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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
    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
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    White matter microglia produce membrane-type matrix metalloprotease, an activator of gelatinase A, in human brain tissues (1995)
    Springer
    Acta neuropathologica 90 (1995), S. 421-424 
    Details
    ISSN: 1432-0533
    Keywords: Membrane-type matrix metalloprotease ; Gelatinase A ; Human brain ; Microglia ; β-Amyloid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Membrane-type matrix metalloprotease (MT-MMP) is an activator of gelatinase A (MMP-2), which has previously been found in carcinoma cells. We examined non-neurological and Alzheimer's disease brain tissues for MT-MMP by immunohistochemistry and in situ hybridization. The anti-MT-MMP antibodies gave positive staining of brain microglial cells in all the brain tissues. Positively stained microglia were found only in the white matter. The cells producing MT-MMP protein were also shown to be white matter microglia. These results provide further evidence that activated gelatinase A, which may be a processing enzyme for degradation of β-amyloid protein, may be produced in white matter microglia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294800
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    White matter microglia produce membrane-type matrix metalloprotease, an activator of gelatinase A, in human brain tissues (1995)
    Springer
    Acta neuropathologica 90 (1995), S. 421-424 
    Details
    ISSN: 1432-0533
    Keywords: Key words Membrane-type matrix metalloprotease ; Gelatinase A ; Human brain ; Microglia ; β-Amyloid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Membrane-type matrix metalloprotease (MT-MMP) is an activator of gelatinase A (MMP-2), which has previously been found in carcinoma cells. We examined non-neurological and Alzheimer's disease brain tissues for MT-MMP by immunohistochemistry and in situ hybridization. The anti-MT-MMP antibodies gave positive staining of brain microglial cells in all the brain tissues. Positively stained microglia were found only in the white matter. The cells producing MT-MMP protein were also shown to be white matter microglia. These results provide further evidence that activated gelatinase A, which may be a processing enzyme for degradation of β-amyloid protein, may be produced in white matter microglia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294800
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 5
    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
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Expression of the membrane-type 3 matrix metalloproteinase (MT3-MMP) in human brain tissues (1998)
    Springer
    Acta neuropathologica 96 (1998), S. 347-350 
    Details
    ISSN: 1432-0533
    Keywords: Key words Membrane-type 3 matrix metalloproteinase ; Gelatinase A ; Human brain ; Microglia ; Reverse ; transcriptase-polymerase chain reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Membrane-type 3 matrix metalloproteinase (MT3-MMP) is a novel MT-MMP which has a transmembrane domain at the C terminus, and mediates activation of pro-gelatinase A, just as does MT1-MMP. Previously, we reported that MT1-MMP was expressed on microglial cells only in the white matter [Yamada T, Yoshiyama Y, Sato H, Seiki M, Shinagawa A, Takahashi M (1995) Acta Neuropathol 90 : 421–424]. In the present study of both non-neurological and Alzheimer brain tissues, we examined the localization of MT3-MMP by immunohistochemistry. Anti-MT3-MMP antibodies gave positive staining of microglial cells in all brain tissues. Positively stained microglia were found not only in the white matter but also in the gray matter. Reverse transcriptase-polymerase chain reaction for MT3-MMP mRNA showed the same amount of expression in gray and white matters, while that for gelatinase A and MT1-MMP mRNA expressed much higher in the white matter than in the gray matter. These results suggest that MT3-MMP may play a role on microglial cells, although its role may be different from MT1-MMP in the brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050904
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    Paper (German National Licenses)
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