IMR Press / FBL / Volume 23 / Issue 6 / DOI: 10.2741/4631

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Review

Prenylcysteine oxidase 1, a pro-oxidant enzyme of low density lipoproteins

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1 Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Veterinaria, Instituto de Investigacion Sanitaria de Aragon-Universidad de Zaragoza, Zaragoza, E-50013, Spain
2 Instituto Agroalimentario de Aragon, CITA-Universidad de Zaragoza, Spain
3 Departamento de Farmacologia y Fisiologia, Facultad de Ciencias de la Salud y del Deporte, Instituto de Investigacion Sanitaria de Aragon-Universidad de Zaragoza, Huesca, E-22002, Spain
4 CIBER de Fisiopatologia de la Obesidad y Nutricion, Instituto de Salud Carlos III, Madrid, E-28029, Spain
5 Departamento de Patologia Animal, Facultad de Veterinaria, Instituto de Investigacion Sanitaria de Aragon-Universidad de Zaragoza, Zaragoza, E-50013, Spain
Front. Biosci. (Landmark Ed) 2018, 23(6), 1020–1037; https://doi.org/10.2741/4631
Published: 1 January 2018
Abstract

Elevated levels of low density lipoproteins (LDLs) cause atherosclerotic disease, and proteomic analyses have found that these lipoproteins are endowed with prenylcysteine lyase. This systematic review summarizes current understanding of this enzyme, now known as prenylcysteine oxidase 1 (PCYOX1), which hydrolyzes the thioether bond of prenylcysteines in the final step in the degradation of prenylated proteins, releasing hydrogen peroxide, cysteine and the isoprenoid aldehyde. Despite the high variability of the PCYOX1 gene, no polymorphism has yet been associated with any disease. The liver, which is responsible for vehiculization of the enzyme in lipoproteins, is one of the main organs responsible for its expression, together with the gastrointestinal tract, kidney, male reproductive tissue and muscle. Moreover, although hepatic mRNA expression is sensitive to diet and hormones, the repercussion of these changes in LDLs containing PCYOX1 has not been addressed. One consequence of its elevated activity could be an increase in hydrogen peroxide, which might help to propagate the oxidative burden of LDLs, thus making PCYOX1 a potential pharmacological target and a new biomarker in cardiovascular disease.

Keywords
Prenylcysteine Oxidase 1
PCYOX1
1200015P13Rik
Prenylcysteine Lyase 1
PCL1
Pcly
Review
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