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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Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-84963647230 
024 7 |2 cas  |a protein arginine methyltransferase; Homeodomain Proteins; Nanog protein, mouse; Octamer Transcription Factor-3; Pou5f1 protein, mouse; PRMT8 protein, mouse; Protein-Arginine N-Methyltransferases; RNA, Small Interfering; Sox2 protein, mouse; SOXB1 Transcription Factors 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BBRCA 
100 1 |a Solari, C. 
245 1 0 |a Protein arginine Methyltransferase 8 gene is expressed in pluripotent stem cells and its expression is modulated by the transcription factor Sox2 
260 |b Elsevier B.V.  |c 2016 
270 1 0 |m Guberman, A.; Laboratorio de Regulación Génica en Células Madre, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Guiraldes 2160, Argentina; email: algub@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a Boyer, L.A., Lee, T.I., Cole, M.F., Johnstone, S.E., Levine, S.S., Zucker, J.P., Core transcriptional regulatory circuitry in human embryonic stem cells (2005) Cell, 122, pp. 947-956. , S0092-8674(05)00825-1 [pii] 
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504 |a Okita, K., Ichisaka, T., Yamanaka, S., Generation of germline-competent induced pluripotent stem cells (2007) Nature, 448, pp. 313-317 
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504 |a Najbauer, J., Johnson, B.A., Young, A.L., Aswad, D.W., Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins (1993) J. Biol. Chem., 268, pp. 10501-10509 
504 |a Bedford, M.T., Richard, S., Arginine methylation an emerging regulator of protein function (2005) Mol. Cell, 18, pp. 263-272 
504 |a Bedford, M.T., Clarke, S.G., Protein arginine methylation in mammals: Who, what, and why (2009) Mol. Cell, 33, pp. 1-13 
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504 |a Pawlak, M.R., Scherer, C.A., Chen, J., Roshon, M.J., Ruley, H.E., Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (2000) Mol. Cell Biol., 20, pp. 4859-4869 
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504 |a Kousaka, A., Mori, Y., Koyama, Y., Taneda, T., Miyata, S., Tohyama, M., The distribution and characterization of endogenous protein arginine N-methyltransferase 8 in mouse CNS (2009) Neuroscience, 163, pp. 1146-1157 
504 |a Zhang, X., Cheng, X., Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides (2003) Structure, 11, pp. 509-520 
504 |a Li, H.-T., Gong, T., Zhou, Z., Liu, Y.-T., Cao, X., He, Y., Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro (2015) Biochem. J., 467, pp. 507-515 
504 |a Lee, W.-C., Lin, W.-L., Matsui, T., Chen, E.S.-W., Wei, T.-Y.W., Lin, W.-H., Protein arginine methyltransferase 8: Tetrameric structure and protein substrate specificity (2015) Biochemistry 
504 |a Toma-Fukai, S., Kim, J.-D., Park, K.-E., Kuwabara, N., Shimizu, N., Krayukuhina, E., Novel helical assembly in arginine methyltransferase 8 (2016) J. Mol. Biol. 
504 |a Sayegh, J., Webb, K., Cheng, D., Bedford, M.T., Clarke, S.G., Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain (2007) J. Biol. Chem., 282, pp. 36444-36453 
504 |a Dillon, M.B.C., Rust, H.L., Thompson, P.R., Mowen, K.A., Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity (2013) J. Biol. Chem., 288, pp. 27872-27880 
504 |a Lin, Y., Tsai, Y.-J., Liu, Y.-F., Cheng, Y.-C., Hung, C.-M., Lee, Y.-J., The critical role of protein arginine methyltransferase prmt8 in zebrafish embryonic and neural development is non-redundant with its paralogue prmt1 (2013) PLoS One, 8, p. e55221 
504 |a Simandi, Z., Czipa, E., Horvath, A., Koszeghy, A., Bordas, C., Póliska, S., PRMT1 and PRMT8 regulate retinoic acid-dependent neuronal differentiation with implications to neuropathology (2015) Stem Cells, 33, pp. 726-741 
504 |a Losino, N., Luzzani, C., Solari, C., Boffi, J., Tisserand, M.L., Sevlever, G., Maintenance of murine embryonic stem cells' self-renewal and pluripotency with increase in proliferation rate by a bovine granulosa cell line-conditioned medium (2011) Stem Cells Dev., 20, pp. 1439-1449 
504 |a Luzzani, C., Solari, C., Losino, N., Ariel, W., Romorini, L., Bluguermann, C., Modulation of chromatin modifying factors' gene expression in embryonic and induced pluripotent stem cells (2011) Biochem. Biophys. Res. Commun., 410, pp. 816-822. , S0006-291X(11)01043-6 [pii] 
504 |a Losino, N., Waisman, A., Solari, C., Luzzani, C., Espinosa, D.F., Sassone, A., EDA-containing fibronectin increases proliferation of embryonic stem cells (2013) PLoS One, 8. , e80681 
504 |a Solari, C., Vázquez Echegaray, C., Cosentino, M.S., Petrone, M.V., Waisman, A., Luzzani, C., Manganese superoxide dismutase gene expression is induced by nanog and oct4, essential pluripotent stem cells' transcription factors (2015) PLoS One, 10. , e0144336 
504 |a Ying, Q.-L., Stavridis, M., Griffiths, D., Li, M., Smith, A., (2003) Conversion of Embryonic Stem Cells into Neuroectodermal Precursors in Adherent Monoculture 
504 |a Solari, C., Losino, N., Luzzani, C., Waisman, A., Bluguermann, C., Questa, M., Induced pluripotent stem cells' self-renewal and pluripotency is maintained by a bovine granulosa cell line-conditioned medium (2011) Biochem. Biophys. Res. Commun., 410, pp. 252-257. , S0006-291X(11)00901-6 [pii] 
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504 |a Kim, J., Chu, J., Shen, X., Wang, J., Orkin, S.H., An extended transcriptional network for pluripotency of embryonic stem cells (2008) Cell, 132, pp. 1049-1061 
504 |a Weng, M.K., Zimmer, B., Pöltl, D., Broeg, M.P., Ivanova, V., Gaspar, J.A., Extensive transcriptional regulation of chromatin modifiers during human neurodevelopment (2012) PLoS One, 7, p. e36708 
504 |a Weng, M.K., Natarajan, K., Scholz, D., Ivanova, V.N., Sachinidis, A., Hengstler, J.G., Lineage-specific regulation of epigenetic modifier genes in human liver and brain (2014) PLoS One, 9, p. e102035 
504 |a Hernandez, S., Dominko, T., Novel protein arginine methyltransferase 8 isoform is essential for cell proliferation (2016) J. Cell. Biochem. 
504 |a Xie, W., Merz, G., Denman, R.B., PH uniquely modulates protein arginine methylation (2011) J. Biophys. Struct. Biol., 3, pp. 49-65 
520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT 2011-2713 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, PIP112-201101-00243, PIP 112-200801-03003 
536 |a Detalles de la financiación: The authors wish to thank to Estefanía Rojas, Marcelo Schultz, Naomi Arakaki, Flavio S. de Souza, Emilly Villodre and Guido Lenz for their helpful assistance. This work was supported by the following grants (to A.G.): ANPCyT , PICT 2011-2713 , CONICET , PIP 112-200801-03003 and PIP112-201101-00243 . CS, MSC, AW and CL are fellows from CONICET. 
593 |a Laboratorio de Regulación Génica en Células Madre, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Guiraldes 2160, Buenos Aires, C1428EGA, Argentina 
593 |a Instituto de Química Biológica - Ciencias Exactas y Naturales (IQUIBICEN), UBA/CONICET, Buenos Aires, Argentina 
593 |a Laboratorio de Investigación Aplicada A Las Neurociencias (LIAN)-CONICET, Fundación Para la Lucha Contra Las Enfermedades Neurológicas de la Infancia (FLENI), Buenos Aires, Argentina 
593 |a Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina 
593 |a Departamento de Fisiología y Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a 4 Ruta 9 Km. 52.5, Escobar, Buenos Aires, B1625XAF, Argentina 
690 1 0 |a EMBRYONIC STEM CELLS 
690 1 0 |a INDUCED PLURIPOTENT STEM CELLS 
690 1 0 |a NANOG 
690 1 0 |a OCT4 
690 1 0 |a PRMT8 
690 1 0 |a SOX2 
690 1 0 |a MESSENGER RNA 
690 1 0 |a OCTAMER TRANSCRIPTION FACTOR 4 
690 1 0 |a PROTEIN ARGININE METHYLTRANSFERASE 
690 1 0 |a PROTEIN ARGININE METHYLTRANSFERASE 8 
690 1 0 |a SHORT HAIRPIN RNA 
690 1 0 |a TRANSCRIPTION FACTOR NANOG 
690 1 0 |a TRANSCRIPTION FACTOR SOX2 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a HOMEODOMAIN PROTEIN 
690 1 0 |a NANOG PROTEIN, MOUSE 
690 1 0 |a OCTAMER TRANSCRIPTION FACTOR 4 
690 1 0 |a POU5F1 PROTEIN, MOUSE 
690 1 0 |a PRMT8 PROTEIN, MOUSE 
690 1 0 |a PROTEIN ARGININE METHYLTRANSFERASE 
690 1 0 |a SMALL INTERFERING RNA 
690 1 0 |a SOX2 PROTEIN, MOUSE 
690 1 0 |a TRANSCRIPTION FACTOR SOX 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a BINDING SITE 
690 1 0 |a CELL DIFFERENTIATION 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a DOWN REGULATION 
690 1 0 |a EMBRYO 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a GENETIC TRANSFECTION 
690 1 0 |a MOUSE 
690 1 0 |a MOUSE EMBRYONIC STEM CELL 
690 1 0 |a NEURAL STEM CELL 
690 1 0 |a NONHUMAN 
690 1 0 |a NUCLEAR REPROGRAMMING 
690 1 0 |a PLURIPOTENT STEM CELL 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROMOTER REGION 
690 1 0 |a UPREGULATION 
690 1 0 |a 3T3 CELL LINE 
690 1 0 |a ANIMAL 
690 1 0 |a CELL DIFFERENTIATION 
690 1 0 |a CYTOLOGY 
690 1 0 |a FIBROBLAST 
690 1 0 |a GENE EXPRESSION REGULATION 
690 1 0 |a METABOLISM 
690 1 0 |a NERVE CELL 
690 1 0 |a PLURIPOTENT STEM CELL 
690 1 0 |a REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION 
690 1 0 |a ANIMALS 
690 1 0 |a CELL DIFFERENTIATION 
690 1 0 |a DOWN-REGULATION 
690 1 0 |a FIBROBLASTS 
690 1 0 |a GENE EXPRESSION REGULATION, ENZYMOLOGIC 
690 1 0 |a HOMEODOMAIN PROTEINS 
690 1 0 |a MICE 
690 1 0 |a NEURONS 
690 1 0 |a NIH 3T3 CELLS 
690 1 0 |a OCTAMER TRANSCRIPTION FACTOR-3 
690 1 0 |a PLURIPOTENT STEM CELLS 
690 1 0 |a PROMOTER REGIONS, GENETIC 
690 1 0 |a PROTEIN-ARGININE N-METHYLTRANSFERASES 
690 1 0 |a REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION 
690 1 0 |a RNA, SMALL INTERFERING 
690 1 0 |a SOXB1 TRANSCRIPTION FACTORS 
690 1 0 |a TRANSFECTION 
700 1 |a Echegaray, C.V. 
700 1 |a Luzzani, C. 
700 1 |a Cosentino, M.S. 
700 1 |a Waisman, A. 
700 1 |a Petrone, M.V. 
700 1 |a Francia, M. 
700 1 |a Sassone, A. 
700 1 |a Canizo, J. 
700 1 |a Sevlever, G. 
700 1 |a Barañao, L. 
700 1 |a Miriuka, S. 
700 1 |a Guberman, A. 
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