Effects of glucagon with or without insulin administration on liver glycogen metabolism

N. Ercan, Mary C Gannon, frank q Nuttall

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8 Scopus citations


Rats fed ad libitum were given insulin alone (4 U/kg), glucagon alone (25 μg/kg), or insulin and glucagon sequentially. Phosphorylase a and synthase R activities, hepatic glycogen, uridine diphosphoglucose, inorganic phosphate (P(i)), and plasma glucose, lactate, glucagon, and insulin concentrations were determined over the subsequent 40 min. In separate animals, muscle extraction of 2-deoxy-D-[3H]glucose also was determined. After glucagon administration, glycogen phosphorylase a and plasma glucose were increased within 5 min. However, the glycogen concentration did not decrease for 20 min. Glucagon administration to rats pretreated with insulin stimulated a similar increase in phosphorylase a activity. Again, glycogen was not degraded for 20 min. After insulin only, glycogen concentration remained unchanged. Plasma glucose decreased as expected. In each group, muscle extraction of 2-deoxy-D-[3H]glucose increased compared with the controls (P < 0.05). In summary, glucagon and/or insulin administration did not stimulate significant glycogen degradation for 20 min, even though phosphorylase was activated. The mechanism remains to be determined.

Original languageEnglish (US)
Pages (from-to)E231-E238
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Issue number2 32-2
StatePublished - 1995
Externally publishedYes


  • glycogen phosphorylase
  • glycogenolysis
  • phosphorylase a activity
  • phosphorylase regulation


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