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

C A Towle; H J Mankin; J Avruch; B V Treadwell

doi:10.1016/0006-291x(84)90697-1

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

C A Towle·H J Mankin·J Avruch·B V Treadwell

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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 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.

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Animals Cartilage, Articular Cattle Electrophoresis Endopeptidases Eukaryotic Initiation Factor-2 In Vitro Techniques Insulin Peptide Initiation Factors Phosphorylation Proteins Reticulocytes Serine Endopeptidases Journal Article Research Support, U.S. Gov't, P.H.S.

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C A Towle, H J Mankin, J Avruch, B V Treadwell. 1984-05-31. Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2.. https://doi.org/10.1016/0006-291x(84)90697-1

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