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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 93 (1977), S. 173-182 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of a somatomedin analog, Temin's multiplication stimulating activity (MSA), on amino acid transport into muscle cells have been characterized in a series of experiments on myoblasts and myotubes in culture. Addition of MSA to serum-starved L6 myoblasts increased the rate of aminoisobutyrate (AIB) uptake 50-150% within five hours. This early effect on transport was followed by increases in cell number, protein content and 3H-thymidine incorporation. Kinetic analyses indicated that MSA increased the maximal velocity of AIB uptake but had no effect on the KM for AIB. When myoblasts were allowed to fuse (and dividing cells eliminated by addition of 10-4 M cytosine arabinoside) the AIB transport system(s) remained similarly responsive to MSA. In myoblasts and in myotubes, both the basal and MSA-stimulated rate of AIB uptake were sodium-dependent processes; little stimulation occurred if sodium was absent from the labeling medium. Further suggesting the involvment of cations in response to hormone, MSA stimulated uptake of the potassium analog, 86Rb+, and increased net intracellular potassium in both myoblasts and myotubes. MSA was active at concentrations equivalent to in vivo levels of somatomedins; neither insulin nor growth hormone had any effect at or near physiological concentrations.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 100 (1979), S. 343-349 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Enhanced uptake of amino acids is frequently associated with hyperplasia in cultured cells; we have recently shown (Merrill et al., '77) that this is true of the stimulation of rat myoblast proliferation in culture by Temin's Multiplication Stimulating Activity (MSA). In many cases the asymmetric distribution of Na+ and K+ across the cell membrane profoundly affects uptake of certain amino acids, so we investigated the possibility that enhanced Na+-dependent AIB transport was the result of an MSA-induced increase in K+ accumulation. MSA stimulated the rate of uptake of the potassium analog 86Rb+ 15-25% within ten minutes; this rate remained elevated for at least seven hours. Effects were limited to the ouabain-sensitive component of Rb+ uptake. (Our simultaneous measurements of 86Rb+ and 42K+ uptake demonstrated that Rb+ provides a useful qualitative but not an exact quantitative index of K+ uptake.) The stimulation of K+ uptake by MSA did not cause a large increase in total cellular K+ of the myoblasts; after five hours, MSA-treated cells contained only about 20% more K+ than did corresponding controls (1.21 ± 0.02 vs. 1.01 ± 0.02 μmoles/mg protein, respectively). To investigate whether this small increase in K+ content could be amplified by the cell to account for the 50-150% stimulation of AIB uptake, we preincubated cells with ouabain for various times and then measured total cell K+ and AIB uptake in the same culture dishes. Under conditions in which the MSA-stimulated increase of total cell K+ was prevented by ouabain, a substantial stimulation of AIB uptake was still observed. We conclude that MSA stimulation of AIB transport is independent of increased accumulation of K+ in rat myoblasts.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: After yeast cells commit to the cell cycle in a process called START, genes required for DNA synthesis are expressed in late G1. Periodicity is mediated by a hexameric sequence, known as a MCB element, present in all DNA synthesis gene promoters. A complex that specifically binds MCBs has been identified. One polypeptide in the MCB complex is Swi6, a transcription factor that together with Swi4 also binds G1 cyclin promoters and participates in a positive feedback loop at START. The finding that Swi6 is directly involved in both START and DNA synthesis gene control suggest a model in which Swi6, activated through its participation in START, serves as the central transcription factor in coordinating late G1 gene expression. The mechanism may be conserved in all eukaryotic cells.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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