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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Experimental Cell Research 114 (1978), S. 1-14 
    ISSN: 0014-4827
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1 DNA levels of SV40 transformed human fibroblasts Days of culture 0 1 2 3 Control (ng DNA per plate) 11.06 24.89 51.86 99.57 Dexamethasone (ixg DNA per plate) 10"7M 106N 25.58 52.55 98.88 23.51 48.40 102.33 Cells were grown as described in Fig. 1 and DNA assay was performed as ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 307-322 
    ISSN: 0091-7419
    Keywords: myoblast differentiation ; Con-A ; extracellular filamentous matrix ; insulin ; dexamethasone ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Myoblasts are mononucleated cells and associated with differentation undergo cell fusion and become multinucleated. The current studies have examined cell surface dynamic changes of Concanavalin A lectin receptor mobility and the role of hormones in modulating myoblast differentiation. A uniform distribution of Con-A receptors is observed in undifferentiated cells when reacted with Con-A at 37°C. Cells from differentiating cultures or fully differentiated myotubes reacted similarly at 37°C show a significant redistribution of Con-A into patches, “caps,” and endocytic vesicles containing Con-A. If undifferentiated and differentiated cells are first prefixed with glutaraldehyde then reacted with Con-A continuous distribution of Con-A is seen across the cell surface. This suggests redistribution of Con-A and its receptors occurs in differentiated cells reacted with lectin at 37°C. It is further shown that insulin (10 μg/ml) significantly enhances myoblast differentiation but that this occurs after an apparent stimulation of proliferation. In contrast to insulin, dexamethasone (10 μM and 100 μM) profoundly inhibits myoblast differentiation while having different effects on proliferation; 10 μM dex stimulates cell growth while 100 μM dex suppresses cell proliferation. Lastly, an extracellular filamentous matirix which binds Con-A is observed at the ultrastructural level in high density cultures. No significant redistribution of Con-A is observed on this matrix in distinction to the redistribution observed on the cell membrane in differentiated cells.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0091-7419
    Keywords: human fibroblast ; ascorbate ; procollagen ; fibronectin ; axial periodicity ; native collagen fibrils ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin and collagens are major constituents of the cell matrix of fibroblasts. Fibronectin is a 220,000 dalton glycoprotein that mediates a variety of adhesive functions of cells examined in vitro. Fibronectin is secreted in a soluble form and interacts with collagen to form extracellular filaments. Fibronectin and procollage type I were localized using the peroxidase anti-peroxidase method. Under standard culture conditions, fibronectin and procollagen were localized to non-periodic 10 nm extracellular fibrils, the cell membrane and plasma membrane vesicles. Ascorbate treatment of cells leads to a new larger fibril with a diameter of approximately 40 nm. Antibodies to fibronectin and procollagen I react to these native collagen fibrils with an axial periodicity of approximately 70 nm. Fibronectin is clearly associated with native collagen fibrils produced by ascorbate treated cells and there is an asymetric distribution or segregation of fibronectin on these collagen fibrils with a 70 nm axial repeat.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
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