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  • 1
    ISSN: 1423-0127
    Keywords: γ-Aminobutyric acid ; L-glutamate decarboxylase ; Protein phosphorylation ; Neurotransmitter synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In the brain, the γ-aminobutyric acid (GABA) level is primarily controlled by the activity of its synthesizing enzyme,L-glutamate decarboxylase (GAD). At present, mechanisms responsible for regulation of GAD activity remain largely unknown. Here we report that GAD activity is inhibited by conditions favoring protein phosphorylation, and this inhibition can be reversed by phosphatase treatment. Furthermore, this inhibition appears to result from the suppression of a Ca2+-dependent phosphatase. Phosphorylation of GAD is demonstrated by direct incorporation of32P into the GAD protein. These results suggest that GAD activity in the brain is inhibited by phosphorylation and activated by dephosphorylation. A model for regulation of GABA synthesis related to neuronal excitation is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of cancer research and clinical oncology 123 (1997), S. 296-299 
    ISSN: 1432-1335
    Keywords: Renal cell carcinoma ; N-acetylglucosaminyltransferase ; γ-Glutamyltranspeptidase ; Glycan ; ConA affinity chromatography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The activities ofN-acetylglucosaminyltransferase (GnT) III, IV and V were determined in 10 cases of renal cell carcinoma (RCC) and compared with the normal kidney cortex (NKC) regions of the same kidney resected from RCC patients. It was found that the GnT III and GnT IV activities decreased consistently in all samples of RCC, while GnT V activity increased, decreased or did not change in different samples. The mean levels of GnT III and GnT IV activities in RCC were found to be very significantly lower than those of NKC on statistical analysis, but the mean value of GnT V activity was almost identical in RCC and NKC. The decrease in GnT activities in RCC were compatible with the decrease in bisectingN-acetylglucosamine (GlcNAc) and antennary number of complex-typeN-glycans in γ-glutamyltranspeptidase (γ-GT) partially purified from RCCs as studied with concanavalin A (ConA) affinity column chromatography, which showed a decrease of unbound fraction and increase of bound fractions.
    Type of Medium: Electronic Resource
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