The effects of aprotonin on platelets in vitro using whole blood flow cytometry
| Autor: | Sibylle A. Kozek-Langenecker, Takahisa Masaki, Craig D. Kamerath, Syed F. Mohammad, Alfred K. Cheung, Green Wf |
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| Rok vydání: | 2000 |
| Předmět: |
Blood Platelets
Serine Proteinase Inhibitors P-selectin Platelet Aggregation Fibrinogen receptor Platelet Glycoprotein GPIIb-IIIa Complex Platelet Membrane Glycoproteins Pharmacology In Vitro Techniques Fibrinogen Platelet membrane glycoprotein Aprotinin Antigens CD medicine Humans Platelet Receptor business.industry Integrin beta3 Antibodies Monoclonal Flow Cytometry Peptide Fragments Adenosine Diphosphate Anesthesiology and Pain Medicine Biochemistry Receptors Thrombin business hormones hormone substitutes and hormone antagonists medicine.drug |
| Zdroj: | Anesthesia and analgesia. 90(1) |
| ISSN: | 0003-2999 |
| Popis: | UNLABELLED 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. |
| Databáze: | OpenAIRE |
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