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  • 1
    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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  • 2
    ISSN: 1432-069X
    Keywords: Chondroitin proteoglycan ; Basement membrane ; Skin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Basement membranes are complex extracellular matrices present at epithelial/mesenchymal interfaces of tissues. The dermal-epidermal junction has been shown to contain numerous components, some of the most well known being laminin, types IV and VII collagens, heparan sulfate proteoglycan, fibronectin, and entactin/nidogen. In this paper we show, using core protein-specific antibodies, the presence of a newly described basement membrane-specific chondroitin sulfate proteoglycan at the epithelial/ mesenchymal interface of adult rat skin. Ultrastructurally, this antigen was proven to reside primarily within the basal lamina, apparently concentrated in the lamina densa. In addition, some of the proteoglycan was also present beneath the lamina densa, associated with the reticular lamina collagen fibrils.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Entomologia experimentalis et applicata 25 (1979), S. 9-15 
    ISSN: 1570-7458
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Der Einfluss der Parasitierung durch den Parasitoiden Diaeretiella rapae auf die Futteraufnahme von Brevicoryne brassicae wurde mit Hilfe ausgeschnittener, mit Radiophosphor behandelter Blätter studiert. Während der ersten Phase, wenn das Ei und die Embryonalstadien des Parasitoiden vorhanden sind, bleibt die Futteraufnahme unverändert. Dagegen fällt sie auf ein gesicher niedrigeres Niveau als bei nichtparasitierten Blattläusen während des ersten Larvenstadiums des Parasitoiden (48 h). Dies ist eine Folge der aktiven Futteraufnahme des Parasitoiden. Während des zweiten Larvenstadiums des Parasitoiden steigt die Futteraufnahme des Wirts wieder an und zwar auf das Niveau nichtparasitierter Blattläuse. Das zweite Larvenstadium des Parasitoiden ist ein Ruhestadium und ernährt sich von flüssigen und halbflüssigen Nährstoffen. Während des dritten Larvenstadiums des Parasitoiden fällt die Futteraufnahme des Wirts und der Tod tritt während des vierten Larvenstadiums des Parasitoiden ein.
    Notes: Abstract The food uptake by Brevicoryne brassicae, as measured by accumulation of radiophosphorus, is influenced by the presence of developing larvae of the parasitoid Diaeretiella rapae. Though the egg and embryonic stages of the parasitoid have no effect on host feeding the presence of a first-instar larva lowers the food uptake. Feeding returns to a level similar to that of non-parasitised aphids when a second-instar parasitoid is present within a host, but drops again when the third instar is reached. Host death occurs during the fourth-larval instar.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 4 (1983), S. 647-661 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The roles of the microfilament-associated proteins vinculin, α-actinin, myosin and filamin have been studied by immunofluorescence and double fluorescence in conjunction with interference reflection microscopy (IRM), during the development of focal contacts and focal adhesions in a chick fibroblast system which initially has no such adhesion specializations but then develops them sequentially over a 48 h period. Without exception, all focal contacts and focal adhesions contain both vinculin and α-actinin at every stage that we can detect by IRM or by double staining to reveal the associated microfilament bundles. Indeed the appearance of small bodies containing α-actinin and vinculin is shown to precede focal contact formation in our model system and such structures (not visible by IRM) are proposed to be the precursors of focal contacts and adhesions. Myosin and filamin are distributed generally with some reticular patterning in the early motile cells which lack the focal specializations, but as focal contacts and adhesions form these proteins become progressively recruited into the associated microfilament bundles. Only then do we see the marked depletion that has been reported earlier of diffusely distributed myosin and filamin in the leading lamella. Although this is not initially associated with any change in the motile status of the cells, the recruitment of these microfilament-associated proteins into stress fibres is proposed to occur in preparation for anchorage and bracing of cells to the substratum when they later become stationary.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 1 (1980), S. 5-14 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The organization of the principal cytoskeletal components (actin, tubulin and 10 nm filament protein) have been compared by immunofluoresence microscopy in two populations of chick heart fibroblasts, previously shown to be adapted respectively for rapid, directed migration or adhesion and growth. We find that neither microtubule nor 10 nm filament distributions alter significantly during the conversion from the migratory to the stationary state but in contrast there are significant differences in the organization of actin. The stationary cells possess more numerous and thicker stress fibre bundles. The variety of patterns observed in the migratory cells are documented and the possible roles of the different components of the cytoskeleton in cell locomotion are discussed.
    Type of Medium: Electronic Resource
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