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  • 1
    Electronic Resource
    Electronic Resource
    Vimentin immunoreactivity in normal and pathological human brain tissue (1992)
    Springer
    Acta neuropathologica 84 (1992), S. 157-162 
    Details
    ISSN: 1432-0533
    Keywords: Vimentin ; Astrocyte ; Microglia ; Macrophage ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Vimentin immunoreactivity was examined in brain tissues from non-neurological and various human central nervous system disease cases. In all brain tissues examined, vimentin immunoreactivity was intensely positive in ependymal cells and subpial tissues, and weakly positive in some capillaries and some white matter astrocytes. In affected areas of Alzheimer's disease (AD), Pick's disease, amyotrophic lateral sclerosis (ALS), multiple sclerosis (MS) and cerebral infarction cases, numerous intensely vimentin-immunopositive astrocytes of both protoplasmic and fibrous morphology were demonstrated. A few such astrocytes were also observed in Parkinson's disease and progressive supranuclear palsy. ALS, MS and infarction brains also had numerous, strongly vimentin-positive, round and fat-laden microglia/macrophages. In AD and ALS, a few reactive microglia with irregularly enlarged shapes were vimentin positive. In AD, they were almost exclusively related to senile plaques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00311389
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Columnar arragement of β-amyloid protein deposits in the cerebral cortex of patients with Alzheimer's disease (1993)
    Springer
    Acta neuropathologica 85 (1993), S. 400-403 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Cerebral cortex ; β-amyloid protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The spatial pattern of β-amyloid protein (BAP) deposits in Alzheimer's disease cerebral cortex was investigated. In cortical areas where the accumulation of BAP was relatively sparse, the deposits tended to accumulate vertically in a columnar arrangement. Typically, these aggregates consisted of both consolidated and diffuse deposits approximately 200 to 600 μm in width. Blood vessels running perpendicularly to the pial surface were sometimes observed penetrating the center of these colunms, but this was not a consistent finding. These BAP extracellular aggregates might be related to the columnar organization of the cerebral cortex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334451
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Selective localization of gelatinase A, an enzyme degrading β-amyloid protein, in white matter microglia and in Schwann cells (1995)
    Springer
    Acta neuropathologica 89 (1995), S. 199-203 
    Details
    ISSN: 1432-0533
    Keywords: Key words Gelatinase A ; β-Amyloid ; Microglia ; Alzheimer's disease ; Schwann cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Gelatinase A is an enzyme capable of cleaving soluble β-amyloid protein (βAP), and may function as an α-secretase to produce secretory forms of amyloid precursor protein. We examined gelatinase A immunoreactivity in the brains and posterior roots of neurologically normal, lacunar stroke, Alzheimer disease (AD), amyotrophic lateral sclerosis, progressive supranuclear palsy and myasthenia gravis cases. The gelatinase A antibody stained only microglial cells in the white matter in all the brain tissues. In AD brain, the reactive microglia located in the center of classical senile plaques, as well as in other microglial cells in the gray matter, showed no immunoreactivity. Gelatinase A in white matter microglial cells may play a role in preventing local deposition of βAP. In the posterior root, Schwann cells had positive immunoreactivity. As with other metalloproteases, gelatinase A in Schwann cells may play an antiproliferative role.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309334
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Selective localization of gelatinase A, an enzyme degrading β-amyloid protein, in white matter microglia and in Schwann cells (1995)
    Springer
    Acta neuropathologica 89 (1995), S. 199-203 
    Details
    ISSN: 1432-0533
    Keywords: Gelatinase A ; β-Amyloid ; Microglia ; Alzheimer's disease ; Schwann cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Gelatinase A is an enzyme capable of cleaving soluble β-amyloid protein (βAP), and may function as an α-secretase to produce secretory forms of amyloid precursor protein. We examined gelatinase A immunoreactivity in the brains and posterior roots of neurologically normal, lacunar stroke, Alzheimer disease (AD), amyotrophic lateral sclerosis, progressive supranuclear palsy and myasthenia gravis cases. The gelatinase A antibody stained only microglial cells in the white matter in all the brain tissues. In AD brain, the reactive microglia located in the center of classical senile plaques, as well as in other microglial cells in the gray matter, showed no immunoreactivity. Gelatinase A in white matter microglial cells may play a role in preventing local deposition of βAP. In the posterior root, Schwann cells had positive immunoreactivity. As with other metalloproteases, gelatinase A in Schwann cells may play an antiproliferative role.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309334
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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