RT Journal Article
SR Electronic
T1 Another PDGF
JF Science's STKE
JO Sci. STKE
FD American Association for the Advancement of Science
SP tw5
OP tw5
DO 10.1126/stke.2001.81.tw5
VO 2001
IS 81
YR 2001
UL http://stke.sciencemag.org/content/2001/81/tw5.abstract
AB A new member joins the family of platelet-derived growth factors (PDGFs). Bergsten et al. and LaRochelle et al. have identified PDGF-D, a secreted homodimer that becomes an active ligand when proteolyzed. Both groups discovered it by first searching the database of human expressed genes and then isolating the human cDNA. LaRochelle also isolated the murine cDNA. Although most homologous to PDGF-C, which also requires proteolyltic activation, PDGF-D specifically activated the beta PDGF receptor (PDGFR-β). PDGF-D only activated the alpha PDGR (PDGFR-α) when PDGFR-β was also expressed in cells, suggesting that receptor heterodimerization occurred. The groups describe the broad expression pattern of PDGF-D in human tissue and in the developing mouse embryo. E. Bergsten, M. Uutela, X. Li, K. Pietras, A. Ostman, C.-H. Heldin, K. Alitalo, U. Eriksson, PDGF-D is a specific, protease-activated ligand for the PDGF β-receptor. Nature Cell Biol. 3, 512-516 (2001). [Online Journal] W. J. LaRochelle, M. Jeffers, W. F. McDonald, R. A. Chillakuru, N. A. Giese, N. A. Lokker, C. Sullivan, F. L. Boldog, M. Yang, C. Vernet, C. E. Burgess, E. Fernandes, L. L. Deegler, B. Rittman, J. Shimkets, R. A. Shimkets, J. M. Rothberg, H. S. Lichenstein, PDGF-D, a new protease-activated growth factor. Nature Cell Biol. 3, 517-521 (2001). [Online Journal]