The platelet-derived growth factor (PDGF) family of heparin-binding growth factors consists of five known members, denoted PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD. The mature and active form of these proteins, an anti-parallel disulfide-linked dimer of two 12-14 kDa polypeptide chains, is obtained through proteolytic processing of biologically inactive precursor proteins, which contain an N-terminal CUB domain and a PDGF/VEGF homologous domain. The PDGFs interact with two related protein tyrosine kinase receptors, PDGFR-α and PDGFR-β, and are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and certain tumor cells. They play an important role in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubules epithelial cell development. Mature PDGFs are stored in platelet α-granules and are released upon platelet activation. PDGF-AA, -AB, -BB and -CC signal primarily through the PDGF-Rα receptor, whereas PDGF-DD interacts almost exclusively with the PDGF-Rβ receptor. Recombinant human PDGF-CC is a 25kDa protein consisting of two identical disulfide-linked 114 amino-acid polypeptide chains.