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  • 1
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; the proteinase inhibitor region of amyloid precursor proteins ; Lipofuscin ; Lysosome ; Amyloid β/A4 protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The immunohistochemical localization of the proteinase inhibitor region of amyloid protein precursors (APPI) in the postmortem human neocortex was studied using a polyclonal antibody raised against a purified recombinant human APPI derivative produced by COS-1 cells. APPI-like immunoreactivity (APPI-LI) was found diffusely in the human neocortex. APPI-LI appeared as irregularly shaped granular structures. The size of the APPI-LI structures was 1–4 μm in diameter. APPI-LI usually formed a cluster of 10- to 20-μm diameter in the cortical gray matter and 20- to 40-μm diameter in the subcortical white matter. Double staining for APPI and glial fibrillary acidic protein indicated that APPI-LI in the white matter and molecular layer was localized exclusively in the fibrillary astrocytes. In contrast, APPI-LI was found in neurons as well as in the fibrillary astrocytes in layers II through to VI. Under fluorescence microscopy, APPI-LI in both neurons and fibrillary astrocytes were found in close association with lipofuscin. The present observations indicate that APPI is localized in neurons and astrocytes in the human neocortex and that APPI may be associated with lipofuscin or lysosome in the human neocortex.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Hirano bodies ; Unit lamellae ; Alzheimer's disease ; Rapid-freeze, deep-etch and replica ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To clarify the yet controversial fine structure of Hirano bodies, we made three-dimensional observations of the tissues from the right hippocampus obtained at autopsy of elderly patients by the quick-freeze, deep-etch and replica method. The basic structure of Hirano bodies was a unit lamella, a closely attached pair of sheets composed of parallel-running smooth filaments, 10 to 12 nm in diameter with 12-nm interspaces. In the unit lamella, filaments from each of the overlapping sheets crossed obliquely at acute or obtuse angles to form lattice-like meshworks. The unit lamellae were arranged in a folded, waved or concentric manner, and connected or supported by cross-linking filaments of the same width. The distance between these unit lamellae was about 50 nm. Occasionally the sheets were separated or fused making layers of one to three sheets. At the periphery of the bodies parallel filaments were dispersed into individual filaments of similar size or directly attached to the cytoplasmic membrane.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Acetylcholinesterase ; Senile plaque ; β/A4 protein ; Amygdala ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To investigate the possible relationship between acetylcholinesterase (AChE)-containing fiber density and senile plaque density and between AChE-positive plaques and β/A4 protein deposition, AChE histochemistry, the modified Bielschowsky's method and β/A4 protein immunohistochemistry were performed on the amygdala of Alzheimer's disease (AD) and aged control cases. Abundant AChE-positive senile plaques were found in the amygdala and related structures in AD. These AChE-positive plaques were mainly of the primitive or diffuse type. In addition to senile plaques of typical morphologies a variety of AChE-positive structures were observed in the amygdala and related regions in AD. A comparison of serial sections stained alternatively with AChE histochemistry and β/A4 protein immunohistochemistry has revealed that these AChE-positive structures with variable morphological appearances displayed β/A4 protein immunoreactivity, indicating that AChE is localized in a variety of β/A4 protein deposition including the diffuse plaque. Thus, it is suggested that AChE is present in some senile plaques at the earliest stage. However, there was no apparent correlation between the numerical density of AChE-positive fibers and senile plaque density. These findings suggest that the degeneration of cholinergic neurons is not attributed to the occurrence of AChE activity in β/A4 protein.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0533
    Keywords: Clathrin ; Alzheimer's disease ; Tangle Senile plaque
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Clathrin, which constitutes coated vesicles, plays important roles in neuronal functions. In the brains of the patients with Alzheimer's disease, distribution of clathrin was immunohistochemically investigated using four monoclonal antibodies against clathrin light chains, LCB.1, LCB.2, X-16 and CON.1, to study the involvement of clathrin in the pathology of Alzheimer's disease. LCB.1, LCB.2, X-16, and CON.1 bind to the aminoterminus of the clathrin light chain b(LCb), to the neuron-specific insert of LCb, to the light chain a(LCa), and to LCa and LCb, respectively. In Alzheimer brains, granular staining of LCB.2 around neurons in the hippocampus was weaker or patchily defected in comparison with control brains. Some neurofibrillary tangles and neurons were intensely stained in Alzheimer brains by LCB.2, whereas neurons were weakly stained in control brains. Crowns of some senile plaques in the brains of early onset Alzheimer's disease were positively stained by LCB. 2. LCB. 1 supported the observations of LCB.2. Reactive astrocytes in Alzheimer brains were intensely stained by X-16. On the other hand, Western blot analysis using LCB.2 and X-16 demonstrated no apparent differences in protein amounts and molecular weights of LCa and LCb between control and Alzheimer brains. These observations demonstrated abnormal distribution of clathrin in Alzheimer brains, implying impairment of axonal transport in this disease.
    Type of Medium: Electronic Resource
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