Platelet-derived growth factor stimulates the phosphorylation of ribosomal protein S6.
The human platelet derived-growth factor (PDGF) is both a potent mitogen and a strong chemoattractant protein for cells involved in inflammation and repair. In seeking mechanisms by which PDGF might initiate specific activities in target cells, it was found that highly purified PDGF stimulates the phosphorylation of an Mr approximately 33000 protein in confluent Swiss mouse 3T3 cells [Biochem. Biophys. Res. Commun. (1981) 103, 355-361]. The Mr approximately 33000 protein has now been recovered in polysomes by differential centrifugation and identified as ribosomal protein S6 by two-dimensional polyacrylamide gel electrophoresis.
D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D006133:Growth Substances / Q000494:pharmacology*; D051379:Mice; D008970:Molecular Weight; D010455:Peptides / Q000494:pharmacology*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D010982:Platelet-Derived Growth Factor; D012269:Ribosomal Proteins / Q000378:metabolism*
D006133:Growth Substances; D010455:Peptides; D010761:Phosphorus Radioisotopes; D010982:Platelet-Derived Growth Factor; D012269:Ribosomal Proteins