Protein arginine Methyltransferase 8 gene is expressed in pluripotent stem cells and its expression is modulated by the transcription factor Sox2

Addition of methyl groups to arginine residues is catalyzed by a group of enzymes called Protein Arginine Methyltransferases (Prmt). Although Prmt1 is essential in development, its paralogue Prmt8 has been poorly studied. This gene was reported to be expressed in nervous system and involved in neuro...

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Autor principal: Solari, C.
Otros Autores: Echegaray, C.V, Luzzani, C., Cosentino, M.S, Waisman, A., Petrone, M.V, Francia, M., Sassone, A., Canizo, J., Sevlever, G., Barañao, L., Miriuka, S., Guberman, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Elsevier B.V. 2016
Acceso en línea:Registro en Scopus
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Sumario:Addition of methyl groups to arginine residues is catalyzed by a group of enzymes called Protein Arginine Methyltransferases (Prmt). Although Prmt1 is essential in development, its paralogue Prmt8 has been poorly studied. This gene was reported to be expressed in nervous system and involved in neurogenesis. In this work, we found that Prmt8 is expressed in mouse embryonic stem cells (ESC) and in induced pluripotent stem cells, and modulated along differentiation to neural precursor cells. We found that Prmt8 promoter activity is induced by the pluripotency transcription factors Oct4, Sox2 and Nanog. Moreover, endogenous Prmt8 mRNA levels were reduced in ESC transfected with Sox2 shRNA vector. As a whole, our results indicate that Prmt8 is expressed in pluripotent stem cells and its transcription is modulated by pluripotency transcription factors. These findings suggest that besides its known function in nervous system, Prmt8 could play a role in pluripotent stem cells. © 2016 Elsevier Inc. All rights reserved.
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ISSN:0006291X
DOI:10.1016/j.bbrc.2016.03.077