Differential phosphorylation of ribosomal protein S6 in isolated rat hepatocytes after incubation with insulin and glucagon

Glucagon and insulin both stimulated the 32P-labelling of ribosomal protein S6 in rat hepatocytes that had been incubated with 32P i. Glucagon selectively enhanced the labelling of the tryptic peptide phosphorylated by cyclic AMP-dependent protein kinase, demonstrating that 6 S is a physiological su...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1982-11, Vol.148 (2), p.207-213
Main Authors: Wettenhall, Richard E.H., Cohen, Philip, Caudwell, Barry, Holland, Ross
Format: Article
Language:English
Subjects:
Animals
Cyclic AMP
Glucagon
Glucagon - pharmacology
Hepatocytes
In Vitro Techniques
Insulin
Insulin - pharmacology
Liver - drug effects
Liver - metabolism
Male
Phosphopeptides - analysis
Phosphorylation
Protein synthesis
Rats
Rats, Inbred Strains
Ribosomal Protein S6
Ribosomal Proteins - metabolism
Ribosomes
Ribosomes - metabolism
Starvation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Glucagon and insulin both stimulated the 32P-labelling of ribosomal protein S6 in rat hepatocytes that had been incubated with 32P i. Glucagon selectively enhanced the labelling of the tryptic peptide phosphorylated by cyclic AMP-dependent protein kinase, demonstrating that 6 S is a physiological substrate for this enzyme. Insulin stimulated the phosphorylation of distinct tryptic peptides, at least one of which appears to be very close in the primary structure to the sites phosphorylated by cyclic AMP-dependent protein kinase.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(82)80809-0