CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LaRochelle, W. J.
Right arrow Articles by Pierce, J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by LaRochelle, W. J.
Right arrow Articles by Pierce, J. H.

Cell Growth & Differentiation, Vol 4, Issue 7 547-553, Copyright © 1993 by American Association of Cancer Research


ARTICLES

Inhibition of platelet-derived growth factor autocrine growth stimulation by a monoclonal antibody to the human alpha platelet-derived growth factor receptor

WJ LaRochelle, RA Jensen, MA Heidaran, M May-Siroff, LM Wang, SA Aaronson and JH Pierce
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.

A potent neutralizing monoclonal antibody to the human alpha platelet-derived growth factor (PDGF) receptor (alpha PDGFR) was raised by immunizing BALB/c mice with 32D cells expressing the human alpha PDGFR. This monoclonal antibody, designated alpha R1, immunoprecipitated human, monkey, rabbit, pig, dog, and cat, but not hamster, rat, or mouse alpha PDGFRs. Comparison with PR292, a monoclonal antibody previously generated against the alpha PDGFR, showed that both recognized alpha PDGFR extracellular domains, but neither demonstrated reactivity against the beta PDGFR. In vitro binding studies revealed that alpha R1, but not PR292, detection of the alpha PDGFR was blocked by either PDGF AA or PDGF BB. These results strongly suggest that the receptor ligand-binding domain spatially overlapped with the alpha R1 epitope. Monoclonal antibody alpha R1 also inhibited PDGF stimulation of [3H]thymidine uptake by 32D cells expressing the alpha PDGFR (32D alpha R) as well as autocrine growth stimulation of 32D alpha R cells transfected with and expressing PDGF AA or PDGF BB. Therefore, monoclonal antibody alpha R1 may be useful in the detection and growth inhibition of malignancies in which PDGF autocrine stimulation and/or alpha PDGFR overexpression plays an important role(s).


This article has been cited by other articles:


Home page
Molecular Cancer TherapeuticsHome page
N. Loizos, Y. Xu, J. Huber, M. Liu, D. Lu, B. Finnerty, R. Rolser, A. Malikzay, A. Persaud, E. Corcoran, et al.
Targeting the platelet-derived growth factor receptor {alpha} with a neutralizing human monoclonal antibody inhibits the growth of tumor xenografts: Implications as a potential therapeutic target
Mol. Cancer Ther., March 1, 2005; 4(3): 369 - 379.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
C.-H. Heldin and B. Westermark
Mechanism of Action and In Vivo Role of Platelet-Derived Growth Factor
Physiol Rev, October 1, 1999; 79(4): 1283 - 1316.
[Abstract] [Full Text] [PDF]


Home page
EMBO J.Home page
G. Celli, W. J. LaRochelle, S. Mackem, R. Sharp, and G. Merlino
Soluble dominant-negative receptor uncovers essential roles for fibroblast growth factors in multi-organ induction and patterning
EMBO J., March 16, 1998; 17(6): 1642 - 1655.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
H. Takayama, W. J. LaRochelle, R. Sharp, T. Otsuka, P. Kriebel, M. Anver, S. A. Aaronson, and G. Merlino
Diverse tumorigenesis associated with aberrant development in mice overexpressing hepatocyte growth factor/scatter factor
PNAS, January 21, 1997; 94(2): 701 - 706.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
A. Uren, J.-C. Yu, W. Li, I.-Y. Chung, D. Mahadevan, J. H. Pierce, and M. A. Heidaran
Identification of a Domain within the Carboxyl-terminal Region of the Platelet-derived Growth Factor (PDGF) Receptor That Mediates the High Transforming Activity of PDGF
J. Biol. Chem., May 10, 1996; 271(19): 11051 - 11054.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
D. Mahadevan, J.-C. Yu, J. W. Saldanha, N. Thanki, P. McPhie, A. Uren, W. J. LaRochelle, and M. A. Heidaran
Structural Role of Extracellular Domain 1 of {alpha}-Platelet-derived Growth Factor (PDGF) Receptor for PDGF-AA and PDGF-BB Binding
J. Biol. Chem., November 17, 1995; 270(46): 27595 - 27600.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1993 by the American Association of Cancer Research.