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Blood, 1 December 2000, Vol. 96, No. 12, pp. 3772-3778
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Vascular endothelial growth factor binds to fibrinogen and fibrin
and stimulates endothelial cell proliferation
Abha Sahni and
Charles W. Francis
From the Vascular Medicine Unit, Department of
Medicine, University of Rochester School of Medicine and Dentistry,
Rochester, NY.
Vascular development and response to injury are regulated by
several cytokines and growth factors including the members of the
fibroblast growth factor and vascular endothelial cell growth factor
(VEGF) families. Fibrinogen and fibrin are also important in these
processes and affect many endothelial cell properties. Possible
specific interactions between VEGF and fibrinogen that could play a
role in coordinating vascular responses to injury are investigated.
Binding studies using the 165 amino acid form of VEGF immobilized on
Sepharose beads and soluble iodine 125 (125I)-labeled
fibrinogen demonstrated saturable and specific binding. Scatchard
analysis indicated 2 classes of binding sites with dissociation constants (Kds) of 5.9 and 462 nmol/L.
The maximum molar binding ratio of VEGF:fibrinogen was 3.8:1. Further
studies characterized binding to fibrin using 125I-labeled
VEGF- and Sepharose-immobilized fibrin monomer. These also demonstrated
specific and saturable binding with 2 classes of sites having
Kds of 0.13 and 97 nmol/L and a molar binding ratio of 3.6:1. Binding to polymerized fibrin demonstrated one binding
site with a Kd of 9.3 nmol/L. Binding of VEGF
to fibrin(ogen) was independent of FGF-2, indicating that there are
distinct binding sites for each angiogenic peptide. VEGF bound to
soluble fibrinogen in medium and to surface immobilized fibrinogen or
fibrin retained its capacity to support endothelial cell proliferation.
VEGF binds specifically and saturably to fibrinogen and fibrin with
high affinity, and this may affect the localization and activity of VEGF at sites of tissue injury.
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