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American Journal of Pathology, Vol 139, 1245-1250, Copyright © 1991 by American Society for Investigative Pathology
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T Ohgami, T Kitamoto, A Weidmann, K Beyreuther and J Tateishi
Department of Neuropathology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
To clarify the relationship between amyloid formation and amyloid precursor protein (APP), the brain sections from eight patients with Alzheimer's disease (AD) and four with Gerstmann-Straussler Syndrome (GSS) were investigated immunohistochemically by the double- immunostaining method. In AD, most APP-positive senile plaques belong to classical plaques or primitive plaques, whereas in diffuse plaques, APP-positive neuritic components are rarely observed. The authors documented that anti-APP-labeled degenerative neurites surrounding kuru plaques in all four GSS patients. These kuru plaques were verified by double immunostaining using anti-prion protein and anti-APP. The APP- positive structures in kuru plaques were almost identical with those seen in the classical plaques in AD. The authors concluded that APP- positive degenerative neurites are not an early event in the amyloid formation of senile plaques. It is therefore postulated that depositions of beta/A4 and prion proteins are primary events that may involve the surrounding microenvironment and result in the secondary formation of APP-positive degenerative neurites, not specific to AD.
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