Platelet-Derived Growth Factor

Literature References: Cationic glycoprotein; mol wt ~30 kDa. Chemoattractant and mitogen for fibroblasts, smooth muscle cells and glial cells. Involved in both normal and pathologic processes such as wound healing, atherosclerosis, and neoplasia. Composed of two disulfide-linked polypeptide chains, A and B, which may be assembled as a heterodimer or as AA or BB homodimers. PDGF-AB is the most abundant. Originally isolated from platelets, subsequently found to be secreted by a number of cell types including macrophages, fibroblasts, and endothelial cells. Identification: R. Ross et al., Proc. Natl. Acad. Sci. USA 71, 1207 (1974); N. Kohler, A. Lipton, Exp. Cell Res. 87, 297 (1974). Isoln: H. N. Antoniades et al., Proc. Natl. Acad. Sci. USA 72, 2635 (1975). Purification: H. N. Antoniades et al., ibid. 76, 1809 (1979); C.-H. Heldin et al., ibid. 3722. Structure: A. Johnsson et al., Biochem. Biophys. Res. Commun. 104, 66 (1982); A. Hammacher et al., J. Biol. Chem. 263, 16493 (1988). PDGF-B is structurally homologous to p28sis, the transforming protein of the simian sarcoma virus: M. D. Waterfield et al., Nature 304, 35 (1983); R. F. Doolittle et al., Science 221, 275 (1983). Comparison of biological properties and transforming potential of A and B chains: M. P. Beckmann et al., Science 241, 1346 (1988). Identification of PDGF receptor: C.-H. Heldin et al., Proc. Natl. Acad. Sci. USA 78, 3664 (1981). Molecular mechanisms of action: L. T. Williams, Science 243, 1564 (1989). Review of role in atherosclerosis: R. Ross, N. Engl. J. Med. 314, 488-500 (1986); in wound healing: G. F. Pierce et al., J. Cell. Biochem. 45, 319-326 (1991). Reviews: R. Ross, Annu. Rev. Med. 38, 71-79 (1987); B. Westermark et al., Ciba Found. Symp. 150, 6-22 (1990); K. C. Hart et al., Genet. Eng. (NY) 17, 181-208 (1995); W. Meyer-Ingold, W. Eichner, Cell Biol. Int. 19, 389-398 (1995).