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  • Title: Regulation of the dephosphorylation of phosphorylase A by glucose, AMP and polyamines.
    Author: Farkas I, Tóth B, Gergely P.
    Journal: Int J Biochem; 1988; 20(2):197-201. PubMed ID: 2832227.
    Abstract:
    1. The effect of glucose, caffeine, AMP and polyamines was investigated on the dephosphorylation of phosphorylase a by the catalytic subunits of protein phosphatase-1 and -2A. 2. Caffeine at 1-20 microM inhibited the dephosphorylation of the dimeric phosphorylase a at 37 degrees C using skeletal muscle enzymes; 0.1-10 mM of caffeine enhanced the rate of dephosphorylation greatly at 13 degrees C and slightly at 37 degrees C. 3. alpha-D-Glucose was more effective in accelerating both the dephosphorylation and the tryptic digestion of phosphorylase a than the beta-anomer. 4. Polyamines were found to moderate the inhibitory effect of AMP at concentrations which may occur in the tissues. In the presence of 5 mM glucose polyamines could cancel the AMP inhibition of the dephosphorylation of liver phosphorylase a by hepatic protein phosphatase-1 and -2A.
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