title: Studies of in vivo phosphorylated proteins in BC3H-1 myocytes suggest that protein kinase C is involved in insulin action.
abstract: Insulin (10 and 100 nM) and phorbol esters increased the phosphorylation of several proteins, including 40, 47 and 80 kDa proteins, which are markers for protein kinase C activation. Insulin effects were evident at 2 min and increased over 20 min. These findings suggest that insulin activates protein kinase C in BC3H-1 myocytes.
authors.affiliation: Veterans Administration Hospital, Tampa, FL.
authors.forename: M C
authors.initials: MC
authors.lastname: Vila
authors.forename: D R
authors.initials: DR
authors.lastname: Cooper
authors.forename: J S
authors.initials: JS
authors.lastname: Davis
authors.forename: M L
authors.initials: ML
authors.lastname: Standaert
authors.forename: R V
authors.initials: RV
authors.lastname: Farese
mesh_terms: D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D007328:Insulin / Q000494:pharmacology*; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
chemical_list: D007328:Insulin; D010750:Phosphoproteins; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate