Ultrastructural heterogeneity in cerebral amyloid of Alzheimer's disease

Cerebral amyloid deposits from five patients with presenile or senile cerebral disease of the Alzheimer type were stained with uranyl acetate and lead citrate or with periodic acid-thiocarbohydrazide-silver proteinate, and examined with traditional high-resolution electron microscopy and with a goni...

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Bibliographic Details
Published inActa neuropathologica Vol. 76; no. 6; p. 613
Main Authors Powers, J M, Skeen, J T
Format Journal Article
LanguageEnglish
Published Germany 01.01.1988
Subjects
Aged
Alzheimer Disease - pathology
Amyloid - ultrastructure
Biopsy
Cerebral Cortex - pathology
Extracellular Matrix - pathology
Female
Hippocampus - pathology
Humans
Male
Microscopy, Electron
Middle Aged
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Summary:Cerebral amyloid deposits from five patients with presenile or senile cerebral disease of the Alzheimer type were stained with uranyl acetate and lead citrate or with periodic acid-thiocarbohydrazide-silver proteinate, and examined with traditional high-resolution electron microscopy and with a goniometer tilting stage. In addition to a carbohydrate-rich matrix, we also consistently found local cell-derived vesicles within plaque and dyshoric amyloid. The most likely source for these vesicles appeared to be degenerate neurites. Amyloid fibrils were intimately associated with plasmalemmata, particularly those of degenerate neurites, which supported a neuronal origin for the amyloid fibril of Alzheimer's disease.
ISSN:0001-6322
DOI:10.1007/BF00689601