-transparent.png){kind=logo}
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.
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1988,
Scandinavian journal of gastroenterology. Supplement,
S R Aggarwal, and
K O Lindros, and
T N Palmer
December 1991,
Biochemical and biophysical research communications,
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1990,
Methods in molecular biology (Clifton, N.J.),
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1986,
Enzyme,
S R Aggarwal, and
K O Lindros, and
T N Palmer
October 1986,
The Biochemical journal,
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1989,
Hepatology (Baltimore, Md.),
S R Aggarwal, and
K O Lindros, and
T N Palmer
December 1998,
The Journal of laboratory and clinical medicine,
S R Aggarwal, and
K O Lindros, and
T N Palmer
September 1988,
The Biochemical journal,
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1998,
Cell transplantation,
S R Aggarwal, and
K O Lindros, and
T N Palmer
January 1988,
Chemico-biological interactions,
