Dissociation of Glycoprotein IIb/IIIa Antagonists From Platelets Does Not Result in Fibrinogen Binding or Platelet Aggregation | Zendy

Andrew L. Frelinger | Zendy; Mark I. Furman | Zendy; Lori A. Krueger | Zendy; Marc R. Barnard | Zendy; Alan D. Michelson | Zendy

Open Access

Dissociation of Glycoprotein IIb/IIIa Antagonists From Platelets Does Not Result in Fibrinogen Binding or Platelet Aggregation

Author(s) -

Andrew L. Frelinger,

Mark I. Furman,

Lori A. Krueger,

Marc R. Barnard,

Alan D. Michelson

Publication year - 2001

Publication title -

circulation

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.795

H-Index - 607

eISSN - 1524-4539

pISSN - 0009-7322

DOI - 10.1161/hc3701.095950

Subject(s) - eptifibatide , tirofiban , abciximab , fibrinogen , platelet , medicine , pharmacology , platelet glycoprotein gpiib iiia complex , platelet membrane glycoprotein , platelet aggregation inhibitor , biochemistry , biophysics , chemistry , biology , percutaneous coronary intervention , myocardial infarction , conventional pci

The primary mechanism of action of glycoprotein (GP) IIb/IIIa antagonists is inhibition of the final common pathway of platelet aggregation: fibrinogen binding to the GP IIb/IIIa complex. However, it has been reported that induction of fibrinogen binding and platelet aggregation is an intrinsic prothrombotic property of low-dose GP IIb/IIIa antagonists. These apparently paradoxical results have been extensively referenced in the cardiology literature.

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