Protein phosphorylation in a myogenic cell line: effects of insulin, epinephrine and glucose.
Protein phosphorylation was studied in L6 cultured muscle cells by incubating cells with Na 32Pi and subsequently exposing them to external agents. L6 cells readily incorporated 32Pi into a number of peptides approaching steady-state incorporation by 2 h. Insulin stimulated the phosphorylation of one peptide of molecular mass 29,000 daltons by 37% with an ED50 of 3 mU/ml. This peptide was located in the high-speed pellet (105,000 g 60 min) which is consistent with an S6 ribosomal protein. Epinephrine (10(-5) M) led to only a modestly stimulated (less than 14%) phosphorylation of three peptides of molecular masses 39,000, 29,000 and 21,000 daltons. Glucose (5-50 mM) stimulated the phosphorylation of one peptide of molecular mass 19,000 daltons by 24%.
D001345:Autoradiography; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D004837:Epinephrine / Q000494:pharmacology*; D005947:Glucose / Q000494:pharmacology*; D007328:Insulin / Q000494:pharmacology*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism*; D010766:Phosphorylation
D007328:Insulin; D009124:Muscle Proteins; D005947:Glucose; D004837:Epinephrine