Prenylcysteine Oxidase 1 (PCYOX1), a New Player in Thrombosis

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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.