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Glucagon stimulates phosphorylation of different peptides in isolated periportal and perivenous hepatocytes
Author(s) -
Sandeep Aggarwal,
Lindros Ko,
Palmer Tn
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01387-3
Subject(s) - glycogen phosphorylase , glucagon , phosphorylation , gluconeogenesis , glycogen , glycogen synthase , biochemistry , glycolysis , biology , glycogen debranching enzyme , phosphorylase kinase , glycogenolysis , chemistry , enzyme , hormone
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 32 P‐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.