Platelet protein S directly inhibits procoagulant activity on platelets and microparticles
| Autor: | Nicole F. Davis, Erning Duan, Fabian Stavenuiter, Mary J. Heeb, Andrew J. Gale |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Blood Platelets
0301 basic medicine Lipoproteins Blotting Western Stimulation Factor VIIa 030204 cardiovascular system & hematology Article Protein S Thromboplastin Cell-Derived Microparticles 03 medical and health sciences 0302 clinical medicine Thrombin medicine Humans Platelet Blood Coagulation biology Chemistry Hematology Antibodies Neutralizing Molecular biology Blood proteins Kinetics 030104 developmental biology Biochemistry Factor Xa biology.protein Protein C medicine.drug |
| Zdroj: | Thrombosis and Haemostasis. 109:229-237 |
| ISSN: | 2567-689X 0340-6245 |
| DOI: | 10.1160/th12-08-0622 |
| Popis: | SummaryAnticoagulant plasma protein S (PS) is essential for maintaining haemostatic balance. About 2.5% of PS is stored in platelets and released upon platelet stimulation. So far, little is known about the functionality and importance of platelet (plt)PS. A platelet-associated protease cleaves plasma-derived (pd)PS and pltPS in the “thrombin-sensitive region”, abolishing activated protein C (APC) cofactor activity. However, we showed that cleaved PS retains APC-independent anticoagulant activities (“PS-direct”). To investigate whether pltPS or pdPS exert PS-direct on platelets or platelet-shed microparticles, thrombin and factor (F)Xa generation on unstimulated or stimulated washed platelets and microparticles were measured. Western blotting revealed that pltPS and pdPS bound to washed, stimulated platelets and microparticles, and that pltPS had slower electrophoretic mobility than pdPS. Platelet stimulation in the presence of inhibitory anti-PS antibodies resulted in 2.6 ± 1.6-fold (p |
| Databáze: | OpenAIRE |
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