Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2

Abstract

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.