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  • 1980-1984  (3)
  • Caldesmon  (2)
  • Intestinal epithelium  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Immunocytochemical demonstration of caldesmon (a calmodulin-binding, F-actin-interacting protein) in smooth muscle fibers and absorptive epithelial cells in the small intestine of the rat (1984)
    Springer
    Cell & tissue research 235 (1984), S. 207-209 
    Details
    ISSN: 1432-0878
    Keywords: Caldesmon ; Actin ; Immunocytochemistry ; Small intestine ; Smooth muscle ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of caldesmon (a calmodulin-binding, F-actin-interacting protein) (Sobue et al. 1982) and of actin was studied in the rat's small intestine by means of light-microscopic immunocytochemistry. Positive immunostaining for caldesmon was seen in smooth muscle cells of the intestinal wall, and of blood vessels, and in the apical portion of the absorptive epithelial cells. The immunoreactivity in goblet cells was difficult to recognize. The positive reaction to immunostaining for actin showed almost the same pattern as that for caldesmon. These results suggest that this calmodulin-binding protein may play an important role in the control of actin-myosin interaction in smooth muscle cells and in non-muscle cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213742
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical demonstration of caldesmon and actin in thyroid glands of rats (1984)
    Springer
    Cell & tissue research 237 (1984), S. 375-377 
    Details
    ISSN: 1432-0878
    Keywords: Thyroid ; Immunocytochemistry ; Caldesmon ; Actin ; Endocytosis ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of caldesmon (a calmodulin-binding, F-actin interacting protein; Sobue et al. 1982) and actin was studied in the rat thyroid gland by means of light-microscopic immunocytochemistry, and the fine-structural distribution of actin filaments was examined by use of heavy meromyosin (HMM). Caldesmon and actin were demonstrated in the apical cytoplasm of almost all the follicle epithelial cells in normal as well as TSH-treated animals. Immunoreactivities for both caldesmon and actin showed almost the same pattern in localization. The smooth muscle cells of the blood vessels were also positive for caldesmon and actin. By electron microscopy, numerous actin filaments decorated by HMM and running perpendicularly or randomly to the apical surface were recognized in the apical cytoplasm of the follicle epithelial cell. These results suggest that caldesmon and actin, in conjugation with calmodulin, play a role in the regulation of cellular activity such as exocytosis and endocytosis in the apical portion of the follicle epithelial cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217161
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Effects of tunicamycin on thin-section and freeze-fracture images of microvilli of the duodenal epithelial cells of the mouse (1984)
    Springer
    Cell & tissue research 238 (1984), S. 653-656 
    Details
    ISSN: 1432-0878
    Keywords: Tunicamycin ; Glycoprotein ; Intestinal epithelium ; Microvilli ; Freeze-fracture ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of tunicamycin, which is known to inhibit the synthesis of N-linked glycoprotein, on the duodenal absorptive epithelial cell of the mouse was studied in thin-section as well as freeze-fracture images. In tunicamycin-treated animals, the apical part of the epithelial cell was almost negative to the PAS reaction. Moreover, microvilli of the epithelial cell became shorter, larger in diameter, and fewer in number in tunicamycin-treated mice. In addition, freeze-fracture images revealed that the population density of membrane particles of the microvillus membrane was lowered by tunicamycin treatment. These results may indicate that the inhibition of synthesis of N-linked glycoprotein causes a decrease of membrane supply from the Golgi apparatus to the apical plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219885
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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