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  • 1
    Electronic Resource
    Electronic Resource
    Merosin and Laminin (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 580 (1990), 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.1749-6632.1990.tb17936.x
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  • 2
    Electronic Resource
    Electronic Resource
    Basement Membrane Protein Merosin is a New Marker for the Intermediate Trophoblast Cells of Choriocarcinoma and Placenta (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 580 (1990), 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.1749-6632.1990.tb17973.x
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  • 3
    Electronic Resource
    Electronic Resource
    CELL SURFACE AND EXTRACELLULAR MATRIX GLYCOPROTEIN FIBRONECTIN: EXPRESSION IN EMBRYOGENESIS AND IN TERATOCARCINOMA DIFFERENTIATION (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 312 (1978), 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.1749-6632.1978.tb16798.x
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  • 4
    Electronic Resource
    Electronic Resource
    Oncocytic myoepithelioma and pleomorphic adenoma of the salivary glands (1999)
    Springer
    Virchows Archiv 434 (1999), S. 537-546 
    Details
    ISSN: 1432-2307
    Keywords: Key words Salivary gland ; Oncocytic myoepithelioma ; Pleomorphic adenoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Twenty oncocytic myoepitheliomas (MEs) and pleomorphic adenomas (PAs) were composed of interlacing fascicles of swollen spindle-shaped or/and epithelioid oncocytic myoepithelial cells showing intense finely granular immunoreactivity with anti-mitochondrial antibody. Focal vacuolation of the cytoplasm of oncocytic myoepithelial cells and their gradual transition into sebaceous metaplasia were observed in 3 cases. Another unusual feature found in 5 cases was the presence of slit-like adenomatoid spaces lined with double-layered oncocytic myoepithelium closely resembling Warthin’s tumour. The nuclei of oncocytic cells were characterized by enlargement, hyperchromasia and polymorphism, which should not be confused with malignancy. Oncocytic change in myoepithelial cells in MEs and PAs can cause pitfalls in the differential diagnosis of salivary gland tumours. We describe some unusual histological features associated with onococytic metaplasia in benign myoepithelial cell-derived salivary gland tumours, hoping to help to avoid the overdiagnosis of malignancy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050381
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  • 5
    Electronic Resource
    Electronic Resource
    Basement membrane proteins in salivary gland tumours (1992)
    Springer
    Virchows Archiv 420 (1992), S. 425-431 
    Details
    ISSN: 1432-2307
    Keywords: Basement membrane proteins ; Type IV collagen ; Laminin ; Salivary gland tumours ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunohistochemical localization of type IV collagen and laminin in normal salivary glands and in salivary gland tumours of various types was studied using rabbit antisera. In normal salivary glands, type IV collagen and laminin were co-localized in basement membranes surrounding acini, ducts, fat cells and peripheral nerves. In salivary gland tumours, three main patterns of co-expression of these basement membrane proteins were distinguished. Linear basement membrane-like staining was detected in duct-cell-derived benign salivary gland tumours and in acinic cell carcinomas. In invasive lesions, however, these basement membrane proteins were distributed in an irregular, interrupted manner, and in many cases they were completely absent. Both benign and malignant salivary gland tumours which have a prominent myoepithelial cell component display a particular deposition of basement membrane molecules adjacent to the modified myoepithelial cells, and at the margins of extracellular matrix deposits within these tumours.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01600514
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  • 6
    Electronic Resource
    Electronic Resource
    Changes in the distribution of integrins and their basement membrane ligands during development of human thyroid follicular epithelium (1997)
    Springer
    Journal of molecular histology 29 (1997), S. 337-345 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Interactions between cells and basement membrane components are crucial for the regulation of epithelial cell differentiation and polarization. We have studied by immunohistochemical methods the distribution of integrin adhesion proteins and some of their basement membrane ligands in foetal (16--19 weeks) and adult thyroid follicular epithelia. A diffuse immunoreactivity for only α3, αv and β1 integrins was found in foetal follicular epithelium, whereas in adult follicular epithelium these integrins were expressed basally in a polarized manner. Additionally, β3 integrin was seen in a more basolaterally confined manner in adult follicular epithelium. Among basement membrane components, laminin α1, β1, γ1 and β2 chains were found in epithelial basement membranes of the foetal thyroid gland, suggestive of the presence of laminins-1 and -3. In contrast, the basement membranes of adult follicular epithelium presented a much weaker immunoreactivity for the laminin β2 chain. Furthermore, immunoreactivity for the laminin α2 chain was occasionally seen in adult thyroid glands, apparently confined to myofibroblasts. Immunoreactivity for type IV collagen α1 and α2 (IV) chains was found in follicular basement membranes of foetal as well as adult thyroid gland. The results suggest that during maturation of foetal thyroid follicular epithelium a distinct polarization of integrins takes place. In mature thyroid follicular epithelium, the presumable adhesion-mediating integrin complexes are α3β1, αvβ1 and/or αvβ3 mediating adhesion to laminin-1 (α1-β1- γ1) and type IV collagen trimer α12 (IV)
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026482700109
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  • 7
    Electronic Resource
    Electronic Resource
    Laminins, tenascin and type VII collagen in colorectal mucosa (1996)
    Springer
    Journal of molecular histology 28 (1996), S. 431-440 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of different laminin polypeptides, type VII collagen and tenascin has been studied in adult and foetal colorectal mucosa by using the indirect immunofluorescence technique. Immunoreactivity for laminin α1 chain was located to basement membranes of epithelia, muscularis mucosae, and blood vessels, respectively in different segments of adult colon and rectum. Laminin β1 and γ1 chains were additionally expressed in lamina propria. Laminin α2 chain was also found in lamina propria around the pericyptal fibrollasts. Immunoreactivity for laminin β2 chain was restricted to basement membranes in the muscularis mucosae and arteries. Laminin α3 and β3 chains, suggestive for laminin-5, were confined especially to surface epithelial basement membranes. Immunoreactivity for type VII collagen was confined to basement membrane of surface epithelium in a punctate manner, while that for tenascin was seen slightly more broadly in the basement membrane zone and also in the muscular layer. The distribution of laminin chains in 16-week-foetal colon mostly resembled that of corresponding adult tissue, although immunoreactivities for laminin α2 and β2 chains were lacking. Type VII collagen and the high molecular weight isoform of tenascin also absent from the foetal colon. The results show that the basement membrane of the surface epithelium of colon and rectum express the components of epithelial adhesion complex, laminin-5 (α3-β3-γ2) and type VII collagen, resembling in this respect small intestine and stomach while laminin-2 (α2-β1-γ1) appears to be associated with pericryptal fibroblasts, and laminin-1 (α1-β1-γ1) widely in most basement membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02331434
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  • 8
    Electronic Resource
    Electronic Resource
    Hemidesmosomal Molecular Changes in Dermatitis Herpetiformis; Decreased Expression of BP230 and Plectin/HD1 in Uninvolved Skin (1999)
    Springer
    Journal of molecular histology 31 (1999), S. 109-116 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Recent BP230-knockout experiments with subsequent blistering and recently identified plectin/HD1 mutations in epidermolysis bullosa simplex patients suggest that defective expression of BP230 and plectin/HD1 may predispose to blister formation in human skin. We have studied the expression of the epithelial adhesion complex as well as the basement membrane and anchoring fibril antigens in uninvolved dermatitis herpetiformis skin to find out if alterations can be detected in these structures predisposing to the blister formation typical of the disease. Ten uninvolved dermatitis herpetiformis skin specimens, which all showed clear granular deposits of IgA under the basement membrane in direct immunofluorescence and five normal skin specimens, were studied by indirect immunofluorescence technique. Six uninvolved dermatitis herpetiformis skin specimens showed distinctly decreased immunoreaction for BP230 and four uninvolved dermatitis herpetiformis skin specimens showed distinctly decreased immunoreaction for plectin/HD1. All five skin controls showed strong immunoreactions for BP230 and plectin/HD1. Other hemidesmosomal proteins including BP180 and integrin α6β4, as well as basement membrane proteins laminin-5, laminin-1, nidogen and type IV collagen, and the anchoring fibril protein type VII collagen showed a normal strong expression. Our results suggest that alterations in BP230 and plectin/HD1 may contribute or predispose to blister formation in dermatitis herpetiformis skin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003465820962
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  • 9
    Electronic Resource
    Electronic Resource
    92-kDa type IV collagenase and TIMP-3, but not 72-kDa type IV collagenase or TIMP-1 or TIMP-2, are highly expressed during mouse embryo implantation (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 202 (1995), S. 388-396 
    Details
    ISSN: 1058-8388
    Keywords: Type IV collagenases ; Tissue inhibitors of metalloproteinases (TIMPs) ; Trophoblast ; Embryo implantation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Expression of 72 kDa and 92 kDa type IV collagenases and the metalloproteinase inhibitors TIMPs 1, 2, and 3 was studied by in situ hybridization in implanting mouse embryos of days 5.5 to 7.5. The 92 kDa type IV collagenase was strongly expressed in invading trophoblasts, signals above background not being observed in the embryonic proper or placental tissue. In contrast, signals above background were not seen for the 72 kDa enzyme in any cells of the implantation region, including trophoblasts and stromal cells of the decidual tissue. Only cells in the mucosal stroma outside the decidual region displayed some expression. TIMP-3 was intensily expressed in maternal cells in the area surrounding the invading embryonic tissue. No expression was observed for TIMP-1 or TIMP-2 in the embryo proper, trophoblasts, or the area of the uterine decidual reactin. Weak signals appeared for TIMP-1 only in the circular layer of myometrial smooth muscle and in some uterine stroma cells distant from the site of embryo implantation. The results suggest a central role for 92 kDa type IV collagenase and TIMP-3 in the extracellular proteolysis associated with implantation of the early embryo. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1002020408
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