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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide.

Addition of glucagon to isolated hepatocytes increased glycogenolysis and phosphorylase a in a proportional manner. KCN caused slightly more glycogenolysis at considerably lower levels of phosphorylase a; the discrepancy was most pronounced after pretreatment of the hepatocytes with EGTA. When incubated with tagatose, the hepatocytes accumulated tagatose 1-phosphate, a presumed inhibitor of phosphorylase a. In these conditions the glucagon-induced glycogenolysis was blocked, but the glycogen loss caused by KCN or anoxia was not affected. Cyanide and anoxia may allow phosphorylase b and a to become equally active, or they may trigger a non-phosphorolytic glycogenolysis.[1]


  1. On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide. Bollen, M., de Ruysscher, D., Stalmans, W. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
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