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Horm Metab Res 1986; 18(1): 18-21
DOI: 10.1055/s-2007-1012215
ORIGINALS
Basic
© Georg Thieme Verlag, Stuttgart · New York

Involvement of Cyclic AMP-Dependent Protein Kinase on the Phosphorylase Kinase Inhibition by Glucose-6-Phosphate in Adipose Tissue Extracts

G. Ruiz, F. Sobrino, B. Roca, R. Goberna
  • Department of Biochemistry, School of Medicine, University of Sevilla, Sevilla, Spain
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Publication History

1982

1984

Publication Date:
14 March 2008 (online)

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Summary

In order to achieve further clarification of the regulation of glycogenolysis in adipose tissue, we studied the effect of glucose-6-phosphate on phosphorylase activation in Sephadex G-25 filtrate of adipose tissue. The activity of phosphorylase kinase was decreased by 50% and by 75% in the presence of 0.5 mM and 2 mM of glucose-6-phosphate, respectively. This inhibition could be partially prevented by 0.5 mM AMP.

Furthermore, we investigated the influence of glucose-6-phosphate on the effect of cyclic-AMP-dependent protein kinase on the activation of phosphorylase. The addition of cyclic-AMP and cyclic-AMP-dependent protein kinase caused a decrease in the inhibition of the phosphorylase activation by glucose-6-phosphate. Also, the glucose-6-phosphate at physiological concentration, decreased adipose tissue cyclic-AMP-dependent protein kinase activity.

Key-Words

Glycogenolysis - Phosphorylase Kinase - Glucose-6-Phosphate - Adipose Tissue

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