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  • 1
    ISSN: 1432-0533
    Keywords: Axonal damage ; Cerebellar focal lesions ; Human Purkinje cell ; Torpedoes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cerebellar torpedoes, unique fusiform swellings of Purkinje cell axons within the granular layer, have been known to occur sparsely associated with diffuse cerebellar changes. This report describes, in three human autopsy cases with focal necrotic lesions in the cerebellar white matter, torpedoes which were essentially confined to the cerebellar cortex overlying the lesions. Purkinje cells in the same region showed no recognizable change, but were obviously decreased in number. The location of the necrotic lesions was such that they may well have severed Purkinje cell axons projecting into the deeply located cerebellar nuclei from the torpedo-carrying cortex. These findings indicate that damage to Purkinje cell axons, even if it occurs far away from the cell bodies, may have a critical influence upon the metabolism of Purkinje cells and play an important role in the formation of torpedoes.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Astrocytes ; Electron microscopy ; Immunohistochemistry ; Paired helical filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A 54-year-old man who had cerebellar ataxia and pseudobulbar palsy at the age of 29 years, and soon developed dementia, myoclonus and convulsions, died after about 20 years in a vegetative state. Histological examination of the extensively atrophic and devastated brain (680 g) revealed the almost total loss of cerebral cortical neurons associated with numerous β-protein amyloid plaques, many extracellular tangles and a large number of hypertrophic astrocytes, and prominent amyloid angiopathy. The astrocytes were frequently immunopositive for anti-human tau antibody (anti-htau) and anti-ubiquitin antibody (anti-ubi). Double immunostaining with anti-htau and anti-glial fibrillary acidic protein (GFAP) antibody clearly demonstrated htau-positive domains within the GFAP-positive perikarya/and processes of several astrocytes. Electron microscopy of the hippocampal CA1, which was completely devoid of pyramidal neurons, revealed, in astrocytes, abnormal filaments indistinguishable from the paired helical filaments (PHFs) seen in neurons. On immunoelectron microscopy, the filaments were observed to be labeled with anti-htau and anti-ubi, exhibiting the same immunohistochemical features as neuronal PHFs. This is the first demonstration of clearly constricted and both tau- and ubiquitin-positive PHFs in astrocytes, indicating that, in some special conditions like in our case, processes similar to those that attack neurons also affect astrocytes and ultimately make the latter form PHFs.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Key words: Neurofibrillary tangle ; Tau ; Phosphorylation ; Astrocyte ; Oligodendrocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Tau accumulating as paired helical filaments (PHF) in Alzheimer's disease brain is considered to be abnormally phosphorylated on distinct sites. To compare the phosphorylation state of tau-positive neuronal inclusions among diverse neurologic diseases, we have probed these lesions with three well-defined PHF/tau monoclonals, C5, M4 and tau 1, that most likely recognize three proline-directed phosphorylation sites in PHF-tau. In Alzheimer's disease brain all three monoclonals intensely immunostained intracellular neurofibrillary tangles, neuropil threads, senile plaque neurites, and “pretangle neurons” in a phosphorylation-dependent manner. They also stained, in the same manner, Pick bodies in Pick's disease, and neurofibrillary tangles and neuropil threads in various tangle-forming neurologic diseases. In most of these diseases (including Pick's disease, progressive supranuclear palsy, subacute sclerosing panencephalitis, and Alzheimer's disease) astrocytes and oligodendrocytes were found to contain tau-positive inclusions which showed the same immunocytochemical characteristics. Thus, the widely occurring tau-positive inclusions share common phosphorylation characteristics irrespective of underlying diseases or cell types.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0533
    Keywords: Neurofibrillary tangle ; Tau ; Phosphorylation ; Astrocyte ; Oligodendrocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Tau accumulating as paired helical filaments (PHF) in Alzheimer's disease brain is considered to be abnormally phosphorylated on distinct sites. To compare the phosphorylation state of tau-positive neuronal inclusions among diverse neurologic diseases, we have probed these lesions with three well-defined PHF/tau monoclonals, C5, M4 and tau 1, that most likely recognize three proline-directed phosphorylation sites in PHF-tau. In Alzheimer's disease brain all three monoclonals intensely immunostained intracellular neurofibrillary tangles, neuropil threads, senile plaque neurites, and “pretangle neurons” in a phosphorylation-dependent manner. They also stained, in the same manner, Pick bodies in Pick's disease, and neurofibrillary tangles and neuropil threads in various tangle-forming neurologic diseases. In most of these diseases (including Pick's disease, progressive supranuclear palsy, subacute sclerosing panencephalitis, and Alzheimer's disease) astrocytes and oligodendrocytes were found to contain tau-positive inclusions which showed the same immunocytochemical characteristics. Thus, the widely occurring tau-positive inclusions share common phosphorylation characteristics irrespective of underlying diseases or cell types.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 82 (1991), S. 159-163 
    ISSN: 1432-0533
    Keywords: Lewy body ; Lewy body-like hyaline inclusion ; Ca2+/calmodulin-dependent protein kinase II ; Parkinson's disease ; Amyotrophic lateral sclerosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is one of the predominant protein kinases in the brain. We found that CaM kinase II immunoreactivity was concentrated in the peripheral halos of Lewy bodies (LBs) in Parkinson's disease and Lewy body-like hyaline inclusions (LBHIs) in amyotrophic lateral sclerosis. An immunoelectron microscopic examination of LBs revealed that the filaments at the periphery of LBs were decorated with immunopositive deposits. Since CaM kinase II has a broad substrate specificity and can phosphorylate neurofilaments and other cytoskeletal proteins, it may play some role in the formation of LBs and LBHIs through the aberrant phosphorylation of the cytoskeletal elements in these inclusions.
    Type of Medium: Electronic Resource
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