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  • 1
    ISSN: 0022-2836
    Keywords: DNA complex ; RecA ; flow orientation ; pitch ; small-angle neutron scattering
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0022-2836
    Keywords: DNA-protein complex ; RecA ; genetic engineering ; linear dichroism ; recombination
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimie 73 (1991), S. 491-495 
    ISSN: 0300-9084
    Keywords: N-AcO-AAF ; RecA ; alternating GC sequences ; frameshift ; mutagenesis ; repetitive sequences
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimie 73 (1991), S. 219-226 
    ISSN: 0300-9084
    Keywords: RecA ; RecA-DNA complex ; linear dichroism ; recombination ; strand exchange
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    International journal of clinical oncology 5 (2000), S. 164-170 
    ISSN: 1437-7772
    Keywords: Key words P-glycoprotein ; Osteosarcoma ; Soft-tissue sarcoma ; Prognosis ; Immunohistochemistry ; RT-PCR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background. The purpose of this study was to investigate the correlation between P-glycoprotein status and outcome in adult patients with high-grade osteosarcomas and soft-tissue sarcomas. Methods. P-glycoprotein status was determined im-munohistochemically in specimens from 28 patients with osteosarcoma and 34 patients with soft-tissue sarcoma. The polyclonal antibody mdr(Ab-1) was used for either decalcified or undecalcified tissue samples which were formalin-fixed and paraffin-embedded. The expression of P-glycoprotein mRNA was also determined by the polymerase chain reaction in 23 fresh sarcoma specimens. P-glycoprotein status was analyzed in relation to the duration of event-free survival. Results. Positivity for P-glycoprotein was found in 29% of the osteosarcomas and 34% of the soft-tissue sarcomas. Consistent results were obtained at both the immunohistochemical and reverse transcriptase-polymerase chain reaction (RT-PCR) levels in 19 of 23 sarcomas (83%). In patients with osteosarcoma, the presence of increased levels of P-glycoprotein was significantly associated with a decreased probability of event-free survival after diagnosis (P = 0.022). In contrast, in patients with soft-tissue sarcoma there was no correlation between the level of P-glycoprotein and prognosis. Conclusions. In patients with high-grade osteosarcomas, the presence of increased levels of P-glycoprotein detected by polyclonal antibody mdr(Ab-1) was associated with a significantly increased risk of adverse events. This association was not found in patients with soft-tissue sarcomas.
    Type of Medium: Electronic Resource
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  • 6
    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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  • 7
    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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  • 8
    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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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 249 (1992), S. 24-27 
    ISSN: 1434-4726
    Keywords: Immune-mediated otitis media ; T-cell subsets ; Immunohistochemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To examine the role of T-cell subsets in immune-mediated otitis media with effusion induced by keyhole limpet hemocyanin (KLH), we used immuno-histochemical methods to investigate the kinetics of immunocytes of the middle ear (ME) and eustachian tube (ET) in healthy BALB/c mice. Antibodies against murine macrophages and granulocytes (anti-Mac-1), helper T cells (anti-Lyt-1), suppressor T cells (anti-Lyt-2), immunoglobulins (anti-IgG, -IgM, -IgA), secretory component (SC) and KLH were used. The ME exhibited a substantial immune response, whereas the response of the ET was minor and was associated with a secondary ME immune response. After KLH challenge, an effusion with an extensive infiltration of inflammatory cells (Mac-1, IgG+ and IgM+ cells) was observed at days 1 and 3 in the ME cavity and rapidly disappeared by day 7. Within the ME mucosa, a large number of cells was observed at days 1 and 3, peaking on day 7 when a submucosal lymphoid infiltration was detected. In the immune response of the ME mucosa, Mac-1 cells were the predominant cell type followed by helper T cells, IgG+ cells, IgA+ cells and then IgM+ cells. Suppressor T cells were rarely detected after KLH challenge. SC was present within ME epithelial cells from days 1 to 14. From these findings, we conclude (1) that the majority of infiltrating cells in the ME cavity originate from circulating blood; (2) that the ME mucosa has an excellent capacity to mount a strong immune response, including mucosal immunity, through the accumulation of immunocytes for antigen processing and antibody production; (3) that elimination of antigen appears to be the most important factor for returning the immune response to a quiescent state.
    Type of Medium: Electronic Resource
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