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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    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 81 (1973), S. 161-170 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A partially purified multiplication-stimulating activity for chicken embryo fibroblasts in cell culture was isolated from rat liver cell conditioned medium (see preceding paper, Dulak and Temin, 1973). It has been analyzed by isoelectric focusing and by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Multiplication-stimulating activity resided in a family of at least four polypeptides which were similar in apparent molecular size, but different in electrical charge. These polypeptides have a specific activity of about 50,000 with respect to serum. One of them has been purified on a small scale to apparent homogeneity in a sodium dodecyl sulfate polyacrylamide gel.
    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 81 (1973), S. 153-160 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A polypeptide fraction with multiplication-stimulating activity for chicken and rat embryo fibroblasts was partially purified from serum-free medium conditioned by the growth of a line of rat liver cells. The specific multiplication-stimulating activity of this fraction was 27,000 times that of serum. The rat liver cell multiplication-stimulating activity had a molecular weight of approximately 10,000 daltons and was inactivated by mercaptoethanol and dithiothreitol. It had sulfation factor and non-suppressible insulin-like activities, but did not have anti-trypsin activity. The rat liver cell multiplication-stimulating activity resembled both multiplication-stimulating activity from calf serum and somatomedin.
    Additional Material: 3 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 90 (1977), S. 127-137 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The application of roller-bottle cell culture techniques and a relatively simple purification scheme has led to the isolation of milligram quantities of a polypeptide cell multiplication stimulating activity (MSA) from Buffalo rat liver cell conditioned medium. We have characterized the apparently homogeneous MSA with respect to its biological activity, its N-terminal amino acid residue, and its amino acid composition, and have tested the MSA for growth-promoting activity in a number of cell types.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 5
    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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  • 6
    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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