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Publicaciones > Review

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

Publicado en:Frontiers in bioscience (Landmark edition). 23 (6): 1020-1037 - 2018-01-01 23(6), doi: 10.2741/4631

Afiliaciones

Centro de Investigación y Tecnología Agroalimentaria de Aragón - Entidad de origen
CIBER de Fisiopatología de la Obesidad y Nutrición, Instituto de Salud Carlos III, Madrid, E-28029, Spain. - Autor o Coautor
Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Veterinaria, Instituto de Investigacion Sanitaria de Aragon-Universidad de Zaragoza, Zaragoza, E-50013, Spain, and Instituto Agroalimentario de Aragon,Spain. - Autor o Coautor
Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Veterinaria, Instituto de Investigacion Sanitaria de Aragon-Universidad de Zaragoza, Zaragoza, E-50013, Spain, Josada@unizar.es. - Autor o Coautor
Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Veterinaria, Instituto Investigacion Sanitaria de Aragon (IIS), Universidad de Zaragoza, Spain. - Autor o Coautor
Instituto Agroalimentario de Aragón, CITA-Universidad de Zaragoza, Spain. - Autor o Coautor
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Resúmen

Resúmen: 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.

Palabras clave: 1200015p13rik; Animal; Animals; Carbon-sulfur lyases; Cardiovascular disease; Cardiovascular diseases; Degenerative disease; Enzymology; Gene expression profiling; Genetics; Human; Humans; Lipoproteins, ldl; Liver; Low density lipoprotein; Lyase; Metabolism; Neoplasm; Neoplasms; Neurodegenerative diseases; Pcl1; Pcly; Pcyox1; Pcyox1 protein, human; Polymorphism, single nucleotide; Prenylcysteine lyase 1; Prenylcysteine oxidase 1; Review; Single nucleotide polymorphism

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