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On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide

1983; Elsevier BV; Volume: 115; Issue: 3 Linguagem: Inglês

10.1016/s0006-291x(83)80039-4

1090-2104

Mathieu Bollen, Dirk De Ruysscher, Willy Stalmans,

Neonatal Health and Biochemistry

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.