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Originally published In Press as doi:10.1074/jbc.M000610200 on March 28, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16891-16898, June 2, 2000
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Identification of Amino Acid Sequences in Fibrinogen gamma -Chain and Tenascin C C-terminal Domains Critical for Binding to Integrin alpha vbeta 3*

Kenji Yokoyama, Harold P. EricksonDagger , Yasuo Ikeda§, and Yoshikazu Takada

From the Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, Dagger  Department of Cell Biology, Duke University School of Medicine, Durham, North Carolina 27710, and § Division of Hematology, Department of Internal Medicine, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan

Integrin alpha vbeta 3 recognizes fibrinogen gamma  and alpha E chain C-terminal domains (gamma C and alpha EC) but does not require the gamma C dodecapeptide sequence HHLGGAKQAGDV400-411 for binding to gamma C. We have localized the alpha vbeta 3 binding sites in gamma C using gamma C-derived synthetic peptides. We found that two peptides GWTVFQKRLDGSV190-202 and GVYYQGGTYSKAS346-358 block the alpha vbeta 3 binding to gamma C or alpha EC, block the alpha vbeta 3-mediated clot retraction, and induce the ligand-induced binding site 2 (LIBS2) epitope in alpha vbeta 3. Neither peptide affects fibrinogen binding to alpha IIbbeta 3. Scrambled or inverted peptides were not effective. These results suggest that the two gamma C-derived peptides directly interact with alpha vbeta 3 and specifically block alpha vbeta 3-gamma C or alpha EC interaction. The two sequences are located next to each other in the gamma C crystal structure, although they are separate in the primary structure. Asp-199, Ser-201, Gln-350, Thr-353, Lys-356, Ala-357, and Ser-358 residues are exposed to the surface. This suggests that the two sequences are part of alpha vbeta 3 binding sites in fibrinogen gamma C domain. We also found that tenascin C C-terminal fibrinogen-like domain specifically binds to alpha vbeta 3. Notably, a peptide WYRNCHRVNLMGRYGDNNHSQGVNWFHWKG from this domain that includes the sequence corresponding to gamma C GVYYQGGTYSKAS346-358 specifically binds to alpha vbeta 3, suggesting that fibrinogen and tenascin C C-terminal domains interact with alpha vbeta 3 in a similar manner.

* This work was supported by National Institutes of Health Grants GM47157 and GM49899 (to Y. T.) and by American Heart Association fellowship 98-84 (to K. Y.). This is Publication 12835-VB from The Scripps Research Institute.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Vascular Biology, CAL-10, The Scripps Research Institute, 10666 North Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-7636; Fax: 858-784-7645; E-mail: takada@scripps.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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