Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2.
Insulin stimulates cellular protein synthesis in calf chondrocytes in suspension culture. This enhanced synthetic activity is seen in association with a decrease in phosphorylation of the alpha subunit of protein synthesis initiation factor eIF-2. [32P] associated with the alpha subunit is reduced approximately 50% by insulin treatment of chondrocytes incubated in [32P] containing media. Identical or closely located amino acids in the eIF-2 alpha subunit are phosphorylated by the chondrocyte kinase(s) and the rabbit reticulocyte hemin regulated kinase as indicated by comparative peptide fragment analysis of [32P] labeled alpha subunits.
D000818:Animals; D002358:Cartilage, Articular / Q000378:metabolism; D002417:Cattle; D004586:Electrophoresis / Q000379:methods; D010450:Endopeptidases / Q000378:metabolism; D015852:Eukaryotic Initiation Factor-2; D066298:In Vitro Techniques; D007328:Insulin / Q000494:pharmacology*; D010448:Peptide Initiation Factors / Q000378:metabolism*; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism; D012697:Serine Endopeptidases
D015852:Eukaryotic Initiation Factor-2; D007328:Insulin; D010448:Peptide Initiation Factors; D011506:Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase