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Platelet‐derived growth factor stimulates the phosphorylation of ribosomal protein S6
Author(s) -
Nishimura Junji,
Deuel Thomas F.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80263-4
Subject(s) - ribosomal protein s6 , ribosomal protein , phosphorylation , polysome , growth factor , microbiology and biotechnology , platelet derived growth factor receptor , platelet derived growth factor , polyacrylamide gel electrophoresis , centrifugation , differential centrifugation , platelet , biology , chemistry , protein phosphorylation , biochemistry , protein kinase a , ribosome , immunology , rna , gene , receptor , enzyme
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 M r ∼33 000 protein in confluent Swiss mouse 3T3 cells [Biochem. Biophys. Res. Commun. (1981) 103, 355–361]. The M r ∼ 33 000 protein has now been recovered in polysomes by differential centrifugation and identified as ribosomal protein S6 by two‐dimensional polyacrylamide gel electrophoresis.