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Blood, 1 December 2004, Vol. 104, No. 12, pp. 3635-3641.
Prepublished online as a Blood First Edition Paper on August 5, 2004; DOI 10.1182/blood-2004-04-1358.
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Submitted April 8, 2004
Accepted July 26, 2004
Stimulation of endothelial cell proliferation by FGF-2 in the presence of fibrinogen requires  v 3
Abha Sahni* and Charles W Francis
Hematology/Oncology Unit, Department of Medicine, University of Rochester School of Medicine & Dentistry, Rochester, NY, USA
* Corresponding author; email: abha_sahni{at}urmc.rochester.edu.
We have shown previously that fibrin(ogen)binding potentiates the capacity of FGF-2 to stimulate EC proliferation. We have now investigated the receptor requirement for EC proliferation by fibrinogen-bound FGF-2. EC were cultured with 25ng/mL FGF-2 with or without 10µg/mL fibrinogen, and proliferation was measured as 3H-thymidine incorporation. Proliferation was increased 2.4 ± 0.5-fold over medium alone with FGF-2 and increased significantly more to 4.0 ± 0.7-fold with fibrinogen and FGF-2 (p<0.005). Addition of 7E3 or LM609, antibodies to  v 3, inhibited EC proliferation with fibrinogen-bound FGF-2 by 80 ± 8% (p < 0.001) or 67 ± 14% (p< 0.002), respectively, to levels significantly less than that observed with FGF-2 alone (p < 0.001). Neither LM609 nor 7E3 exhibited any inhibition of activity with FGF-2 alone. Peptide GRGDS caused dose-dependent inhibition of proliferation by fibrinogen-bound FGF-2 of 31 ± 8%, 45 ± 9%, and 68 ± 11% at 0.25, 0.5, and 1 mM, respectively. Co-immunoprecipitation and immuno-fluorescence studies demonstrated a direct specific association between v3 and FGFR1 in EC and fibroblasts when exposed to both FGF-2 and fibrinogen but not with vitronectin. We conclude that fibrinogen binding of FGF-2 enhances EC proliferation through the coordinated effects of co-localized v3 and FGFR1.
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