Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 10 June 1988:
Vol. 240. no. 4858, pp. 1532 - 1534
DOI: 10.1126/science.2836953
Prev | Table of Contents | Next

Articles

Science, Vol 240, Issue 4858, 1532-1534
Copyright © 1988 by American Association for the Advancement of Science

articles

A common PDGF receptor is activated by homodimeric A and B forms of PDGF

JA Escobedo, S Navankasatussas, LS Cousens, Coughlin SR, GI Bell, and LT Williams

Department of Medicine, University of California, San Francisco.

The human platelet-derived growth factor (PDGF) receptor complementary DNA was cloned and expressed by transfection of Chinese hamster ovary (CHO) fibroblasts. The ability of CHO cells expressing the human receptor complementary DNA (CHO-HR5) to interact with different recombinant forms of PDGF (AA and BB homodimers) was tested. Both forms of PDGF bind to the transfected receptor, stimulate the receptor tyrosine kinase activity, and elicit a mitogenic response in a manner that was indistinguishable from the responses of Balb/c 3T3 cells to AA and BB forms of PDGF can be attributed to a single type of receptor and show that the AA form, like the BB form, is a true mitogen.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Efficacy of the Novel Selective Platelet-Derived Growth Factor Receptor Antagonist CT52923 on Cellular Proliferation, Migration, and Suppression of Neointima following Vascular Injury.
J.-C. Yu, N. A. Lokker, S. Hollenbach, M. Apatira, J. Li, A. Betz, D. Sedlock, S. Oda, Y. Nomoto, K. Matsuno, et al. (2001)
J. Pharmacol. Exp. Ther. 298, 1172-1178
   Abstract »    Full Text »    PDF »
The Role of Alpha and Beta Platelet-Derived Growth Factor Receptor in the Vascular Response to Injury in Nonhuman Primates.
N. A. Giese, M. M. H. Marijianowski, O. McCook, A. Hancock, V. Ramakrishnan, L. J. Fretto, C. Chen, A. B. Kelly, J. A. Koziol, J. N. Wilcox, et al. (1999)
Arterioscler. Thromb. Vasc. Biol. 19, 900-909
   Abstract »    Full Text »    PDF »
Functional Importance of Platelet-derived Growth Factor (PDGF) Receptor Extracellular Immunoglobulin-like Domains. IDENTIFICATION OF PDGF BINDING SITE AND NEUTRALIZING MONOCLONAL ANTIBODIES.
N. A. Lokker, J. P. O'Hare, A. Barsoumian, J. E. Tomlinson, V. Ramakrishnan, L. J. Fretto, and N. A. Giese (1997)
J. Biol. Chem. 272, 33037-33044
   Abstract »    Full Text »    PDF »
FGF-1–Induced Platelet-Derived Growth Factor-A Chain Gene Expression in Endothelial Cells Involves Transcriptional Activation by Early Growth Response Factor-1.
G. J. Delbridge and L. M. Khachigian (1997)
Circ. Res. 81, 282-288
   Abstract »    Full Text »
Signal transduction by the platelet-derived growth factor receptor.
L. Williams (1989)
Science 243, 1564-1570
   Abstract »    PDF »
Role of phosphatidylinositol kinase in PDGF receptor signal transduction.
S. Coughlin, J. Escobedo, and L. Williams (1989)
Science 243, 1191-1194
   Abstract »    PDF »
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
T Matsui, M Heidaran, T Miki, N Popescu, W La Rochelle, M Kraus, J Pierce, and S Aaronson (1989)
Science 243, 800-804
   Abstract »    PDF »
Signal Transduction by the Platelet-derived Growth Factor Receptor.
L.T. Williams, J.A. Escobedo, M.T. Keating, and S.R. Coughlin (1988)
Cold Spring Harb Symp Quant Biol 53, 455-465
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)