[58] Purification of human platelet-derived growth factor

Publisher Summary This chapter describes a method for the purification of human platelet-derived growth factor (PDGF) from outdated plateletrich plasma (PRP), using commonly available laboratory reagents and yielding a mitogen purified 800,000-fold over the starting material. The chapter discusses the methods of analysis and properties of highly purified PDGF. PDGF has a 30,000 molecular weight glycoprotein, which is released from the platelet during coagulation and has been shown to be one of the principal macromolecules in whole blood serum capable of stimulating deoxyribonucleic acid (DNA) synthesis and cell growth in connective tissue cells in vitro. PDGF plays a physiologic role in wound healing and tissue repair and a pathologic role in the formation of lesions of atherosclerosis. Studies with highly purified PDGF help determine the role of PDGF and other platelet mitogens in these processes and in defining the early cellular changes that occur in response to stimulation by PDGF. However, it is now known that PDGF like molecules are also synthesized by cultured vascular endothelial cells, newborn rat aortic smooth muscle cells, and cells transformed by a wide variety of transforming agents.