Glucagon stimulates phosphorylation of different peptides in isolated periportal and perivenous hepatocytes.
The perivenous and periportal zones of the liver acinus differ in enzyme complements and capacities for gluconeogenesis, glycolysis and other metabolic processes. The biochemical factors governing this metabolic zonation are still poorly understood. Glucagon-mediated protein phosphorylation is an important factor in the regulation of hepatic metabolism. Here we show, by comparing the 32P-labelling pattern of isolated periportal and perivenous hepatocytes, that glucagon promotes the phosphorylation of zone-specific peptides as well as three common peptides (glycogen phosphorylase, glycogen synthase and pyruvate kinase) in the two cell types. We propose that the zone-specific phosphorylation of peptides is an important factor governing the shortterm zonation of metabolic processes in the liver.
Department of Biochemistry, University of Western Australia, Nedlands, Australia.
S R
SR
Aggarwal
K O
KO
Lindros
T N
TN
Palmer
D000818:Animals; D002469:Cell Separation; D004305:Dose-Response Relationship, Drug; D005934:Glucagon / Q000494:pharmacology*; D006006:Glycogen Synthase / Q000378:metabolism; D008099:Liver / Q000098:blood supply* / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D010455:Peptides / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism; D010766:Phosphorylation; D011168:Portal System; D011506:Proteins / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D014018:Tissue Distribution; D014680:Veins
D010455:Peptides; D011506:Proteins; D005934:Glucagon; D006005:Phosphorylases; D006006:Glycogen Synthase; D011770:Pyruvate Kinase