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  • Glycoprotein  (1)
  • Immunohistochemistry  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 266 (1979), S. 295-310 
    ISSN: 1432-069X
    Keywords: Fibronectin ; Skin ; Basement membranes ; Immunohistochemistry ; Electron microscopy ; Fibronectin ; Haut ; Basalmembran ; Immunohistochemie ; Elektronenmikroskopie
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Verteilung des extracellulären Glykoproteins Fibronectin im Haut- und Zungengewebe der Ratte wurde unter Verwendung von spezifischem Antiserum licht- und elektronenmikroskopisch mit Hilfe der Immunofluorescenz- und Immunoperoxidasemethoden untersucht. Aus den Ergebnissen schließen wir, daß Fibronectin weder in stabilen, differenzierten Gewebeteilen wie Talgdrüsen, Matrix, Mark, Rinde oder Cuticula des Haares oder der inneren und äußeren Haarwurzelscheide, noch in Geweben, in denen die Zellen zum Teil beweglich sind (z. B. Epidermis), vorkommt. Es ist aber charakteristisch für Zonen, wo Zellteilung in Berührung mit einem extracellulären Gerüst vor sich geht, wie z. B. an einer Basalmembran oder in lockerem Bindegewebe. Auffallende Beispiele waren die mit Follikelepithelien verbundene Hyalinmembran und Bindegewebsscheide, die unter Gefäßendothelzellen liegende Basalmembran, die Bindegewebe, welche die Nerven- und Muskelfaserbündel umgeben und durchsetzen und das Bindegewebe der Dermis. Im letzteren Falle war das Fibronectin oft mit Kollagenfasern eng verbunden. In der Basalmembran an der Grenze zwischen Dermis und Epidermis war Fibronectin an der Plasmamembran der basalen Zellen und im Gebiet der Lamina lucida zu finden. Es bestand kein Zusammenhang mit spezifischen Stellen der Zellen-Substrat-Adhäsion wie den Hemidesmosomen. Das endoplasmatische Reticulum der Fibroblaste ließ sich stark färben — ein Hinweis, daß diese Zellen einen wichtigen Ort der Synthese darstellen.
    Notes: Summary Specific antiserum was used to investigate the distribution of the extracellular glycoprotein, fibronectin, in rat skin and tongue tissue by light and electron microscopy with immunofluorescence and immunoperoxidase techniques. We conclude that fibronectin is absent from stable, differentiated parts of tissues, such as the sebaceous glands or the matrix, medulla, cortex, and cuticles of the hair and the inner and outer root sheaths, or even in tissues in which there is some cell movement, such as the epidermis. It is, however, characteristic of sites at which cell division is occurring in contact with an extracellular scaffolding, such as basement membrane or loose connective tissue. Conspicuous examples were in the glassy membrane and connective tissue sheath associated with the follicular epithelium, the basement membrane underlying vascular endothelial cells, the connective tissues surrounding and investing nerve and muscle fibre bundles, and the dermal connective tissue where fibronectin was often associated closely with collagen fibres. At the basement membrane of the dermal/epidermal junction, fibronectin occurred at the plasma membrane of the basal cells and in the lamina lucida area. There was no correlation with specific areas of cell-substrate adhesion, such as the hemidesmosomes. The endoplasmic reticulum of fibroblasts stained strongly suggesting that these cells represent a major site of synthesis.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-069X
    Keywords: Entactin ; Basement membrane ; Immunoelectron microscopy ; Glycoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Entactin is a recently described sulfated glycoprotein component of mouse endodermal cell-derived extracellular matrix and is present in a number of basement membranes. It has been ultrastructurally localized to both lamina densa and adjacent epithelial cell membranes in rodent kidney. In the present study, we have sought to determine the localization of entactin in mouse skin. Indirect immunofluorescence and immunoelectron microscopy (the latter via immunoperoxidase technique) were performed on both intact and NaCl-separated mouse skin, using a well-characterized IgG class entactin-specific ratxmouse monoclonal antibody. At the light microscopic level, entactin was present in all skin basement membranes. On NaCl-split skin, staining was noted solely on the dermal portion. At the electron microscopic level, in intact skin, entactin was primarily localized to the lamina densa and adjacent upper papillary dermis. However, smaller amounts of immunoreaction products were also detectable within the lamina lucida and in close apposition to overlying hemidesmosomes. In partially separated skin, immunoreactants were similarly noted above the level of the lamina densa. However, in completely separated areas, hemidesmosomal or cell membrane staining was no longer visible. We conclude that entactin is an ubiquitous component of mouse skin basement membranes. Similar to previous findings in rodent kidney, entactin is present in multiple regions of skin basement membrane, although its primary localization remains within and directly beneath the lamina densa.
    Type of Medium: Electronic Resource
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