| First Author | Banfi C | Year | 2022 |
| Journal | Int J Mol Sci | Volume | 23 |
| Issue | 5 | PubMed ID | 35269975 |
| Mgi Jnum | J:321915 | Mgi Id | MGI:7255774 |
| Doi | 10.3390/ijms23052831 | Citation | Banfi C, et al. (2022) Prenylcysteine Oxidase 1 (PCYOX1), a New Player in Thrombosis. Int J Mol Sci 23(5) |
| abstractText | 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 alphaIIbbeta3 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. |
