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  • 1
    ISSN: 1432-0533
    Keywords: Alzheimer-type dementia ; Senile plaques ; Amyloid β/A4 protein ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We compared the ultrastructure between diffuse and primitive plaques in the brains of senile dementia, using pairs of routine electron microscopic ultrathin sections and adjacent semithin sections, which were immunolabeled for β protein. In the frontal cortex, amyloid fibrils were rarely seen in a minority of diffuse plaques, suggesting an initial stage of the diffuse plaques. A majority of the diffuse plaques had electrondense material and/or amyloid fibrils between cell processes in part of but not the entire β/A4-immunoreactive areas. Small degenerating neurites were often seen with apparent amyloid fibrils in the diffuse plaques, and these were considered to be in an advanced stage. The size and number of degenerating neurites were proportional to the amount of amyloid. Bundles of amyloid fibrils were occasionally surrounded by astroglial processes forming gap junctions. Neurons were found within some diffuse plaques, but capillaries were rarely seen. In contrast, in the temporal cortex, the diffuse plaques were smaller, and even these small ones had apparent amyloid fibrils. The amount of amyloid correlated significantly with plaque size in the temporal cortices, but not in the frontal cortices. Most of the diffuse plaques of the frontal lobe remained as advanced diffuse plaques (apparent amyloid with occasional astroglia and some degenerating neurites) for a long time, and did not transformed into primitive plaques, whereas the temporal diffuse plaques tended to transform into primitive plaques.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Senile plaques ; Methenamine silver stain ; Alzheimer-type dementia ; Down's syndrome ; Amyloid β protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have developed a new methenamine silver (MS) stain for detecting diffuse plaques distinctively on paraffin-embedded tissue sections of Alzheimer-type dementia, Down'n syndrome, and mentally normal aged brains. This rapid and easy method selectively labels amyloid-related component of senile plaques, but not of kuru plaques found in Gerstmann-Sträussler syndrome. Our MS stain shows almost the same staining pattern as that of the β protein immunostaining with formic acid pretreatment. Therefore, new MS stain is appropriate to routine or screening studies for senile plaques including diffuse plaques.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Neuropil threads ; Alzheimer-type dementia ; tau protein ; Palred helical filaments ; Senile plaques
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Thread-like structures immunoreactive with paired helical filaments and tau antisera were demonstrated as mesh-works in the neocortices of five brains with Alzheimer-type dementia, but not in those of five normal aged control brains. The ultrastructure of the threads was examined using paired routine electron microscopic ultrathin sections and adjacent 0.4-μm-thick semithin sections, immunostained for β protein. Outside the β protein-positive senile plaques, neuropil threads appeared sporadically as small slender neurites, containing either regularly constricted or straight filaments. These neurites often showed dendritic profiles. Similar threads were also seen within the senile plaques. The threads were accumulated in amyloid fibril-rich primitive plaques, but not in amyloid fibril-poor diffuse plaques. The presence of these threads was closely associated with neurofibrillary tangle formation. Our findings suggest that wide-spread change of the neuropil neurites, neuropil threads or curly fibers, both outside and inside of the senile plaques are dendritic in origin and play an important role in the clinical manifestation of dementia.
    Type of Medium: Electronic Resource
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