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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 109 (1987), S. 1274-1275 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 110 (1988), S. 244-250 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Inflammation research 25 (1988), S. 360-367 
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract α2Macroglobulin is a proteinase inhibitor which is converted from its native form into an electrophoretically “fast” form by reaction with a proteinase or methylamine. All α2M “fast” forms bind to a specific high-affinity receptor on macrophages. α2M “fast” forms inhibit the interferon-γ (IFN)-induced increase in macrophage Ia expression. This study examined whether α2M-proteinase complexes alter prostaglandin (PG) E2 synthesis, and whether PGE2 mediates α2M “fast” forms effects on macrophage Ia expression. Culture with α2M “fast” forms increased PGE2 accumulation in the medium over control values in a dose-dependent manner. Culture with IFN alone did not increase PGE2 levels, but potentiated the effect of α2M-proteinase complexes on PGE2 levels. Inhibition of PGE2 synthesis did not alter the PGE2 did suppress IFN-induced Ia expression. Thus, α2M-proteinase complexes increase macrophage PGE2 synthesis, but increased synthesis of PGE2 or other cyclooxygenase products is not the mediator of antagonism of IFN-induced Ia expression by α2M-proteinase complexes.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0533
    Keywords: Endothelial cell ; Factor VIII/von Willebrand factor ; Glial fibrillary acidic protein ; Hemangioblastoma ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The histogenesis of hemangioblastoma stromal cells is unresolved. Ultrastructural observations suggest that the stromal cells, endothelial cells, and pericytes that compose this neoplasm are all derived from angiogenic mesenchyme. The expression of factor VIII/von Willebrand factor (FVIII/vWF), a specific marker for endothelial cells, and of glial fibrillary acidic protein (GFAP), a specific marker for glial cells, was examined in 16 hemangioblastomas using the peroxidase-antiperoxidase immunohistochemical method. Endothelial cell staining for FVIII/vWF was intense in 14 tumors, weak in one, and absent in another. There was no stromal cell staining in any of the neoplasms. Process-bearing, GFAP-positive cells were observed near the tumor margin in 13 cases, and deeper in the neoplasm in 8. In two of these tumors there were also occasional GFAP-positive cells that lacked processes and had a vacuolated cytoplasm. Virtually all of the GFAP-positive cells were interpreted as trapped astrocytes rather than stromal cells. The lack of expression of FVIII/vWF by the stromal cells indicates that they are antigenically distinct from endothelial cells. Several alternatives for stromal cell histogenesis remain open. The stromal cells may be derived from endothelial cells that have undergone antigenic loss, or from angiogenic mesenchymal cells that do not express FVIII/vWF. Alternatively, the stromal cells may originate from nonangiogenic mesenchymal cells derived from the mesoderm or neuroectoderm.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Histopathology 13 (1988), S. 0 
    ISSN: 1365-2559
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A case of a primary undifferentiated sarcoma of the descending thoracic aorta in a 75-year-old man is reported. Intraluminal growth and occlusion produced congestive heart failure and renal failure. The thoracic aorta was relatively normal on chest radiography so that the lesion was undiscovered until the autopsy. To our knowledge, it is the first case of a primary undifferentiated sarcoma of the thoracic aorta, and the first undifferentiated aortic sarcoma to be examined with immunohistochemistry and electron microscopy. Electron microscopy and immunohistochemistry verified the sarcomatous nature of the undifferentiated neoplasm.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Porphyromonas gingivalis is closely associated with the development of some forms of periodontitis. The major cysteine proteinases released by this bacterium hydrolyze peptide bonds only after arginyl (gingipain R) or lysyl residues (gingipain K). No target protein inhibitors have been identified for either enzyme, leading us to investigate their inhibition by human plasma α2-macroglobulin (α2M). Both 50- and 95 kDa gingipain R were efficiently inhibited by α2M, whereas the catalytic activity of gingipain K could not be eliminated. All 3 enzymes were, however, inhibited by a homologous macroglobulin from rat plasma, α1-inhibitor-3 a-Macroglobulins must be cleaved in the so-called “bait region“ in order to inhibit proteinases by a mechanism involving physical entrapment of the enzyme. A comparison of the aminio acid sequences of the 2 macroglobulins indicates that the lack of lysyl residues within the bait region of α2M protects Lys-specific proteinases from being trapped. On this basis, other highly specific proteinases might also not be inhibited by α2M, possibly explaining the inability of the inhibitor to control proteolytic activity in some bacterially induced inflammatory states, despite its abundance (2-5 mg/ml) in vascular fluids.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 74 (1996), S. 463-469 
    ISSN: 1432-1440
    Keywords: Plasminogen ; Autoimmunity ; Rheumatoid arthritis ; Systemic lupus erythematosus ; Sjögren's syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Sera from patients with rheumatoid arthritis containing high titers of anti-streptokinase antibodies were found to contain anti-plasminogen antibodies of the IgG and IgA classes. High titers of anti-plasminogen autoantibodies of the IgA class were also found in sera from patients with systemic lupus erythematosus and Sjögren syndrome. Studies of the immune response to thrombolytic therapy with streptokinase in patients with no prior history of autoimmune disease suggest a strong correlation between streptokinase administration and the appearance of autoantibodies to plasminogen of the IgA class. The IgA anti-plasminogen autoantibody is specific for an epitope in a region of plasminogen which binds streptokinase and the IgG autoantibody reacts with an epitope in the C-terminal region corresponding to the catalytic domain of the plasminogen zymogen. Our findings suggest a different origin for the two classes of antiplasminogen immunoglobulins in rheumatoid arthritis patients. Since plasminogen binding to rheumatoid synovial fibroblasts is enhanced, the high titers of both classes of anti-plasminogen autoantibodies may add to the localization and perpetuation of the immune response. We suggest that plasminogen may be a target of the immune response in autoimmune disease.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 74 (1996), S. 463-469 
    ISSN: 1432-1440
    Keywords: Key words Plasminogen ; Autoimmunity ; Rheumatoid arthritis ; Systemic lupus erythematosus ; Sjögren’s syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Sera from patients with rheumatoid arthritis containing high titers of anti-streptokinase antibodies were found to contain anti-plasminogen antibodies of the IgG and IgA classes. High titers of anti-plasminogen autoantibodies of the IgA class were also found in sera from patients with systemic lupus erythematosus and Sjögren syndrome. Studies of the immune response to thrombolytic therapy with streptokinase in patients with no prior history of autoimmune disease suggest a strong correlation between streptokinase administration and the appearance of autoantibodies to plasminogen of the IgA class. The IgA anti-plasminogen autoantibody is specific for an epitope in a region of plasminogen which binds streptokinase and the IgG autoantibody reacts with an epitope in the C-terminal region corresponding to the catalytic domain of the plasminogen zymogen. Our findings suggest a different origin for the two classes of anti-plasminogen immunoglobulins in rheumatoid arthritis patients. Since plasminogen binding to rheumatoid synovial fibroblasts is enhanced, the high titers of both classes of anti-plasminogen autoantibodies may add to the localization and perpetuation of the immune response. We suggest that plasminogen may be a target of the immune response in autoimmune disease.
    Type of Medium: Electronic Resource
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