Prenylcysteine Oxidase 1 (PCYOX1), a New Player in Thrombosis
<p>This record contains raw data related to the article "Prenylcysteine Oxidase 1 (PCYOX1), a New Player in Thrombosis"</p> <p>Abstract: Prenylcysteine Oxidase 1 (PCYOX1) is an enzyme involved in the degradation of prenylated<br> proteins. It is expressed in different tissues including vascular and blood cells. We recently<br> showed that the secretome from Pcyox1-silenced cells reduced platelet adhesion both to fibrinogen<br> and endothelial cells, suggesting a potential contribution of PCYOX1 into thrombus formation. Here,<br> we show that in vivo thrombus formation after FeCl3 injury of the carotid artery was delayed in<br> Pcyox1/ mice, which were also protected from collagen/epinephrine induced thromboembolism.<br> The Pcyox1/ mice displayed normal blood cells count, vascular procoagulant activity and plasma<br> fibrinogen levels. Deletion of Pcyox1 reduced the platelet/leukocyte aggregates in whole blood, as<br> well as the platelet aggregation, the alpha granules release, and the IIb3 integrin activation in<br> platelet-rich plasma, in response to adenosine diphosphate (ADP) or thrombin receptor agonist peptide<br> (TRAP).Washed platelets from the Pcyox1/ and WT animals showed similar phosphorylation<br> pathway activation, adhesion ability and aggregation. The presence of Pcyox1/ plasma impaired<br> agonist-induced WT platelet aggregation. Our findings show that the absence of PCYOX1 results<br> in platelet hypo-reactivity and impaired arterial thrombosis, and indicates that PCYOX1 could be a<br> novel target for antithrombotic drugs.</p>
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