Critical residues of integrin αIIb subunit for binding of αIIbβ3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3)

Tetsuji Kamata, Atsushi Irie, Michihide Tokuhira, Yoshikazu Takada

研究成果: Article査読

83 被引用数 (Scopus)

抄録

Integrin αIIbβ3 plays a critical role in platelet aggregation through its interaction with fibrinogen. Elucidation of the mechanisms of αIIbβ3- fibrinogen interaction is critical to understanding hemostasis and thrombosis. Here we report that mutations of Gly-184, Tyr-189, Tyr-190, Phe- 191, and Gly-193 within the predicted turn structure of the third amino- terminal repeat of αIIb significantly block binding of αIIbβ3 to soluble fibrinogen. These mutations also block binding of αIIbβ3 to ligand-mimetic monoclonal antibodies PAC-1, OP-G2, LJ-CP3, which have an RGD-related RYD sequence in their antigen-binding sites. These mutations do not significantly affect the expression of αIIbβ3, in contrast to most of the natural αIIb mutations occurring in Glanzmann's thrombasthenic patients. The data suggest that these residues are critically involved in αIIbβ3-ligand interactions.

本文言語English
ページ(範囲)18610-18615
ページ数6
ジャーナルJournal of Biological Chemistry
271
31
DOI
出版ステータスPublished - 1996
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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