| Publications [#64098] of Harold P. Erickson
Papers Published
- Yokoyama, Kenji and Erickson, Harold P. and Ikeda, Yasuo and Takada, Yoshikazu, Identification of amino acid sequences in fibrinogen γ-chain and tenascin C C-terminal domains critical for binding to integrin αvβ3,
Journal of Biological Chemistry, vol. 275 no. 22
(2000),
pp. 16891 - 16898 [jbc.M000610200]
(last updated on 2007/04/15)
Abstract: Integrin αvβ3 recognizes fibrinogen γ, and αE chain C-terminal domains (γ/C and αEC) but does not require the γC dodecapeptide sequence HHLGGAKQAGDV400-411 for binding to γC. We have localized the αvβ3 binding sites in γC using γC-derived synthetic peptides. We found that two peptides GWTVFQKRLDGSV190-202 and GVYYQGGTYSKAS346-358 block the αvβ3 binding to γC or αEC, block the αvβ3-mediated clot retraction, and induce the ligand-induced binding site 2 (LIBS2) epitope in αvβ3. Neither peptide affects fibrinogen binding to αIIbβ3. Scrambled or inverted peptides were not effective. These results suggest that the two γC-derived peptides directly interact with αvβ3 and specifically block αvβ3-γC or αEC interaction. The two sequences are located next to each other in the γC crystal structure, although they are separate in the primary structure. Asp-199, Ser-201, Gin-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 αvβ3 binding sites in fibrinogen γ/C domain. We also found that tenascin C C-terminal fibrinogen-like domain specifically binds to αvβ3. Notably, a peptide WYRNCHRVNLMG-RYGDNNHSQGVNWFHWKG from this domain that includes the sequence corresponding to γ/C GVYYQGGTYSKAS346-358 specifically binds to αvβ3, suggesting that fibrinogen and tenascin C C-terminal domains interact with αvβ3 in a similar manner.
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