• DOI:10.1097/00000539-200001000-00004
• Corpus ID: 17979814

The Effects of Aprotinin on Platelets In Vitro Using Whole Blood Flow Cytometry

@article{KozekLangenecker2000TheEO,
  title={The Effects of Aprotinin on Platelets In Vitro Using Whole Blood Flow Cytometry},
  author={Sibylle A. Kozek-Langenecker and Fazal S. Mohammad and Takahisa Masaki and Wayne Green and Craig D. Kamerath and Alfred K. Cheung},
  journal={Anesthesia \& Analgesia},
  year={2000},
  volume={90},
  pages={12–16}
}

• S. Kozek-Langenecker, F. S. Mohammad, +3 authors A. Cheung
• Published 1 January 2000
• Biology, Medicine
• Anesthesia & Analgesia

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.