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Volume 271, Number 26, Issue of June 28, 1996 pp. 15724-15728
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Identification of a Novel Binding Site to the Integrin _IIb3 Located in the C-terminal Heparin-binding Domain of Human Plasma Fibronectin

(Received for publication, November 29, 1995, and in revised form, March 11, 1996)

From The First Department of Internal Medicine, Yokohama City University School of Medicine, 3-9 Fukuura, Kanazawa-ku, Yokohama 236, Japan

Fibronectin has been shown to bind to integrin _IIb3 in Arg-Gly-Asp (RGD)-dependent and -independent manners. A recent study has indicated that a 29-kDa dispase-digestive fragment from the C-terminal heparin-binding domain of human plasma fibronectin (lacking RGD sequence) inhibits binding of fibronectin to thrombin-stimulated platelets and ADP-induced aggregation (Tanabe, J., Fujita, H., Iwamatsu, A., Mohri, H., and Ohkubo, T. (1993) J. Biol. Chem. 268, 27143-27147). We provide here the evidence that a peptide corresponding to residues from Ala¹⁷⁰⁴ to Glu¹⁷¹⁸ (designated F1) from this fragment inhibited binding of ¹²⁵I-labeled 29-kDa fragment of fibronectin to thrombin-stimulated platelets and ADP-induced aggregation. The F1 peptide bound directly to _IIb3 integrin receptor. These results indicate that a novel binding site in the C-terminal heparin-binding region of fibronectin is localized within the residues from Ala¹⁷⁰⁴ to Glu¹⁷¹⁸. Binding of ¹²⁵I-labeled 29-kDa fragment of fibronectin to thrombin-stimulated platelets was not inhibited by RGDS peptide and the 12-residue peptide from the cell-binding domain of fibronectin, suggesting that binding site in the C-terminal heparin-binding domain may be different from those of RGDS and the 12-residue peptide. This additional _IIb3-binding domain(s) in fibronectin may also play some role for prevention of thrombus formation by direct interaction with _IIb3.

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