Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2 |
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Authors: | CA Towle HJ Mankin J Avruch BV Treadwell |
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Institution: | 1. Orthopaedic Research Laboratories, Massachusetts General Hospital, Boston, MA USA;2. Harvard Medical School, Boston, MA USA |
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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 α subunit of protein synthesis initiation factor eIF-2. 32P] associated with the α 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 α 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 α subunits. |
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