Stimulated phosphorylation of non-histone phosphoproteins in SV-40 transformed WI-38 human diploid fibroblasts
Department of Cell Biology
Biological Transport; Cell Line; *Cell Transformation, Neoplastic; Diploidy; Kinetics; Phosphates; Phosphoproteins; Simian virus 40; Transcription, Genetic
Because the phosphorylation of non-histone proteins has been suggested to play a role in the regulation of eukaryotic gene transcription, we have compared the phosphorylation of these proteins in normal and SV-40 transformed WI-38 human diploid fibroblasts. The rate of phosphorylation was found to be roughly ten-fold higher in the transformed cells, and this striking difference could not be accounted for by either an increased rate of phosphate transport or by the synthesis of new species of non-histone proteins which subsequently become phosphorylated. To our knowledge this is the most dramatic alteration in non-histone protein phosphorylation ever described, and therefore may have important implications for our understanding of malignant transformation.
Biochim Biophys Acta. 1975 Aug 6;402(1):125-30.
Biochimica et biophysica acta
Pumo DE, Stein GS, Kleinsmith LJ. (1975). Stimulated phosphorylation of non-histone phosphoproteins in SV-40 transformed WI-38 human diploid fibroblasts. Stein, Stein, Lian, vanWijnen Lab Publications. Retrieved from https://escholarship.umassmed.edu/stein/206