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-alpha and PDGFR-beta, 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 alpha-granules, and are released upon platelet activation. PDGF-AA, -AB, -BB and -CC signal primarily through the PDGFR-alpha receptor, whereas PDGF-DD interacts almost exclusively with the PDGFR-beta receptor. Recombinant Human PDGF-CC is a 25.0 kDa protein consisting of two identical disulfide-linked, 112 amino acid, polypeptide chains.