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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 127 (1986), S. 83-88 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Stimulation of quiescent cultures of AKR-2B cells with transforming growth factor type β (TGFβ) resulted in a transitory increase in actin cytoplasmic poly(A) + RNA. Levels of actin mRNA peaked approximately 4-8 hours subsequent to TGFβ addition and approached basal levels by 24 hours. The accumulation of actin transcripts was dose dependent and insensitive to inhibitors of protein synthesis; 1-3 ng/ml TGFβ induced maximal actin gene expression. Actin isotype-specific probes demonstrated that both β- and γ-cytoplasmic actins are induced by TGFβ.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Nontransformed mouse embryo derived AKR-2B cells stop growing in the G1 phase of the cell cycle at saturation density due to depletion of serum growth factors, whereas a chemically transformed derivative line (AKR-MCA) arrests in G1 at a higher saturation density due to depletion of amino acids and glucose. Stimulation of DNA synthesis is inhibited in the AKR-2B cells, but not in the AKR-MCA cells, by two inhibitors of RNA metabolism, α-amanitin and 5-fluorouridine (5-FU). To determine whether the AKR-MCA cells growth arrest at a uniue point in G1 or whether they arrest in a physiologic state which can also be achieved by the nontransformed cells, AKR-2B cells were maintained in medium with 10% serum containing the mitogens, epidermal growth factor (EGF) or 12-O-tetradecanoylphorbol-13-acetate (TPA), until they reached saturation density or were arrested at subconfluence by artificial deletion of amino acids from the medium. The AKR-2B cells maintained in EGF or TPA stopped growing in G1 at a higher saturation density, due to depletion of amino acids. Cells arrested in EGF or TPA or in amino acid deficient medium had a shortened interval between stimulation and the onset of DNA synthesis, and the stimulation of DNA synthesis was not inhibited by α-amanitin or 5-FU. The data show that the nontransformed AKR-2B cells have two different arrest states which may represent two separate and distinct G1 arrest points - a growth factor deficiency arrest point and a nutrient deficiency arrest point. The nutrient deficiency arrested cells were very similar to the G1 arrested transformed AKR-MCA cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 110 (1982), S. 169-174 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A growth-factor-like substance capable of inducing nontransformed mouse AKR-2B, rat NRK, and EGF-receptorless mouse NR6 cells to form progressively growing colonies in soft agar was identified in acid/ethanol extracts of 17-day mouse embryos. This “mouse embryo factor” (MEF) is similar to previously described transforming growth factors in that it is capable of stimulating DNA synthesis and conferring a reversible transformed morphology on nontransformed cells in vitro. Passage of crude embryo extracts over a Bio-Gel P-60 column gave a major peak of soft agar growth-stimulating activity in the 15,000 molecular weight range with a minor peak at about 22,000. This biological activity was sensitive to treatment with either trypsin or dithiothreitol, but was unaffected by heat (56°C for 30 minutes or 100°C for 3 minutes), indicating that the activity is due to a heat-stable polypeptide(s) with disulfide bonds. Separation of these polypeptide(s) by chromatography on carboxymethyl cellulose revealed two peaks of soft agar growth-stimulating activity which did not cochromatograph with a peak of epidermal growth factor receptor-competing activity. The similarities of this mouse embryo-derived growth factor to previously identified transforming growth factors suggest that both fetal development and neoplastic transformation may be affected by similar mechanisms.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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