Interleukin 1 beta regulates glycogen metabolism in primary cultured rat hepatocytes.
We examined the effects of human recombinant IL-1 beta on glycogen metabolism in cultured rat hepatocytes. When IL-1 beta was present at 8 nM in the culture medium for 15 hours prior to cell harvest, glycogen storage in hepatocytes was lowered approximately by 60% of the control. The enzymatic activity of glycogen synthase I in the IL-1 beta-treated cells (8 nM) was decreased by 70%; however, the activity ratio of the synthases I to D was not different from the untreated. In addition, the activity of glycogen phosphorylase a, the active form of phosphorylase involved in glycogenolysis, was increased by approximately 27% while the total phosphorylase activity was not changed. The data demonstrate for the first time that IL-1 beta lowers the intracellular glycogen contents in primary cultured rat hepatocytes.
Lee
J D
JD
Department of Biochemistry, College of Medicine, University of Ulsan, Seoul, Korea.
Cho
S W
SW
Hwang
O
O
D000818:Animals; D002478:Cells, Cultured; D006006:Glycogen Synthase / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1 / Q000494:pharmacology*; D008099:Liver / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D008112:Liver Glycogen / Q000378:metabolism*; D008297:Male; D006005:Phosphorylases / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D011994:Recombinant Proteins / Q000494:pharmacology
D007375:Interleukin-1; D008112:Liver Glycogen; D011994:Recombinant Proteins; D006005:Phosphorylases; D006006:Glycogen Synthase