Editors' ChoiceCell Biology

Another PDGF

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Science's STKE  08 May 2001:
Vol. 2001, Issue 81, pp. tw5
DOI: 10.1126/stke.2001.81.tw5

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]

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