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J. Biol. Chem., Vol. 259, Issue 13, 8151-8155, 07, 1984
JD Rothermel, B Jastorff and LH Botelho
The ability of the Rp diastereomer of adenosine cyclic 3',5'-
phosphorothioate (Rp cAMPS) to inhibit glucagon-induced glycogenolysis was
studied in hepatocytes isolated from fed rats. Preincubation of the cells
for 20 min with progressively higher concentrations of Rp cAMPS followed by
a 1 X 10(-9) M glucagon challenge resulted in a 50% inhibition of glucose
production over a 30-min period at 2-3 X 10(-6) M Rp cAMPS. A maximal
inhibition of 50-74% was achieved, the actual value depending upon the
length of preincubation with Rp cAMPS. The inhibitory effect did not
increase when the concentration of Rp cAMPS was increased from 3 X 10(-6)
to 3 X 10(-4) M. Addition of 1 X 10(-5) M Rp cAMPS to the cells followed by
10(-11) to 10(-6) M glucagon shifted the glucagon concentration required
for half-maximal glucose production measured at 10 min to 6-fold higher
glucagon concentrations and the concentration of glucagon required for
apparent maximal glucose production measured at 10 min to greater than
10-fold higher glucagon concentrations. The cAMP-dependent protein kinase
activation curve was similarly shifted to higher concentrations of
glucagon. These data show that Rp cAMPS acts as a cAMP antagonist capable
of opposing the glucagon-induced activation of cAMP-dependent protein
kinase and the concomitant activation of the glycogenolytic cascade.
Inhibition of glucagon-induced glycogenolysis in isolated rat hepatocytes by the Rp diastereomer of adenosine cyclic 3',5'- phosphorothioate
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