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  • 1
    Electronic Resource
    Electronic Resource
    Gelatinase A expression and localization in human breast cancers. An in situ hybridization study and immunohistochemical detection using confocal microscopy (1994)
    Springer
    Virchows Archiv 424 (1994), S. 641-645 
    Details
    ISSN: 1432-2307
    Keywords: Gelatinase A ; Breast carcinoma ; Basement membrane ; Invasion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The gelatinase A (72 kDa type IV collagenase) is a matrix metallo-proteinase which degrades basement membrane collagens. Various studies emphasize its role in stromal invasion of cancers, but there is some controversy about its origin. Gelatinase A was localized by immunohistochemistry using confocal microscopy in 15 human mammary carcinomas. In addition, the cells responsible for the synthesis of this enzyme were detected by in situ hybridization. Most invasive and non-invasive tumour cells were labelled by immunohistochemistry. Of particular interest was the pattern observed in some pre-invasive areas. Gelatinase A was found in fibroblasts in close contact with pre-invasive tumour clusters. Confocal observation allowed a more precise localization of gelatinase A to the periphery of tumour clusters along the basement membranes and in peritumour fibroblasts. The malignant epithelial cells were negative by immunohistochemistry in these areas. By in situ hybridization, mRNAs encoding gelatinase A were detected only in fibroblasts in close contact with pre-invasive and well differentiated tumour clusters. These findings support the hypothesis that peritumour fibroblasts produce gelatinase A and that breast cancer cells may bind this enzyme to their cell surface and/or internalize it.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01069745
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Gelatinase A expression and localization in human breast cancers. An in situ hybridization study and immunohistochemical detection using confocal microscopy (1994)
    Springer
    Virchows Archiv 424 (1994), S. 641-645 
    Details
    ISSN: 1432-2307
    Keywords: Gelatinase A ; Breast carcinoma ; Basement membrane ; Invasion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The gelatinase A (72 kDa type IV collagenase) is a matrix metallo-proteinase which degrades basement membrane collagens. Various studies emphasize its role in stromal invasion of cancers, but there is some controversy about its origin. Gelatinase A was localized by immunohistochemistry using confocal microscopy in 15 human mammary carcinomas. In addition, the cells responsible for the synthesis of this enzyme were detected by in situ hybridization. Most invasive and non-invasive tumour cells were labelled by immunohistochemistry. Of particular interest was the pattern observed in some pre-invasive areas. Gelatinase A was found in fibroblasts in close contact with pre-invasive tumour clusters. Confocal observation allowed a more precise localization of gelatinase A to the periphery of tumour clusters along the basement membranes and in peritumour fibroblasts. The malignant epithelial cells were negative by immunohistochemistry in these areas. By in situ hybridization, mRNAs encoding gelatinase A were detected only in fibroblasts in close contact with pre-invasive and well differentiated tumour clusters. These findings support the hypothesis that peritumour fibroblasts produce gelatinase A and that breast cancer cells may bind this enzyme to their cell surface and/or internalize it.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195779
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Collagens, laminin, fibronectin, and cytoskeletal composition of cells in syngeneic aortal vein grafts in the rat (1985)
    Springer
    Research in experimental medicine 185 (1985), S. 355-366 
    Details
    ISSN: 1433-8580
    Keywords: Connective tissue ; Arterial graft ; Collagens ; Laminin ; Cytoskeleton
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The supradiaphragmatic vena cava of the rat was transplanted to the abdominal aorta in syngeneic recipients. The cells and the connective tissue matrix of these grafts were studied 3 days to 12 weeks after transplantation by immunofluorescence staining of the cytoskeletal proteins desmin, vimentin, and myosin. The matrix proteins, collagen Types I and III, laminin, fibronectin, and fibrin(ogen) were similarly demonstrated. Blood coagulation Factor VIII was used as a marker for endothelial cells. Inflammatory cells invaded the graft during Week 1, but later on the grafts were crowded with cells containing vimentin. Intimal thickenings developed already after 1 week. Smooth muscle cells containing desmin proliferated in these thickenings. After transplantation collagen Type I increased in the graft, but collagen Type III rather decreased. During the phase of intense proliferation of smooth muscle cells the media contained a rich matrix of diffusely distributed laminin. The laminin of older grafts was confined mostly to the subintimal zone and to the intimal plaques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01851915
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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