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

This work was funded by the Italian Ministry of Health, Italy (Ricerca Corrente ID 2755301 MPP 1A, ID 2757640MPP 2B and Ricerca Finalizzata RF-2013-02355543)