Effect of glucagon on insulin receptor phosphorylation in intact liver cells.
Evidence is presented that incubation of rat liver cells with glucagon leads to an increase in the phosphorylation of specific serine residues within insulin receptors, particularly in the presence of insulin. However, no changes in either the tyrosine phosphorylation of the receptors or the tyrosine kinase activity towards a synthetic peptide substrate was detected.
Issad
T
T
Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
Young
S W
SW
Tavaré
J M
JM
Denton
R M
RM
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D005934:Glucagon / Q000494:pharmacology*; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism; D008099:Liver / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011972:Receptor, Insulin / Q000187:drug effects / Q000378:metabolism*
D007328:Insulin; D005934:Glucagon; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin