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Thromb Haemost 2001; 86(01): 34-40
DOI: 10.1055/s-0037-1616198
Research Article
Schattauer GmbH

αIIbβ3 and Its Antagonism at the New Millennium

Edward F. Plow
1   Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, OH, USA
,
Czeslaw S. Cierniewski
2   Department of Biophysics, Medical University in Lodz, Lodz, Poland
,
Zihui Xiao
1   Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, OH, USA
,
Thomas A. Haas
1   Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, OH, USA
,
Tatiana V. Byzova
1   Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, OH, USA
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Publikationsdatum:
12. Dezember 2017 (online)

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Summary

Because of its major role in regulating platelet functions and its prominence on the cell surface, integrin αIIbβ3 has been the subject of intensive investigations. Such studies have provided substantial insights into its structure-function relationships and have led to the development of anti-thrombotic drugs that target the receptor. Nevertheless, recent findings have indicated that our understanding of the structure and function of αIIbβ3 remains inadequate. This article addresses two aspects of still evolving αIIbβ3 function: 1) the interface between αIIbβ3 and the blood coagulation system, resulting from interaction of prothrombin with the receptor; and 2) the molecular basis for recognition of the RGD and the fibrinogen γ-chain peptide ligands by αIIbβ3. As illustrated by these two examples, there is still much to be learned about αIIbβ3 if we are to fully appreciate its functions and its potential as a therapeutic target.

Key words

Anti-thrombotic therapy - integrin αIIbβ3 - adhesive proteins - blood coagulation proteins
 

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