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Thromb Haemost 2002; 87(02): 317-322
DOI: 10.1055/s-0037-1612992
Letters to the Editor
Schattauer GmbH

Paradoxical Platelet Activation Was not Observed on Dissociation of Abciximab from GPIIb-IIIa Complexes

Serge Ndoko
1   UMR 5533 CNRS, Hôpital Cardiologique, Pessac, France
,
Christel Poujol
1   UMR 5533 CNRS, Hôpital Cardiologique, Pessac, France
,
Robert Combrié
1   UMR 5533 CNRS, Hôpital Cardiologique, Pessac, France
,
Alan Nurden
1   UMR 5533 CNRS, Hôpital Cardiologique, Pessac, France
,
Paquita Nurden
1   UMR 5533 CNRS, Hôpital Cardiologique, Pessac, France
› Author Affiliations
Further Information

Publication History

Received 10 July 2001

Accepted after resubmission 15 November 2001

Publication Date:
13 December 2017 (online)

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Summary

The ability of abciximab to bind and dissociate from platelets raises the question of the conformational state of GPIIb-IIIa complexes losing abciximab and the risk of paradoxical drug-induced platelet activation. Platelets incubated with abciximab and mixed in vitro with c7E3 Fab-free platelets lost the drug to the new platelets giving a single platelet population with a unimodal abciximab distribution within 17 h. Prelabeling the receiving platelets with phycoerythrin-labeled anti-GPIb monoclonal antibody (MoAb), permitted their identification by flow cytometry. Binding of PAC-1 and AP6, two MoAbs specific for activated GPIIb-IIIa, was then assessed to both losing and receiving platelet populations during transfer of abciximab. The subpopulation losing c7E3 Fab failed to show increased binding of these MoAbs. However, PAC-1 binding increased in both subpopulations after addition of ADP. Thus GPIIb-IIIa complexes are not in an activated state after dissociation of abciximab unless there is an additional source of activation.

Keywords

Platelet activation - GPIIb-IIIa complex - abciximab - antithrombotic therapy
 

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