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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 451 (1985), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2307
    Keywords: Keratin ; Alpha-1-antitrypsin ; Lysozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The light microscopic, electron microscopic and histochemical features of a highly malignant colonic tumor resected from a 39 year old man are presented. The tumor was composed predominantly of undifferentiated cells, with focally admixed neuroendocrine, exocrine and squamous cells, occasionally arranged in an organoid manner. Histochemically the tumor contained argyrophilic cells as well as cells that reacted positively with the antibodies to alpha-1-antitrypsin, alpha-1-antichymotrypsin, carcinoembryonic antigen and lysozyme. The term “stem cell carcinoma of the intestine” is proposed for this highly malignant tumor composed of undifferentiated cells exhibiting only focally their multidirectional developmental capacity.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 73 (1981), S. 195-199 
    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
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 232 (1994), S. 40-46 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The formation of basal laminar deposit (BLD) is one of the histopathologic changes in the aging human macula. BLD is assumed to be an early stage of age-related macular degeneration. The location of BLD, between the RPE plasma membrane and its basement membrane and in the outer collagenous zone of Bruch's membrane, and its ultrastructure suggest that it is composed of excessive amounts of basement membrane material. The main components of basement membranes are type IV collagen, heparan sulfate proteoglycans (HSPG) and laminin. Labeled antibodies against these components can therefore be used for the identification and localization of basement membrane material by means of immunohistochemical techniques. In this study the presence of type IV collagen, laminin and HSPG was determined in aged human maculae by immunohistochemistry and immunoelectron microscopy. Tests for the presence of type VI collagen and fibronectin were also performed. We obtained 76 eyes from 68 human subjects at autopsy or after surgical enucleation for anteriorly located choroidal melanomas. The finely granular component of BLD stained positive with antibodies against type IV collagen, HSPG and laminin, but the long-spacing collagen component of BED did not. Neither component of BED was stained with antibodies against type VI collagen or fibronectin. We conclude that BLD consists partly of excess basement membrane material.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Virchows Archiv 435 (1999), S. 391-399 
    ISSN: 1432-2307
    Keywords: Key words Nucleus ; Nuclear matrix ; Lamin ; Nucleolus ; Fibrillogranular network
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  For a long time the molecular basis of nuclear structure has been a matter of debate rather than an established fact. In the last decade the concept of the nuclear matrix has emerged, and the molecular basis of this nuclear infrastructure, although still incomplete, is gradually being unravelled. In early studies concerning the nuclear structure, autoantibodies derived from patients with collagen disease had a significant role. This matrix, the structure remaining after extraction of membranes, nucleic acids and histones, consists of the nuclear lamina, the nucleolus and a fibrillogranular network. The nuclear lamina is composed of the lamins. The nucleolar matrix contains the proteins involved in rRNA processing. The fibrillogranular network is composed of nuclear matrix proteins, a wide variety of which has been discovered. It has become clear that the nuclear matrix not only provides a structural basis for nuclear architecture but also plays a part in regulating nuclear function. Lamins provide mechanical continuity between cytoskeleton and nuclear interior. Aberrant patterns of lamin expression have been described in cancer; these are not sufficiently specific to be used in histopathological diagnosis, however. Nucleolar size and expression levels of nucleolar proteins have been shown to correlate well with proliferative activity, which may revitalize interest in nucleolar organizing regions as a tool in histological diagnosis of cancer. The fibrillogranular network is involved in functional compartmentalization of replication and transcription. A variety of nuclear matrix proteins has been described, which appear to be specifically expressed in cancer cells. Analysis of expression of these proteins might play a significant role in cancer diagnosis.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 28 (1994), S. 216-225 
    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
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 15 (1983), S. 189-200 
    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
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  • 8
    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
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 21 (1989), S. 629-633 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 25 (1993), S. 469-477 
    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
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