Platelet-derived growth factor (PDGF), originally recognized as the principal source of mitogenic activity present in whole blood serum and missing in plasma or plasma-derived serum, has now been shown to be derived from many diploid cells as well as a number of tumor cells. Although the platelet was the first cell of origin to be discovered, it is clear that PDGF is stored in alpha granules in the platelet and is synthesized and stored in these granules in the megakaryocyte. Since the purification and characterization of platelet-derived growth factor has been accomplished by a number of different laboratories, several assays have been developed that permit the determination of other cells that can make and secrete PDGF. The assays that are routinely used in our laboratory include: 1) a receptor competition binding assay based on the fact that PDGF binds with high affinity (10-11M) to a specific cell-surface receptor. This competition binding assay, therefore, measures the capacity of unknowns containing PDGF or PDGF-like substances to compete for binding to this receptor. 2) An ELISA was established based on the development of a monospecific polyclonal anti-PDGF IgG that was developed in a goat. This antibody can completely abolish the mitogenic activity of highly purified PDGF.
KeywordsMitogenic Activity Competition Binding Assay Alpha Granule Simian Sarcoma Virus Receptor Competition Binding Assay
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Barrett TB, Gajdusek CM, Schwartz SM, McDougall JK, Benditt EP (1984) Expression of the sis gene by endothelial cells in culture and in vivo. Proc Natl Acad Sci USA 81:6772–6774PubMedCrossRefGoogle Scholar
Bowen-Pope DF, Vogel A, Ross R (1984) Production of platelet-derived growth factor-like molecules and reduced expression of platelet-derived growth factor receptors accompany transformation by a wide spectrum of agents. Proc Natl Acad Sci USA 81: 2396–2400PubMedCrossRefGoogle Scholar
Dicorleto PE, Bowen-Pope DF (1983) Cultured endothelial cells produce a platelet-derived growth factor-like protein. Proc Natl Acad Sci USA 80: 1919–1923PubMedCrossRefGoogle Scholar
Martinet Y, Bitterman PB, Mornex J-F, Grotendorst GR, Martin GR, Crystal RG (1986) Activated human monocytes express the c-sis proto-oncogene and release a mediator showing PDGF-like activity. Nature 319: 158–160PubMedCrossRefGoogle Scholar
Ross R, Raines EW, Bowen-Pope DF (1986) The biology of platelet-derived growth factor. Cell 46: 155–169PubMedCrossRefGoogle Scholar
Seifert RA, Schwartz SM, Bowen-Pope DF (1984) Developmentally regulated production of platelet-derived growth factor-like molecules. Nature 311: 669–671PubMedCrossRefGoogle Scholar
Shimokado K, Raines EW, Madtes DK, Barrett TB, Benditt EP, Ross R (1985) A significant part of macrophage-derived growth factor consists of at least two forms of PDGF. Cell 43: 277–286PubMedCrossRefGoogle Scholar
Walker LN, Bowen-Pope DF, Ross R, Reidy MA (1986) Production of platelet-derived growth factor-like molecules by cultured arterial smooth muscle cells accompanies proliferation after arterial injury. Proc Natl Acad Sci USA 83: 7311–7315PubMedCrossRefGoogle Scholar
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