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  • 11
    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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  • 12
    Electronic Resource
    Electronic Resource
    Differences in tetranectin immunoreactivity between benign and malignant breast tissue (1991)
    Springer
    Histochemistry and cell biology 95 (1991), S. 427-433 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Tetranectin (TN) is a human, plasminogen kringle 4 binding plasma protein with ubiquitous cellular distribution and lectin-like characteristics. By means of the peroxidase-antiperoxidase staining technique a polyclonal and a monoclonal antibody were used to demonstrate TN within the intracellular as well as the extracellular compartment of invasive breast carcinoma. Whereas cell associated TN was universal showing only quantitative differences depending of the growth pattern of the tumor, 78 of 133 tumors displayed TN extracellularly as well. The occurrence of this stromal TN immunoreactivity was closely associated with desmoplasia, recognized morphologically by an increase in fibroblastic cells and immunohistochemically by an intense staining for the connective tissue glycoprotein fibronectin (FN). Benign breast tissue displayed a universal, intense cytoplasmic but no extracellular reaction for TN, with the exception of rare foci of granulation tissue and around dilated cysts. Functional studies have shown that human embryonal lung fibroblasts increase their release of TN to the growth medium upon stimulation. The presence of TN extracellularly within fibroblast-rich foci of desmoplasia (and granulation tissue) suggests that a similar increased release of the protein takes place in vivo during active states. Desmoplasia has been found to have a protective effect on tumor cell propagation and metastasis in a murine model. The molecular interactions, which are responsible for this effect, are undoubtedly complex. However, TN may, by its specific binding to kringle 4 of plasminogen and its high affinity for sulphated polysaccharides, add to the understanding of how plasminogen activation is modulated at the local extracellular level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315737
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  • 13
    Electronic Resource
    Electronic Resource
    The value of hyaluronidase treatment of different tissues before demonstration of fibronectin by the indirect immunoperoxidase technique (1982)
    Springer
    Histochemistry and cell biology 76 (1982), S. 517-525 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The influence of testicular hyaluronidase treatment on the immunohistochemical localization of fibronectin in different tissues (human articular cartilage, large intestine, synovial membrane and experimental granulation tissue) as well on frozen as on formaldehyde fixed, paraffin embedded tissue, has been studied using the indirect immunoperoxidase technique. Pretreatment with hyaluronidase is essential in demonstrating fibronectin in frozen sections of human articular cartilage. In the other tissues examined treatment with hyaluronidase was not essential, but gave a more optimal staining quality. The effect of hyaluronidase treatment was to some extent dependent on the duration of treatment. In formaldehyde fixed, paraffin processed tissue the improvement with hyaluronidase treatment was only seen when the hyaluronidase followed pepsin digestion of the deparaffinized tissue sections.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489906
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  • 14
    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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  • 15
    Electronic Resource
    Electronic Resource
    Opsonic activity of fibronectin in the phagocytosis ofStaphylococcus aureus by polymorphonuclear leukocytes (1984)
    Springer
    European journal of clinical microbiology & infectious diseases 3 (1984), S. 108-112 
    Details
    ISSN: 1435-4373
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effect of the opsonic activity of human purified fibronectin on phagocytosis ofStaphylococcus aureus by human polymorphonuclear leukocytes was investigated. After opsonization with fibronectin there was a significant increase in the rate of phagocytosis of four out of sixStaphylococcus aureus strains. Both attachment to and ingestion by leukocytes was affected, as revealed by lysostaphin treatment. Incubation of leukocytes with fibronectin prior to phagocytosis did not enhance the phagocytosis ofStaphylococcus aureus. This shows that the observed enhancement of phagocytosis was dependent on the binding of fibronectin toStaphylococcus aureus. The ability of fibronectin to opsonize different strains ofStaphylococcus aureus varied with the strain. A variation was also observed in fibronectin-induced phagocytosis by leukocytes from different donors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02014326
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