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J Biol Chem, Vol. 274, Issue 42, 30215-30221, October 15, 1999
From the Following tissue injury, a fibrin network formed
at the wound site serves as a scaffold supporting the early migration
of stromal cells needed for wound healing. Growth factors such as insulin-like growth factor-I (IGF-I) concentrate in wounds to stimulate
stromal cell function and proliferation. The ability of IGF-binding
proteins (IGFBPs) such as IGFBP-3 to reduce the rate of IGF-I clearance
from wounds suggests that IGFBP-3 might bind directly to
fibrinogen/fibrin. Studies presented here show that IGFBP-3 does indeed
bind to fibrinogen and fibrin immobilized on immunocapture plates, with
Kd values = 0.67 and 0.70 nM,
respectively, and competitive binding studies suggest that the
IGFBP-3 heparin binding domain may participate in this binding. IGF-I
does not compete for IGFBP-3 binding; instead, IGF-I binds immobilized
IGFBP-3·fibrinogen and IGFBP-3·fibrin complexes with affinity
similar to that of IGF-I for the type I IGF receptor. In the presence
of plasminogen, most IGFBP-3 binds directly to fibrinogen, although
35-40% of the IGFBP-3 binds to fibrinogen-bound plasminogen. IGFBP-3
also binds specifically to native fibrin clots, and addition of
exogenous IGFBP-3 increases IGF-I binding. These studies suggest that
IGF-I can concentrate at wound sites by binding to fibrin-immobilized
IGFBP-3, and that the lower IGF affinity of fibrin-bound IGFBP-3 allows
IGF-I release to type I IGF receptors of stromal cells migrating into
the fibrin clot.
Insulin-like Growth Factor-binding Protein-3 Binds Fibrinogen
and Fibrin
,, Institute for Complex Engineered Systems,
Carnegie Mellon University, Pittsburgh, Pennsylvania 15212 and the
§ Department of Pediatrics, Baylor College of Medicine,
Houston, Texas 77030
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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