title: Ultrastructural heterogeneity in cerebral amyloid of Alzheimer's disease.
abstract: 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.
authors.affiliation: Department of Pathology, Medical University of South Carolina, Charleston 29425.
authors.forename: J M
authors.initials: JM
authors.lastname: Powers
authors.forename: J T
authors.initials: JT
authors.lastname: Skeen
mesh_terms: D000368:Aged; D000544:Alzheimer Disease / Q000473:pathology*; D000682:Amyloid / Q000648:ultrastructure*; D001706:Biopsy; D002540:Cerebral Cortex / Q000473:pathology*; D005109:Extracellular Matrix / Q000473:pathology; D005260:Female; D006624:Hippocampus / Q000473:pathology*; D006801:Humans; D008297:Male; D008854:Microscopy, Electron; D008875:Middle Aged
chemical_list: D000682:Amyloid