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  • Blackwell Publishing Ltd  (2)
  • 1985-1989  (2)
Document type
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Regulation by Dibutyryl Cyclic AMP of Carnosine Synthesis in Astroglia-Rich Primary Cultures Kept in Serum-Free Medium (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The synthesis of carnosine (β-Ala-His) by astroglia-rich primary cultures was much higher if the cells were cultivated in Ham's nutrient mixture F-12 than if they were grown in Dulbecco's modified Eagle's medium. Carnosine synthesis was not affected by the presence of insulin, trans-ferrin. phorbol myristate acetate, or dexamethasone. However. dibutyryl cyclic AMP and other agents that can, directly or ndirectly, activate cyclic AMP-dependent protein kinases strongly lower the rate of carnosine synthesis. The depression of carnosine synthesis was dependent on the concentration of dibutyryl cyclic AMP. The effect was maximal (approximately 80% inhibition) in cultures preincubated with 1 mM dibutyryl cyclic AMP for 4 days. The adenylate cyclase activator forskolin, the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine, and 8-bromo-cyclic AMP caused the same depression as dibutyryl cyclic AMP, whereas neither butyrate nor dibutyryl cyclic GMP elicited any effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb10921.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Peptide Uptake by Astroglia-Rich Brain Cultures (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 49 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Uptake of carnosine has been investigated in as-troglia-rich primary cultures derived from brains of newborn mice. It could be demonstrated that carnosine is not degraded by these cells but rapidly taken up in an energy and sodium-dependent process. Uptake and release of carnosine by these cells were found to be mediated by a saturable, high-affinity transport system with apparent kinetic constants of Km=50 μMand Vmax= 22.7 nmol h1 mg protein1. Uptake of carnosine is strongly inhibited by other dipeptides as well as by various oligopeptides, e.g., Leu-en-kephalin. However, uptake of the radiolabeled tripeptide D Ala-L-Ala-L-Ala was not observed. Radiolabeled Leu-en-kephalin also did not accumulate intracellularly, even if degradation of the peptide was prevented by use of peptidase inhibitors. These results suggest that uptake of carnosine is catalyzed by a dipeptide-specific transport system with broad substrate specificity. With neuronal cells in primary culture, uptake of carnosine or other peptides was not observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb00957.x
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    Paper (German National Licenses)
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