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  • 1
    Electronic Resource
    Electronic Resource
    Adenosine Deaminase Complexing Protein in Transformed Cells and Colon Cancer (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 451 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb27129.x
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  • 2
    Electronic Resource
    Electronic Resource
    Polyethylene glycol embedded tissue sections for immunoelectronmicroscopy (1981)
    Springer
    Histochemistry and cell biology 73 (1981), S. 195-199 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Several methods for tissue embedding in polyethylene glycol (PEG) were compared with regard to their applicability for pre-embedding immunoelectronmicroscopy. Existing embedding procedures gave unsatisfactory results and therefore a modified procedure was developed. This method, consisting of very brief tissue infiltration with PEG 1500, to which 3% water is added, allowed adequate tissue sectioning. Using these sections for preembedding immunoelectronmicroscopical localisation of glucagon in bovine pancreatic islets adequate ultrastructural morphology was obtained in combination with excellent preservation of peptide hormone immunoreactivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493019
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  • 3
    Electronic Resource
    Electronic Resource
    Some recent developments in immunocytochemistry (1983)
    Springer
    Journal of molecular histology 15 (1983), S. 189-200 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunocytochemistry has become an indispensable tool both in basic biomedical research and in diagnostic histophathology. Several recent innovations have led to improvements in the sensitivity, specificity and precision of these techniques. Numerous modifications of the original methods have been developed, many with increased sensitivity. In particular, methods using protein A or the avidin-biotin complex as second steps appear to be promising. New methods for the quantitative determination of sensitivity have become available. The introduction of monoclonal antibodies as immunocytochemical reagents appears to be a major improvement. New methods of immunochemical analysis, such as immunoblotting and immunospotting of antigens extracted from tissue specimens, allow the molecular composition of immunoreactive antigenic sites in a tissue to be analysed. The accuracy of localization in immunoelectron microscopy has been improved significantly through the use of ultracryotomy of unfixed tissue in combination with colloidal gold particles as a label. In addition, gold particles can be counted and thus allow relatively simple quantification of the immune reaction. Using flow cytometry, especially in combination with monoclonal antibodies, quantitative immunofluorescence has become feasible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01006235
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  • 4
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of adenosine deaminase complexing protein in intestinal mucosa and in colorectal adenocarcinoma as a marker for tumour cell heterogeneity (1985)
    Springer
    Journal of molecular histology 17 (1985), S. 23-31 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Adenosine deaminase complexing protein (ADCP), a dimeric glycoprotein, has been reported to be decreased or deficient in transformed or cancer-derived cell lines, indicating its potential significance as an indicator of malignant transformation. A similar deficiency was reported in total homogenates of tumours of colon, kidney, lung and liver. In previous biochemical studies we failed to confirm the consistent reduction in ADCP concentration in cancer tissues. A possible explanation for our findings was thought to be intercellular heterogeneity in ADCP expression in individual tumour cells. To study ADCP expression in individual cells we developed an immunohistochemical method which was applied to tissue sections. Paraformaldehyde-lysine-periodate (PLP) solution was found to be a suitable fixative. Fixed tissue samples were paraffin-embedded, sectioned and stained for ADCP, using an indirect peroxidase-labelled antibody procedure. The protein was localized in normal colonic mucosa, mainly in the brush border region of the luminal epithelium and in cytoplasmic granules. Intense ADCP immunoreactivity was found also in the basal part of some cells. In cancer cells, three staining patterns were observed: membranous, diffuse cytoplasmic and granular cytoplasmic. The adenocarcinomas exhibited significant intratumour and intertumour heterogeneity in their staining types. Further studies on ADCP expression in colorectal cancer in relation to clinical and histopathological characteristics are warranted in order to fully evaluate the potential significance of ADCP as a cancer associated antigen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003400
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  • 5
    Electronic Resource
    Electronic Resource
    Basement membrane heterogeneity (1989)
    Springer
    Journal of molecular histology 21 (1989), S. 629-633 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01002481
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  • 6
    Electronic Resource
    Electronic Resource
    Integrins: cell adhesives and modulators of cell function (1993)
    Springer
    Journal of molecular histology 25 (1993), S. 469-477 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Integrins encompass a family of cell-surface molecules which play a crucial role in cell-cell and cell-extracellular matrix interaction. Of these heterodimeric transmembrane glycoproteins (consisting of an α and β chain) as yet at least 20 different types have been described, all with a different pattern of reactivity with extracellular matrix components. In this review the cell and tissue distribution of the integrins is discussed, with special emphasis on immunohistochemical localization of the β1 integrins and the α6β4 integrin. The β1 integrins comprise a subfamily in which eight α chains combine with one β (the β1) chain. The α2β1, α3β1 and α6β1 and the α6β4 integrins are expressed on a wide variety of epithelia on the basolateral surface or exclusively on the basal surface facing the basement membrane (e.g. α6β1 and α6β4). Leucocyte integrins, which share a common α2 chain, occur almost exclusively on white blood cells and their precursors. The vitronectin receptors, which share a common αv chain, occur in a wide variety of cell types. Integrins play a major role in the interaction of the cell with the extracellular matrix in order to create and maintain tissue architecture. It has become clear, however, that through integrin-ligand interaction cell function is also modulated. Furthermore, in pathological conditions integrins play a role of some significance. Integrins mediate leucocyte traffic in developing inflammatory processes and function in neoplastic growth when it comes to invasion and metastasis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00159282
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  • 7
    Electronic Resource
    Electronic Resource
    The borderline: Basement membranes and the transition from premalignant to malignant neoplasia (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 28 (1994), S. 216-225 
    Details
    ISSN: 1059-910X
    Keywords: Type IV collagen ; Laminin ; Immunohistochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: In this paper, the use of immunohistochemistry for the analysis of basement membrane components and related extracellular matrix proteins in human cancer is reviewed. Basement membranes in cancer are dynamic structures that are constantly degraded but also deposited, in close collaboration between tumor cells and stromal cells. Basement membrane immunohistochemistry, using antibodies against type IV collagen and laminin, appears to be a useful tool in the analysis of lesions on the borderline between premalignant and malignant. Basement membrane interruptions, however, cannot be used as the only criterion for the diagnosis of malignancy. Type VII collagen is often degraded prior to type IV collagen and laminin in early invasion. This protein also tends to be expressed in carcinomas when it is not found in the corresponding normal tissue. Tenascin seems to play a complex role in the development of human tumors, including promotion of cell growth and differentiation, cell migration during invasion, and tissue remodeling during the development of primary and metastatic lesions. Further systemic exploration of extracellular matrix molecules in neoplasms should yield new information relevant for cancer biologists and useful in cancer diagnosis. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070280306
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  • 8
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    Histochemistry in gene technology (2000)
    Springer
    Details
    Publication Date: 2000-12-09
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 9
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    Immunohistochemical localization of hTERT protein in human tissues (2004)
    Springer
    Details
    Publication Date: 2004-05-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 10
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    Expression of NDRG1, a differentiation-related gene, in human tissues (2002)
    Springer
    Details
    Publication Date: 2002-11-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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