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  • 2020-2021
  • 1995-1999  (6)
  • 1980-1984  (12)
  • 1
    Electronic Resource
    Electronic Resource
    Ecto-5′-nucleotidase is expressed by pericytes and fibroblasts in the rat heart (1995)
    Springer
    Histochemistry and cell biology 103 (1995), S. 227-236 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Ecto-5′-nucleotidase is anchored at the outer surface of cell membranes and thus its reaction product adenosine is released into the extracellular space. Extracellular adenosine displays via specific receptors a wide range of physiological effects in heart. There are discrepancies in the literature concerning the distribution of ecto-5′-nucleotidase in heart. Since we suspected that these may be due to technical problems, in the present study on ecto-5′-nucleotidase in rat heart we attempted to circumvent some technical pitfalls. Good preservation of the tissue with open capillary lumina, providing a clear identification of endothelium, was obtained by perfusion fixation. At the light microscopic level, the distribution of ecto-5′-nucleotidase studied by enzyme histochemistry and immunohistochemistry using a monoclonal and a polyclonal antibody yielded congruent results. The enzyme was rather homogeneously distributed throughout the myocardium, with a slightly higher incidence of stained cells in the outer thirds than in the inner third of the wall. Consistently high levels of ecto-5′-nucleotidase were seen only in interstitial cells. The walls of large vessels and heart muscle cells were constantly negative for ecto-5′-nucleotidase. The endothelia of capillaries were mostly negative but a few profiles occasionally displayed a weak immunoreaction. The interstitial cells staining positive for ecto-5′-nucleotidase could be identified as pericytes and as fibroblasts according to their shapes and localizations. The immunoreactivity of fibroblasts was confirmed by electron microscopy. These data indicate that adenosine may be formed extracellularly in the interstitium of the myocardium, where it would have direct access to important targets such as myocytes, arterioles and nerve endings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01454028
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  • 2
    Electronic Resource
    Electronic Resource
    The activities of peroxisomal oxidases in periportal and perivenous zones of the rat liver acinus (1980)
    Springer
    Histochemistry and cell biology 69 (1980), S. 95-99 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using a new biochemical microassay the activities of three peroxisomal oxidases in single microdissected periportal and perivenous zones of the liver acinus were measured. Whereas urate oxidase is homogeneously distributed through the acinus, the activities of D-aminoacid oxidase and α-hydroxyacid oxidase are respectively 1.80-and 2.71-fold higher in the periportal hepatocytes than in the perivenous hepatocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00508370
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  • 3
    Electronic Resource
    Electronic Resource
    The cellular specificity of lectin binding in the kidney (1982)
    Springer
    Histochemistry and cell biology 74 (1982), S. 521-530 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In order to estimate the usefulness of lectins in the study of the functional segmentation of the nephron, the sites of binding of five lectins were identified in the rat kidney. Lectin-peroxidase conjugates were applied to cryostat sections. The bound conjugates were stained with 3,3′-diaminobenzidine for light microscopical observation. Each lectin has a specific binding pattern along the nephron. Reversely, the different segments of the nephron defined by other histological methods can be identified on the basis of their affinity for lectins. The different parts of the thick ascending limb, namely the medullary segment, the cortical segment and the macula densa, can be distinguished even more readily with lectin histochemistry than with any other histochemical procedure. The binding of lectins to luminal membranes in some segments indicate the possibility to use lectins for the separation of particular cell types and for the modification of the transport properties of their membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496666
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  • 4
    Electronic Resource
    Electronic Resource
    The cellular specificity of lectin binding in the kidney (1982)
    Springer
    Histochemistry and cell biology 74 (1982), S. 531-540 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In order to estimate the usefulness of lectins in the study of the functional segmentation of the nephron, the sites of binding of four lectins were identified in the rabbit kidney. Lectin-peroxidase conjugates were applied to unfixed cryostat sections. The bound conjugates were stained with 3,3′-diaminobenzidine for light microscopical observation. Each lectin has a specific binding pattern along the nephron. The patterns generally fit in with the segmentation of the nephron established by conventional histology. However in the proximal tubule and in the thick ascending limb the lectin binding suggests functional transitions in histologically homogeneous tubular portions. In contrast to the other cell types of the connecting tubule and of the collecting duct the intercalated cells bind two lectins at their luminal membrane. Segmental differences in the lectin affinity of the basement membrane suggest that this structure has not only mechanical functions. The binding of lectins to luminal membranes in some segments indicate the possibility to use lectins for the separation of particular cell types and for modification of the transport properties of their membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496667
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  • 5
    Electronic Resource
    Electronic Resource
    Distal tubular segments of the rabbit kidney after adaptation to altered Na- and K-intake (1982)
    Springer
    Cell & tissue research 224 (1982), S. 493-504 
    Details
    ISSN: 1432-0878
    Keywords: Na-K-ATPase ; Cell-membrane area ; Renal distal tubule ; Cortical collecting duct ; Mineralocorticoids ; Rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Na-K-ATPase activity was measured in the convoluted part of the distal tubule (DCT), the connecting tubule (CNT) and the cortical collecting duct (CCD). The segments were microdissected from freeze-dried kidney tissue of rabbits adapted to various salt diets and exposed to large differences in endogenous and exogeneous mineralocorticoids. The Na-K-ATPase activity in the DCT is not influenced by mineralocorticoids. They do influence the activity in the CNT and in the CCD. In the CNT the highest activity was found with a low Na-, high K-diet. At the beginning of the CNT the enzyme activity is higher than in the end portion. While canrenoate-K treatment has no effect on Na-K-ATPase activity in the initial portions of the CNT, this drug decreases the Na-K-ATPase activity significantly in the end portion of the CNT. DOCA treatment has a significant effect on the enzyme activity in the CNT only in the end-portion of the segment, but provokes the highest Na-K-ATPase activity in the CCD. The changes in Na-K-ATPase are found to be associated with corresponding changes in the baso-lateral cell-membrane area in the segments affected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213747
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  • 6
    Electronic Resource
    Electronic Resource
    Distal tubular segments of the rabbit kidney after adaptation to altered Na- and K-intake (1982)
    Springer
    Cell & tissue research 224 (1982), S. 469-492 
    Details
    ISSN: 1432-0878
    Keywords: Renal distal tubule ; Cortical collecting duct ; Cell membrane area ; Mineralocorticoids ; K- and Na-adaptation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The baso-lateral cell-membrane area in kidney tubules appears to be associated with the capacity for electrolyte transport; in the rabbit, it decreases from the distal convoluted tubule (DCT-cells) over the connecting tubule (CNT-cells) to the cortical collecting duct (principal cells). Adaptation to low Na-, high K-intake changes this pattern: CNT-cells at the beginning of the connecting tubule have the highest membrane area, which decreases along the segment, but remains two-fold higher than in controls. Principal cells have a four-fold higher membrane area than in controls. Simultaneous treatment with the antimineralocorticoid canrenoate-K inhibits the structural changes in CNT-cells only in end-portions of the connecting tubule and in principal cells. After prolonged high Na-, low K-intake DCT-cells display a two-fold higher membrane area than controls, while CNT-cells and principal cells are not affected. Simultaneous treatment with DOCA does not affect the DCT-cells but provokes a moderate increase in membrane area in CNT-cells, and a 5.5-fold increase in principal cells. The data provide evidence that DCT-, CNT- and principal cells are functionally different cell types. The baso-lateral cell-membrane area, associated with electrolyte-transport capacity, appears to be influenced in DCT-cells mainly by Na-intake, in CNT-cells mainly by K-intake and in part also by mineralocorticoids, and in principal cells mainly by mineralocorticoids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213746
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  • 7
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    Distal tubular segments of the rabbit kidney after adaptation to altered Na- and K-intake (1982)
    Springer
    Details
    Publication Date: 1982-06-01
    Print ISSN: 0302-766X
    Electronic ISSN: 1432-0878
    Topics: Biology , Medicine
    Published by Springer
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  • 8
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    Distal tubular segments of the rabbit kidney after adaptation to altered Na- and K-intake (1982)
    Springer
    Details
    Publication Date: 1982-06-01
    Print ISSN: 0302-766X
    Electronic ISSN: 1432-0878
    Topics: Biology , Medicine
    Published by Springer
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  • 9
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    The cellular specificity of lectin binding in the kidney (1982)
    Springer
    Details
    Publication Date: 1982-12-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 10
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    Ecto-5?-nucleotidase is expressed by pericytes and fibroblasts in the rat heart (1995)
    Springer
    Details
    Publication Date: 1995-03-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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