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: 雜誌貢獻文章同行評審

79 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)18610-18615
頁數6
期刊Journal of Biological Chemistry
271
發行號31
DOIs
出版狀態已發佈 - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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