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  • Articles: DFG German National Licenses  (7)
  • Gelatinase A  (4)
  • Human brain  (3)
  • Stratum corneum  (3)
  • 1
    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
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  • 2
    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
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  • 3
    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
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  • 4
    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
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 279 (1987), S. 281-282 
    ISSN: 1432-069X
    Keywords: Stratum corneum ; Desquamation ; Cell renewal time ; Dansyl chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-069X
    Keywords: Hematoxylin stainable protein ; Keratohyalin granules ; Membrane lining protein ; Stratum corneum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A monoclonal antibody (Ted-R-1) to the keratohyalin granules (KHGs) of the newborn rat epidermis was developed by immunizing mice with a pH 4.7 hematoxylin-stainable fraction of the extract in a 50 mM Tris-HCl buffer, pH 7.3, containing 10 μ/ml phenylmethylsulfonyl fluoride (PMSF) from the newborn rat whole epidermis. Using an indirect immunofluorescence technique, Ted-R-1 was located in two places: (a) the KHGs and (b) the cell membrane region of the stratum corneum. Under immunoelectron microscopy, the antigenic materials were located at the periphery of the KHGs. Immunoblotting analyses of the antigenic pH 4.7 fraction, the Tris-HCl extract from the stratum corneum, and the Tris-8M urea extract from freeze-dried whole skin demonstrated that there were 55 kd, 43 kd, and 78 kd polypeptides, respectively, with which Ted-R-1 reacts. No possitive spot was seen in the dermal extract. The major amino acids of the 55 kd protein were glycine (24.4%), serine (17.3%), glutamic acid (14.1%), and alanine (7.7%), while the histidine residue was only 3.1%. On the basis of its amino acid composition, the 55 kd protein is the third component of KHGs — in addition to histidine-rich and cystinerich proteins.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 285 (1993), S. 372-377 
    ISSN: 1432-069X
    Keywords: Stratum corneum ; Protease ; Desquamation ; Scaly skin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In order to identify the endogenous protease associated with stratum corneum (SC) desquamation, we examined properties of proteases in the stratum corneum of normal human skin. SC were obtained by tape stripping, washed in toluene and then dried. The proteolytic activity in SC was measured using peptidyl 4-methyl-coumaryl-7-amides (MCAs). The SC was dispersed uniformly in the reaction mixture with dimethylformamide and Triton X-100 and incubated with the peptidyl MCAs. The protease in the SC hydrolysed both Boc-Phe-Ser-Arg-MCA and Boc-Gln-Ala-Arg-MCA (substrates for trypsin) very effectively. The hydrolytic activity was inhibited by the serine protease inhibitors diisopropyl fluorophosphate (DFP), aprotinin, antipain and leupeptin, but not by chymostatin, a chymotrypsin inhibitor. These results show that one or more trypsin-like serine protease is present in the SC of normal human skin. Casein-acrylamide electrophoresis showed that the molecular weight of this serine protease was about 30 kDa. We have previously shown that cells dissociate from human SC sheets in a detergent mixture (N,N-dimethyldodecylamine oxide and sodium lauryl sulphate). This cell dissociation was inhibited by aprotinin and leupeptin. In addition, the proteolytic activity in the outer SC was higher than that in the inner SC, and the activity in the SC of scaly skin induced by SLS treatment was higher than that of untreated skin. These results strongly suggest that the trypsin-like serine protease described here is involved in SC desquamation.
    Type of Medium: Electronic Resource
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