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  • 1
    Electronic Resource
    Electronic Resource
    Ultrastructural and immunohistochemical studies on non-ciliated cells of the tracheal epithelium of normal, phenobarbital-treated, and 3-methylcholanthrene-treated mice (1985)
    Springer
    Cell & tissue research 240 (1985), S. 501-504 
    Details
    ISSN: 1432-0878
    Keywords: Non-ciliated tracheal cell ; Smooth endoplasmic reticulum ; Ultrastructure ; Cytochrome P-450 ; Immunohistochemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Non-ciliated SER-rich cells of the tracheal epithelium of normal, phenobarbital-treated and 3-methylcholanthrene-treated mice were studied ultrastructurally and immunohistochemically. The apical portion of these cells protrudes into the tracheal lumen, especially in the mice treated with the two compounds, and the apical cytoplasm is filled with numerous tubular elements of SER. Besides, the non-ciliated cells of 3-methylcholanthrene-treated mice show a strong positive reaction to the antiserum against microsomal cytochrome P-450 of liver. These findings support the concept that the non-ciliated tracheal cell may be involved in the metabolism of endogeneous and exogeneous chemical compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00222368
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    Paper (German National Licenses)
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  • 2
    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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  • 3
    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)
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrastructural and immunohistochemical studies on steroid-secreting cells of the testis and ovary of normal and 3-methylcholanthrene-treated mice (1986)
    Springer
    Cell & tissue research 245 (1986), S. 681-683 
    Details
    ISSN: 1432-0878
    Keywords: Smooth endoplasmic reticulum ; Cytochrome P-450 ; Testis ; Ovary ; Immunohistochemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The testis and ovary of normal and 3-methylcholanthrene-treated mice were studied ultrastructurally and immunohistochemically in order to learn whether steroid-secreting cells of the gonads are involved in drug metabolism. The steroid-secreting cells, i.e., Leydig cells of the testis, and theca interna cells, interstitial gland cells, and corpus luteum cells of the ovary of 3-methylcholanthrene-treated mice, show a strong positive reaction to the antiserum against, hepatic microsomal cytochrome P-450, of liver which is the terminal oxidase of the drug-metabolizing enzyme complex. In addition, it was found that elements of smooth endoplasmic reticulum (SER) in drug-treated mice become well developed as compared with those in control animals. These findings indicate that the steroid secreting cells in testis as well as ovary are involved in the metabolism of both endogenous and exogenous chemical compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218572
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    Paper (German National Licenses)
    Fulltext
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