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  • 1985-1989  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    High-Dose Survival in the Lymphocytic Choriomeningitis Virus Infection Is Accompanied by Suppressed DTH but Unaffected T-Cell Cytotoxicity (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 21 (1985), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Provided that intracerebral inoculation is applied, an increase in the virus dose from 102to 104 LD50 of lymphocytic choriomeningitis virus (LCMV) leads to strikingly reduced mortality. To analyse the background for this autointerferencc, we measured several virologic and immunologic variables in mice infected with these doses of virus. In the high-dose mice we found generally higher organ virus titres and serum interferon titres than in the low-dose mice. Since we could demonstrate that virus-specific T-cell cytotoxicity in spleen, peripheral blood, and meningeal exudate was similar after intracerebral infection with large and small virus doses, and since the LCMV infection in the brain qualitatively and quantitatively was independent of the size of virus inoculum, the explanation for the survival of the high-dose animals is obviously not lack of possibilities for interaction between cytotoxic T cells and infected sensitive targets in the central nervous system. On the other hand, high doses of virus caused a clear suppression of the LCMV-specific delayed-type hypersensitivity(DTH). In addition, when splenocytes from high-dose animals were transferred either intravenously or locally into the footpad of newly virus-challenged mice. DTH was markedly suppressed as compared with the response after transfer of spleen cells from low-dose mice. We therefore conclude that autointerferencc in the LCMV infection is due to a selective suppression of Td function. Large amounts of persistent virus late after infection with high doses of virus suggest a central role for Td function also in virus clearance. Finally, our results indicate the existence of two subsets of K, D region-restricted T cells, one mediating cytotoxicity and the other mediating DTH. This possibility is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01406.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Tetranectin immunoreactivity in normal human tissues (1989)
    Springer
    Histochemistry and cell biology 92 (1989), S. 29-35 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A recently discovered human plasma protein, tetrancetin (TN), which has previously been demonstrated immunohistochemically within various endocrine tissues, was in this study identified in an additional number of epithelial and mesenchymal cells by two polyclonal antibodies and one monoclonal using the conventional immunoperoxidase staining technique and a modification of the CLONO-GLAD procedure. TN was found in endothelial and epithelial tissues, particularly in cells with a high turn-over or storage function such as gastric parietal and zymogenic cells absorptive surface epithelium of the small intestine, ducts of exocrine glands and pseudostratified respiratory epithelium. Also mesenchymal cells produced a TN positive staining reaction, which was most conspicious in mast cells, but also present in some lymphocytes, plasma cells, macrophages, granulocytes, striated and smooth muscle cells and fibroblasts. SDS-PAGE and Western blotting analysis of cultured human embryonal fibroblasts (WI-38) showed that the cells besides TN contain another protein with a molecular weight of 82 000. As this protein, however, reacted with our affinity purified antibodies it probably represents a precussor of TN or a protein with a molecular weight of approximately 60 000, which is covalently linked to TN. This and the fact that TN shows amino acid sequence homologiess to the carboxyterminal part of the asialo-glycoprotein receptor and a cartilage proteoglycan core protein as well a binding affinity to plasminogen points to TN as being part of a larger molecule, which possibly has been cleaved by proteolysis at the cellular site and then passed into the blood, where it polymerizes into a tetramer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495012
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of a novel, human plasma protein, tetranectin, in human endocrine tissues (1987)
    Springer
    Histochemistry and cell biology 87 (1987), S. 195-199 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A monospecific antibody to a plasminogen Kringle 4-binding tetramer protein of human blood, tetranectin, was applied to various human endocrine tissues employing the peroxidase-antiperoxidase staining technique. Endocrine cells with a known protein or glycoprotein hormonal production such as chromophils (pituitary), follicular and parafollicular cells (thyroid), chief cells (parathyroid), hepatocytes (liver), islet cells (pancreas) and ganglion cells of the adrenal medulla displayed a convincing, positive staining reaction for tetranectin, which varied from cell to cell within the different tissues. The liver showed a distinct and universal reaction within almost all hepatocytes, thus raising suspicion of producing the bulk of tetranectin to the blood. Tetranectin has recently been characterized as a lectin-like protein with amino acid sequence homology to the core protein of a rat chondrosarcoma proteoglycan. Proteoglycans have been demonstrated in secretory granules of rat pituitary and pancreatic islet cells, where they probably serve as modulators in hormonal production. The granular, cytoplasmic immunohistochemical localization of tetranectin demonstrated in this study combined with the fact that tetranectin is known to attach to plasminogen and promote plasminogen activation catalysed by tissue plasminogen activator suggests that this protein might have a dual function, serving both as a regulator in the seretion of certain hormones and as a participant in the regulation of the limited proteolysis, which is considered important for the activation of prohormones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492409
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    Paper (German National Licenses)
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