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PRMT5 prognostic value in cancer

Protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues on both histones and non-histone proteins. PRMT5, a member of the PRMT family, is overexpressed in a wide variety of cancers and its activity is associated with cell transformation. Moreover, its expression is...

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Detalles Bibliográficos
Autores principales: Lattouf, Hanine, Poulard, Coralie, Le Romancer, Muriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6516714/
https://www.ncbi.nlm.nih.gov/pubmed/31139329
http://dx.doi.org/10.18632/oncotarget.26883
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author Lattouf, Hanine
Poulard, Coralie
Le Romancer, Muriel
author_facet Lattouf, Hanine
Poulard, Coralie
Le Romancer, Muriel
author_sort Lattouf, Hanine
collection PubMed
description Protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues on both histones and non-histone proteins. PRMT5, a member of the PRMT family, is overexpressed in a wide variety of cancers and its activity is associated with cell transformation. Moreover, its expression is associated with a decrease in patient survival in several cancers, a rationale for developing highly potent inhibitors of its enzymatic activity. However, most studies do not take into account the subcellular localization of PRMT5, which can modify its properties. Indeed, our team recently showed that PRMT5 nuclear expression is associated with prolonged survival. These results corroborated findings in prostate cancer, in which the nuclear fraction of PRMT5 was responsible for inhibiting cell growth, while the cytoplasmic fraction promoted cell growth. In conclusion, this criterion should be evaluated prior to administering PRMT5 inhibitors, which may have adverse effects.
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spelling pubmed-65167142019-05-28 PRMT5 prognostic value in cancer Lattouf, Hanine Poulard, Coralie Le Romancer, Muriel Oncotarget Research Perspective Protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues on both histones and non-histone proteins. PRMT5, a member of the PRMT family, is overexpressed in a wide variety of cancers and its activity is associated with cell transformation. Moreover, its expression is associated with a decrease in patient survival in several cancers, a rationale for developing highly potent inhibitors of its enzymatic activity. However, most studies do not take into account the subcellular localization of PRMT5, which can modify its properties. Indeed, our team recently showed that PRMT5 nuclear expression is associated with prolonged survival. These results corroborated findings in prostate cancer, in which the nuclear fraction of PRMT5 was responsible for inhibiting cell growth, while the cytoplasmic fraction promoted cell growth. In conclusion, this criterion should be evaluated prior to administering PRMT5 inhibitors, which may have adverse effects. Impact Journals LLC 2019-05-07 /pmc/articles/PMC6516714/ /pubmed/31139329 http://dx.doi.org/10.18632/oncotarget.26883 Text en Copyright: © 2019 Lattouf et al. http://creativecommons.org/licenses/by/3.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) (CC-BY), which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Research Perspective
Lattouf, Hanine
Poulard, Coralie
Le Romancer, Muriel
PRMT5 prognostic value in cancer
title PRMT5 prognostic value in cancer
title_full PRMT5 prognostic value in cancer
title_fullStr PRMT5 prognostic value in cancer
title_full_unstemmed PRMT5 prognostic value in cancer
title_short PRMT5 prognostic value in cancer
title_sort prmt5 prognostic value in cancer
topic Research Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6516714/
https://www.ncbi.nlm.nih.gov/pubmed/31139329
http://dx.doi.org/10.18632/oncotarget.26883
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