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  • 1995-1999  (5)
  • β-Amyloid  (4)
  • A/Aichi/2/68  (1)
  • 1
    ISSN: 1432-0533
    Schlagwort(e): Key words Membrane-type matrix metalloprotease ; Gelatinase A ; Human brain ; Microglia ; β-Amyloid
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-0533
    Schlagwort(e): Membrane-type matrix metalloprotease ; Gelatinase A ; Human brain ; Microglia ; β-Amyloid
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    ISSN: 1432-0533
    Schlagwort(e): Key words Gelatinase A ; β-Amyloid ; Microglia ; Alzheimer's disease ; Schwann cell
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    ISSN: 1432-0533
    Schlagwort(e): Gelatinase A ; β-Amyloid ; Microglia ; Alzheimer's disease ; Schwann cell
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    ISSN: 1432-0533
    Schlagwort(e): Key words Cytoplasmic dynein ; Influenza A virus ; A/Aichi/2/68 ; Molecular mimicry ; Immunohistochemistry
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Immunohistochemistry with an antibody to influenza A/Aichi/2/68 (H3N2) virus was performed using normal mouse, rat and human brain tissues. Dot-like or filamentous structures in the neuronal cytoplasm were clearly stained. Axons were also stained, but weakly. Lewy bodies in Parkinson’s disease substantia nigra were also positive. Immunoscreening of the antibody using mouse brain cDNA revealed that this antibody recognized the heavy chain of cytoplasmic dynein. Immunoblot analysis also showed that the reactive molecule was the same size as cytoplasmic dynein (microtubule-associated protein 1C). This is an example of molecular mimicry between cytoplasmic dynein and influenza A virus, and the antibody appears to be useful for the localization on cytoplasmic dynein in the central nervous system.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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