Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function (By similarity). Homodimer; disulfide-linked. Interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB domain) with PLAT (via kringle domain) (By similarity). Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Highly expressed in the kidney and adrenal gland. In the kidney, it is expressed in arteriolar smooth muscle cells and in epithelial cells of individual segments (at protein level). Expressed in the floor plate of the spinal cord at E11 and also in the ventricular zone at E16, but not in adult. In the brain, expression is more significant at E16 than at adult, with high expression in the cortex, pontine area and choroid plexus. Detected in the otocyst at E16. Up-regulated in mesangial, visceral epithelial, and interstitial cells after predominant injury to these cells. Expression levels increase in hepatic cells undergoing in vitro transdifferentiation, which represents a model for hepatic fibrogenesis. Expression induced by indoxyl sulfate. Expression induced by angiotensin-2 via EGR1 in smooth muscle cells in neonatal but not in adult rats. Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG (By similarity). Sumoylated with SUMO1. N-glycosylated. Belongs to the PDGF/VEGF growth factor family.