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*Department of Anesthesiology, University of Vienna, School of Medicine, Vienna, Austria;
Department of Pathology,
Artificial Heart Laboratory,
§Division of Nephrology & Hypertension, Department of Medicine,
||Huntsman Cancer Institute, University of Utah School of Medicine; and
¶Medical and Research Service, Veterans Affairs Medical Center, Salt Lake City, Utah
Address correspondence and reprint requests to Sibylle A. Kozek-Langenecker, MD, Department of Anesthesiology and General Intensive Care, University of Vienna, Währinger Gürtel 18-20, 1090-Vienna, Austria. Address e-mail to sibylle.kozek-langenecker @univie.ac.at.
We sought to evaluate the effects of aprotinin on the number and function of the platelet glycoprotein (GP) IIb–IIIa receptor and on the expression of P-selectin in vitro in order to gain insight into the potential mechanisms involved in the platelet-protective action of aprotinin during cardiopulmonary bypass. Aprotinin at 50 to 200 kallikrein inhibiting units/mL decreased the expression of activated GP IIb–IIIa complex in response to adenosine diphosphate or thrombin receptor activator peptide 6 in a dose-dependent manner in both citrated and heparinized whole blood experiments. Aprotinin inhibited adenosine diphosphate-induced platelet aggregation, but it exhibited no effect on the expression of GP IIIa and P-selectin. These results indicate that aprotinin interferes with the platelet fibrinogen receptor function during pharmacological activation. Reduced aggregability and platelet adhesion to fibrinogen adsorbed to synthetic surfaces in the presence of aprotinin may prevent platelet consumption during clinical cardiopulmonary bypass. This in vitro study demonstrates that aprotinin decreases the agonist-induced expression of activated GP IIb–IIIa receptors that play a major role in platelet aggregation and adhesion to biomaterial surfaces.
Implications: This in vitro study demonstrates that aprotinin decreases the agonist-induced expression of activated glycoprotein IIb–IIIa receptors that play a major role in platelet aggregation and adhesion to biomaterial surfaces.
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