Human platelet-derived growth factor: structure and function.

Abstract

Human platelet-derived growth factor (PDGF) is a heat-stable, cationic polypeptide transported in blood in the alpha granules of platelets. It is released from platelets during blood clotting. PDGF has been resolved into at least two closely related active polypeptides, PDGF-I and PDGF-II, each consisting of two inactive chains linked together by disulfide bonds. PDGF stimulates the growth of normal cells in culture, including fibroblasts, arterial smooth muscle cells, and glial cells. In addition, PDGF has been shown to stimulate cell migration and many diverse metabolic functions such as amino acid transport, protein synthesis, cholesterol ester synthesis, phospholipid turnover, and prostacyclin synthesis. It modulates receptor binding of other active components such as epidermal growth factor, luteinizing hormone, low-density lipoprotein, and somatomedin C. Specific cell membrane receptors for PDGF have been demonstrated in arterial smooth muscle cells and fibroblasts.