Pcyox1l, or Prenylcysteine oxidase 1 like protein, is significantly conserved evolutionarily, with murine and human proteins sharing 94% amino-acid homology. It is involved in modulating the prenylation pathway, which impacts autophagy, cellular viability, and has connections to neutrophil functionality [1].

In gene-knockout studies, loss of Pcyox1l protein leads to significant reductions in the mevalonate pathway, affecting autophagy and cellular viability under homeostatic conditions. Pcyox1l CRISPR-edited neutrophils show deficient bactericidal properties, and Pcyox1l knockout mice are highly susceptible to infection by the gram-negative pathogen Pseudomonas aeruginosa, as evidenced by increased neutrophil infiltrates, hemorrhaging, and reduced bactericidal functionality [1]. In addition, in a deep vein thrombosis (DVT) mouse model, lncRNA Crnde promotes DVT by sequestering miR-181a-5p, which in turn releases the expression of Pcyox1l, aggravating thrombus formation [2].

In conclusion, Pcyox1l is crucial for neutrophil bactericidal activities through its role in the prenylation pathway. Gene knockout mouse models have revealed its significance in infection susceptibility. Additionally, its involvement in the lncRNA-miRNA-mRNA ceRNA network in DVT further highlights its importance in disease-related biological processes [1,2].

References:

1. Petenkova, Anastasiia, Auger, Shelby A, Lamb, Jeffrey, Distefano, Mark D, Gadjeva, Mihaela. 2023. Prenylcysteine oxidase 1 like protein is required for neutrophil bactericidal activities. In Nature communications, 14, 2761. doi:10.1038/s41467-023-38447-z. https://pubmed.ncbi.nlm.nih.gov/37179332/

2. He, Xin, Liu, Yu, Li, Yaozhen, Wu, Kemin. 2023. Long non-coding RNA crnde promotes deep vein thrombosis by sequestering miR-181a-5p away from thrombogenic Pcyox1l. In Thrombosis journal, 21, 44. doi:10.1186/s12959-023-00480-9. https://pubmed.ncbi.nlm.nih.gov/37076891/