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  • 1
    Electronic Resource
    Electronic Resource
    Microthread-like filaments connecting the epithelial basal lamina with underlying fibrillar components of the connective tissue in the rat trachea (1985)
    Springer
    Cell & tissue research 239 (1985), S. 485-495 
    Details
    ISSN: 1432-0878
    Keywords: Trachea ; Basal lamina ; Anchoring fibril ; Ruthenium red-positive filaments ; New anchoring device ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The structural relationship between the basal lamina and the underlying reticular tissue was studied, with special attention to the relationship among basal lamina-associated anchoring fibrillar (AF) arcs (Kawanami et al. 1978, 1979) and other fibrillar components, in the epithelium-denuded trachea of the rat. Quantitative analysis of a large number of AF arcs reveals that the majority of the AF arcs has no other fibrillar components of passage. This suggests that most AF arcs do not serve as a real anchoring device, connecting the basal lamina with the underlying reticular tissue, as has so far been suggested by Kawanami et al. (1978). Ruthenium-red staining reveals the presence of a unique meshwork of microthread-like filaments connecting the undersurface of the basal lamina or the AF arcs with the underlying fibrillar components with a remarkable continuity, suggesting that the filaments act as a real anchoring device; these filaments link, instead of the AF arcs, the basal lamina, to the subjacent reticular tissue. Various enzymatic treatments of the filaments indicate that their chemical nature is probably non-collagenous (glyco)protein without glycosaminoglycan moieties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219226
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  • 2
    Electronic Resource
    Electronic Resource
    APUD-type recepto-secretory cells in the chicken lung (1979)
    Springer
    Cell & tissue research 201 (1979), S. 197-205 
    Details
    ISSN: 1432-0878
    Keywords: Avian lung ; Pulmonary receptor ; APUD endocrine cells ; Monoamine histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The epithelium of the intrapulmonary airways of the chicken lung has been studied by fluorescence and electron microscopy. Numerous intensely yellow-fluorescent cells occur in the epithelium of the primary and secondary bronchi. The cell cytoplasm contains characteristic granular vesicles with an electron-dense central core. The vesicles react positively to chromaffm and argentaffin treatment, indicating that they are possible storage sites for amines. Synapse-like junctions occur between the granular cells and the intraepithelial nerve endings, filled with numerous mitochondria, suggesting that these granular cells may have a dual function as both receptor and endocrine cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00235057
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  • 3
    Electronic Resource
    Electronic Resource
    Rat intestinal galactoside-binding lectin L-36 functions as a structural protein in the superficial squamous cells of the esophageal epithelium (1995)
    Springer
    Cell & tissue research 281 (1995), S. 77-83 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Esophagus ; Epithelial cells ; Intestinal lectin ; L-36 ; RI-H fragment ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Using an affinity purified antibody raised against the RI-H fragment of rat intestinal lectin L-36, the latter protein has been identified within the esophageal epithelium by means of ultracryotomy followed by immunogold labeling. The epithelium consists of 4 morphologically distinct cell-types, namely, the basal, spiny, granular and squamous cells, and each of these exhibits a different immunolabeling pattern. The basal cells form a layer on the basal lamina, and in these a diffuse cytoplasmic staining is observed. This basal cell layer is overlaid by spiny cells that extend many cell processes into wide intercellular spaces. In these cells, immunogold particles are found only on small granular inclusions consisting of an electron-lucent homogeneous substance. The granular cells form a third layer over the spiny cells, and are characterized by a number of large granular inclusions with an electron-dense core rimmed by a less electron-dense substance. Immunogold labeling is found on these granules, both on the core and peripheral region. Squamous cell-types constitute the most superficial layer of the epithelium. They are without granular inclusions, and immunogold labeling is confined to the cytoplasmic surface of the thickened plasma membrane. These findings suggest that L-36 is produced in the basal cells as free cytosolic protein, then becomes progressively aggregated into the granular inclusions of the spiny and granular cells, and is eventually transferred onto the cytoplasmic surface of the squamous cell plasma membrane where it may interact with complementary glycoconjugate(s) located at this site. The membrane lining substance thus formed may play a role in stabilizing the squamous cell membranes, thereby maintaining the structural integrity of the epithelium against mechanical stress coming from the esophageal lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307960
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  • 4
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of 14 kDa β-galactoside-binding lectin in various organs of rat (1990)
    Springer
    Cell & tissue research 259 (1990), S. 43-49 
    Details
    ISSN: 1432-0878
    Keywords: Lectin ; Smooth muscle cells ; Immunohistochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunohistochemical localization of 14 kDa β-galactoside-binding lectin in various organs of adult rat was achieved using a monospecific antibody raised against lectin purified from rat lung. The antibody-stained cells were formed into small aggregates, thin fascicles, or thick bundles in the walls of blood vessels, gastrointestinal tracts and urogenital organs. From the patterns of distribution, as well as their organization, these immunoreactive cells were regarded as smooth muscle cells. This was confirmed by a double immunofluorescence study using a mixture of anti 14 kDa lectin and anti α-smooth muscle-specific actin antibodies. Strong 14 kDa lectin immunoreactivity was seen in the pericellular matrix of smooth muscle cells in intact organs as well as in detergent-treated organs from which all cellular components were extracted. From these findings, it is suggested that the 14 kDa lectin may be externalized by smooth muscle cells into their pericellular matrix and participate in the crosslinking of the complementary glycoconjugate(s) localized at that site. The macromolecular complex of glycoconjugates thus formed around smooth muscle cells may play a role in anchoring smooth muscle cells to the pericellular connective tissue thereby permitting the force of muscle contraction to be efficiently transmitted to the surrounding connective tissue proper.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571428
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  • 5
    Electronic Resource
    Electronic Resource
    Rat intestinal galactoside-binding lectin L-36 functions as a structural protein in the superficial squamous cells of the esophageal epithelium (1995)
    Springer
    Cell & tissue research 281 (1995), S. 77-83 
    Details
    ISSN: 1432-0878
    Keywords: Esophagus ; Epithelial cells ; Intestinal lectin, L-36 ; RI-H fragment ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Using an affinity purified antibody raised against the RI-H fragment of rat intestinal lectin L-36, the latter protein has been identified within the esophageal epithelium by means of ultracryotomy followed by immunogold labeling. The epithelium consists of 4 morphologically distinct cell-types, namely, the basal, spiny, granular and squamous cells, and each of these exhibits a different immunolabeling pattern. The basal cells form a layer on the basal lamina, and in these a diffuse cytoplasmic staining is observed. This basal cell layer is overlaid by spiny cells that extend many cell processes into wide intercellular spaces. In these cells, immunogold particles are found only on small granular inclusions consisting of an electron-lucent homogeneous substance. The granular cells from a third layer over the spiny cells, and are characterized by a number of large granular inclusions with an electron-dense core rimmed by a less electron-dense substance. Immunogold labeling is found on these granules, both on the core and peripheral region. Squamous cell-types constitute the most superficial layer of the epithelium. They are without granular inclusions, and immunogold labeling is confined to the cytoplasmic surface of the thickened plasma membrane. These findings suggest that L-36 is produced in the basal cells as free cytosolic protein, then becomes progressively aggregated into the granular inclusions of the spiny and granular cells, and is eventually transferred onto the cytoplasmic surface of the squamous cell plasma membrane where it may interact with complementary glycoconjugate(s) located at this site. The membrane lining substance thus formed may play a role in stabilizing the squamous cell membranes, thereby maintaining the structural integrity of the epithelium against mechanical stress coming from the esophageal lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307960
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    A scanning and transmission electron-microscopic study on neuro-epithelial bodies in the neonatal mouse lung (1981)
    Springer
    Cell & tissue research 216 (1981), S. 481-490 
    Details
    ISSN: 1432-0878
    Keywords: Neonatal mouse lung ; SEM and TEM ; Neuro-epithelial bodies ; Pulmonary receptor ; Local endocrine organ
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Neuro-epithelial bodies (NEBs) in the neonatal mouse lung have been studied by transmission (TEM) and scanning (SEM) electron microscopy. The TEM appearance of mouse NEBs is in agreement with previous descriptions (Wasano 1977). In SEM, NEBs are easily identified as island-like, half-spherical epithelial protrusions whose surface structure is obviously different from that of the surrounding ordinary respiratory epithelium. Their surfaces are devoid of ciliated cells and are covered by flattened, irregular-contoured Clara cells and the apical surfaces of NEB cells. The latter are singly dispersed among the modified Clara cells, and the apical surface structure consists of characteristic microvillous projections. The SEM also reveals that most of the NEBs (86%) are preferentially located at the branching points of the intrapulmonary airways. The unique surface structure of NEBs, as well as their strategic location at the branching points of airways, gives support to the suggestion that NEBs might function not only as an intrapulmonary chemoreceptor, but also as a local endocrine organ regulating the air-flow and/or blood-flow dynamics in the specific peripheral regions of the lung.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00238645
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  • 7
    Electronic Resource
    Electronic Resource
    Immunolocalization of 67 kDa elastin-binding protein in perinatal rat lungs (1992)
    Springer
    Cell & tissue research 268 (1992), S. 277-281 
    Details
    ISSN: 1432-0878
    Keywords: Lung ; Elastin-binding protein ; Lectins ; Galactose ; Monocytes ; Immunocytochemistry ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 67 kDa elastin-binding protein (RL-67EBP) has been isolated from neonatal rat lungs by the use of an elastin-coupled affinity column, followed by elution with either lactose or synthetic elastin hexapeptide (VGVAPG), and immunohistochemistry has been used on perinatal rat lungs to determine the tissue localization of this protein. No immunoreactive structures occur in fetal lungs, or in the lungs of day-1 and-4 neonates. On day-7 after birth, immunoreactive cells appear in the subepithelial connective tissue of the intrapulmonary airways, from day-10 on, these cells become evenly distributed in the alveolar parenchyma. Occasionally, some cells occur in the alveolar air space, being free from the surface of the alveolar septum. Unpermeabilized cells obtained by bronchoalveolar lavage, show cell surface immunoreactivity, indicating that RL-67EBP is expressed on the surface membrane of the cells. From these findings, it is suggested that the immunoreactive cells are blood-borne monocytes, and that RL-67EBP may function as an elastin peptide receptor by which monocytes mobilize through interstitial connective tissue during their migration from blood to alveolar air space, where they eventually differentiate into alveolar macrophages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318796
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  • 8
    Electronic Resource
    Electronic Resource
    Monoamine-containing granulated cells in the frog lung (1978)
    Springer
    Cell & tissue research 193 (1978), S. 201-209 
    Details
    ISSN: 1432-0878
    Keywords: Frog lung ; Pulmonary receptor ; Biogenic amines ; APUD endocrine system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The epithelium of the primary bronchus of the frog lung has been studied by fluorescence and electron microscopy. Clusters of five to ten, ovoid, brilliantly yellow fluorescent cells were observed in the basal portion of the epithelium. These cells contained numerous electron-dense granules of variable shape and size. The granules gave a positive argentaffin reaction at the ultrastructural level, suggesting a possible existence of monoamines in the granules. In addition, synaptic contact between the intraepithelial nerves and the cells, which was characterized by the aggregation of the granules toward the presynaptic membrane thickening of the cell, was also noted. These data are discussed in relation to similar studies in birds and mammals, and a possible function of these cells suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00209034
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  • 9
    Electronic Resource
    Electronic Resource
    Lectin-gold cytochemistry of mucin oligosaccharide biosynthesis in golgi apparatus of airway secretory cells1Mucin-secreting cells in the surface epithelium of the hamster trachea do not have a goblet shape, and whether the mucin produced by these cells is to be classified as “mucous” or “serous” is not known. The term airway secretory cell is therefore tentatively used in this report of the hamster (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 221 (1988), S. 635-644 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: To elucidate the mechanism for the biosynthesis of O-linked mucin oligosaccharides, airway secretory cells of the hamster trachea were embedded in Lowicryl K4M resin, and section were examined by lectin-gold cytochemistry with special attention focused on the Golgi apparatus. The interrelations between the Golgi cisternae stained with five different lectins were determined by double-staining procedures using various combinations of lectins conjugated with 14-nm and 8-nm colloidal gold. Several cis cisternae were stained only with HPA (Helix pomatia aggulutinin specific for terminal α-N-acetylgalactosamine). The next medial cisternae were not stained with HPA. but reacted positively with two lectins, GSII (Griffonia simplicifolia agglutinin II specific for terminal α- or β-N-acetlyglucosamine) and RCAI (Ricinus communis agglutinin I specific for β-galactose). The transcisternae as well as condensing and mature secretory granules were labeled with four lectins, UEAI (Ulex europaeus aggulutinin I specific for terminal α-L-fucose) and LFA (Limax flavus aggulutinin specific for terminal N-acetyl or N-glycolyl neuraminic acid) in addition to HPA and RCAI. The same number of trans cisternae were positive to HPA and UEAI, whereas LFA bound to a few transmost cisternae but fewer than were stained with HPA or UEAI. The observed sequential appearance of different sugar residues in different levels of Golgi cisternae (from cis to trans cisternae) coincides quite well with the sugar sequence of airway mucin oligosaccharide (from reducing to nonreducing ends) proposed by biochemical analysis. It is suggested that airway mucin oligosaccharides elongate during a vectorial movement through the Golgi stack from cis toward trans and that the stack consists of at least three functionally distinct segments, cis, medial, and trans; in these three segments there take place, respectively, the initial O-glycosylation of mucin core peptide, the formation of a core region of oligosaccharide chain, and the completion of chain growth by addition of terminal sugar moieties.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092210209
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