrates compatible with N-and O-linked saccharides. When added to tissue culture of sympathetic and sensory neurons APCP and βA inhibited neuritic sprouting, a reversible phenomenon at low doses. Higher concentrations of both substances kill the neurons in culture. APCP is significantly more toxic than βA, suggesting the minor components may play an important role in increasing the toxicity of βA. If the observed toxic effects of APCP in situ are occurring in vivo during the course of AD, then the accumulation of these extracellular proteins could be largely responsible for some of the neuronal death observed in this neuropathology.

Type
Research Article
Copyright
Copyright © Canadian Neurological Sciences Federation 1991

References

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