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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.

Publication ,  Journal Article
Yokoyama, K; Erickson, HP; Ikeda, Y; Takada, Y
Published in: J Biol Chem
June 2, 2000

Integrin alpha(v)beta(3) recognizes fibrinogen gamma and alpha(E) chain C-terminal domains (gammaC and alpha(E)C) but does not require the gammaC dodecapeptide sequence HHLGGAKQAGDV(400-411) for binding to gammaC. We have localized the alpha(v)beta(3) binding sites in gammaC using gammaC-derived synthetic peptides. We found that two peptides GWTVFQKRLDGSV(190-202) and GVYYQGGTYSKAS(346-358) block the alpha(v)beta(3) binding to gammaC or alpha(E)C, block the alpha(v)beta(3)-mediated clot retraction, and induce the ligand-induced binding site 2 (LIBS2) epitope in alpha(v)beta(3). Neither peptide affects fibrinogen binding to alpha(IIb)beta(3). Scrambled or inverted peptides were not effective. These results suggest that the two gammaC-derived peptides directly interact with alpha(v)beta(3) and specifically block alpha(v)beta(3)-gammaC or alpha(E)C interaction. The two sequences are located next to each other in the gammaC 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(v)beta(3) binding sites in fibrinogen gammaC domain. We also found that tenascin C C-terminal fibrinogen-like domain specifically binds to alpha(v)beta(3). Notably, a peptide WYRNCHRVNLMGRYGDNNHSQGVNWFHWKG from this domain that includes the sequence corresponding to gammaC GVYYQGGTYSKAS(346-358) specifically binds to alpha(v)beta(3), suggesting that fibrinogen and tenascin C C-terminal domains interact with alpha(v)beta(3) in a similar manner.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

June 2, 2000

Volume

275

Issue

22

Start / End Page

16891 / 16898

Location

United States

Related Subject Headings

  • Tenascin
  • Recombinant Proteins
  • Receptors, Vitronectin
  • Protein Conformation
  • Protein Binding
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • Fibrinogen
  • Cricetinae
 

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Yokoyama, K., Erickson, H. P., Ikeda, Y., & Takada, Y. (2000). Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3. J Biol Chem, 275(22), 16891–16898. https://doi.org/10.1074/jbc.M000610200
Yokoyama, K., H. P. Erickson, Y. Ikeda, and Y. Takada. “Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.J Biol Chem 275, no. 22 (June 2, 2000): 16891–98. https://doi.org/10.1074/jbc.M000610200.
Yokoyama, K., et al. “Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.J Biol Chem, vol. 275, no. 22, June 2000, pp. 16891–98. Pubmed, doi:10.1074/jbc.M000610200.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

June 2, 2000

Volume

275

Issue

22

Start / End Page

16891 / 16898

Location

United States

Related Subject Headings

  • Tenascin
  • Recombinant Proteins
  • Receptors, Vitronectin
  • Protein Conformation
  • Protein Binding
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • Fibrinogen
  • Cricetinae