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  • 1
    ISSN: 1524-475X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Smad3 is involved in mediating intracellular signaling by members of the transforming growth factor-β superfamily and plays a critical role in the cellular proliferation, differentiation, migration, and elaboration of matrix pivotal to cutaneous wound healing. Cross-talk between Smad3 and hormone signaling in vitro has been suggested as an important control mechanism regulating cell activities; however, its relevance in vivo is unknown. Here we report that Smad3 plays a role in androgen-mediated inhibition of wound healing but not in the responses to estrogen modulation in vivo. Both wild-type and Smad3 null female mice exhibited delayed healing following ovariectomy, which could be reversed by estrogen replacement. By contrast, castration accelerated healing in wild-type male mice and was reversible by exogenous androgen treatment. Intriguingly, modulation of androgen levels resulted in no discernible perturbation in the healing response in the Smad3 null mice. Mutant monocytes could be lipopolysaccharide stimulated to produce specific pro-inflammatory agents (macrophage monocyte inhibitory factor) in a fashion similar to wild-type cells, but exhibited a muted response to androgen-mediated stimulation while maintaining a normal response to estrogen-induced macrophage inhibitory factor inhibition. These data suggest that Smad3 plays a role in mediating androgen signaling during the normal wound healing response and implicate Smad3 in the modulation of inflammatory cell activity by androgens. (WOUND REP REG 2003;11:468–473)
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 44 (1990), S. 229-239 
    ISSN: 0730-2312
    Keywords: adrenocortical carcinoma cells ; protein purification ; anchorage independent growth ; epithelial cell proliferation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A polypeptide growth factor has been partially purified from medium conditioned by the human adrenocortical carcinoma cell line SW13. This factor, designated h-TGFe, stimulates anchorage-independent growth of the SW13 cells. Similar activity was observed in human milk, and in conditioned media from seven of 14 epithelial cell lines. The SW13-derived activity is stable to low pH and 8M urea but labile to dithiothreitol and 2% sodium dodecyl sulfate. Human TGFe does not bind to heparin and fails to stimulate growth of endothelial cells in monolayer culture. The apparent molecular weight of h-TGFe is 59k by size exclusion chromatography in the presence of 8M urea and the activity binds strongly to cation exchangers. The activity elutes at 15-30% acetonitrile from a C18 reversephase column and has been partially purified by using a four-step chromatographic procedure. TGFe appears to be a novel growth factor produced by many epithelial cells and tissues.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 126 (1986), S. 312-318 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Several growth factors implicated in the process of cellular transformation were tested for their ability to induce anchorage-independent (AI) growth of primary rat embryo (RE) cells. Our results show that in the presence of 10% calf serum, platelet-derived growth factor (PDGF), 1-30 ng/ml, has the strongest effect of all growth factors tested on Al growth. Type-β transforming growth factor (TGF-β), by itself, does not stimulate Al growth, and it inhibits the PDGF-induced colony formation in a dose-dependent manner (ED50 ∼ 0.03 ng/ml). Qualitatively similar responses are obtained by using an established line of fibroblasts, NIH 3T3 cells; the principal difference between the response of the primary cells and the established cell line is in colony-forming efficiency in soft agar culture (15% and 90%, respectively, for growth of colonies 〉 1,500 μm2 diameter in the presence of 10 ng/ml PDGF). Since Al growth has been shown to correlate well with tumorigenicity in vivo, our results suggest that the transforming potential of PDGF in an appropriate responsive cell can be controlled not only through its interaction with its own receptor, but also by the presence of inhibitory factors such as TGF-β.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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