메뉴 건너뛰기




Volumn 41, Issue 6, 2013, Pages 3551-3562

Epigenetic control of type 2 and 3 deiodinases in myogenesis: Role of Lysine-specific Demethylase enzyme and FoxO3

Author keywords

[No Author keywords available]

Indexed keywords

DNA; LYSINE SPECIFIC DEMETHYLASE 1; OXYGENASE; THYROID HORMONE; THYROXINE 5 DEIODINASE; THYROXINE 5 DEIODINASE 2; THYROXINE 5 DEIODINASE 3; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG;

EID: 84876033991     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt065     Document Type: Article
Times cited : (33)

References (39)
  • 1
    • 0009295670 scopus 로고    scopus 로고
    • The link between chromatin structure, protein acetylation and cellular differentiation
    • Sartorelli,V. and Puri, P.L. (2001) The link between chromatin structure, protein acetylation and cellular differentiation. Front Biosci., 6, D1024-D1047.
    • (2001) Front Biosci. , vol.6
    • Sartorelli, V.1    Puri, P.L.2
  • 2
    • 24344491888 scopus 로고    scopus 로고
    • MyoD and the transcriptional control of myogenesis
    • Berkes, C.A. and Tapscott, S.J. (2005) MyoD and the transcriptional control of myogenesis. Semin. Cell Dev. Biol., 16, 585-595.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 585-595
    • Berkes, C.A.1    Tapscott, S.J.2
  • 3
    • 24344472628 scopus 로고    scopus 로고
    • Signaling to the chromatin during skeletal myogenesis: Novel targets for pharmacological modulation of gene expression
    • Forcales, S.V. and Puri, P.L. (2005) Signaling to the chromatin during skeletal myogenesis: novel targets for pharmacological modulation of gene expression. Semin. Cell Dev. Biol., 16, 596-611.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 596-611
    • Forcales, S.V.1    Puri, P.L.2
  • 4
    • 24344497824 scopus 로고    scopus 로고
    • Mechanisms underlying the transcriptional regulation of skeletal myogenesis
    • Sartorelli,V. and Caretti, G. (2005) Mechanisms underlying the transcriptional regulation of skeletal myogenesis. Curr. Opin. Genet. Dev., 15, 528-535.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 528-535
    • Sartorelli, V.1    Caretti, G.2
  • 6
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., O'Carroll, D., Rea, S., Mechtler,K. and Jenuwein, T. (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature, 410, 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 7
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J.R., Cole, P.A. and Casero, R.A. (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell, 119, 941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7
  • 8
    • 64249138238 scopus 로고    scopus 로고
    • Developmental roles of the histone lysine demethylases
    • Nottke, A., Colaiacovo, M.P. and Shi, Y. (2009) Developmental roles of the histone lysine demethylases. Development, 136, 879-889.
    • (2009) Development , vol.136 , pp. 879-889
    • Nottke, A.1    Colaiacovo, M.P.2    Shi, Y.3
  • 16
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: Biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast,N. and Shi,Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem., 79, 155-179.
    • Annu. Rev. Biochem. , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 17
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • Hou,H. and Yu,H. Structural insights into histone lysine demethylation. Curr. Opin. Struct. Biol., 20, 739-748.
    • Curr. Opin. Struct. Biol. , vol.20 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 19
    • 77958152990 scopus 로고    scopus 로고
    • Histone demethylase LSD1 is required to induce skeletal muscle differentiation by regulating myogenic factors
    • Choi, J., Jang, H., Kim, H., Kim, S.T., Cho, E.J. and Youn, H.D. Histone demethylase LSD1 is required to induce skeletal muscle differentiation by regulating myogenic factors. Biochem. Biophys. Res. Commun., 401, 327-332.
    • Biochem. Biophys. Res. Commun. , vol.401 , pp. 327-332
    • Choi, J.1    Jang, H.2    Kim, H.3    Kim, S.T.4    Cho, E.J.5    Youn, H.D.6
  • 20
    • 84877580572 scopus 로고    scopus 로고
    • The deiodinases and the control of intracellular thyroid hormone signaling during cellular differentiation
    • May 25 (10.1016/j.bbagen.2012.05.007; epub ahead of print)
    • Dentice, M., Marsili, A., Zavacki, A., Larsen, P.R. and Salvatore,D. The deiodinases and the control of intracellular thyroid hormone signaling during cellular differentiation. Biochim. Biophys. Acta., May 25 (10.1016/j.bbagen. 2012.05.007; epub ahead of print).
    • Biochim. Biophys. Acta.
    • Dentice, M.1    Marsili, A.2    Zavacki, A.3    Larsen, P.R.4    Salvatore, D.5
  • 21
    • 39449099628 scopus 로고    scopus 로고
    • Thyroid hormone as a determinant of metabolic and contractile phenotype of skeletal muscle
    • Simonides, W.S. and van Hardeveld, C. (2008) Thyroid hormone as a determinant of metabolic and contractile phenotype of skeletal muscle. Thyroid, 18, 205-216.
    • (2008) Thyroid , vol.18 , pp. 205-216
    • Simonides, W.S.1    Van Hardeveld, C.2
  • 22
    • 85041987831 scopus 로고
    • Clinical observations on thyrotoxicosis coexisting with myotonic dystrophy
    • Peterson, D.M., Bounds, J.V. Jr and Karnes, W.E. (1976) Clinical observations on thyrotoxicosis coexisting with myotonic dystrophy. Mayo. Clin. Proc., 51, 176-179.
    • (1976) Mayo. Clin. Proc. , vol.51 , pp. 176-179
    • Peterson, D.M.1    Bounds Jr., J.V.2    Karnes, W.E.3
  • 25
    • 27644592904 scopus 로고    scopus 로고
    • Pendrin is a novel in vivo downstream target gene of the TTF-1/Nkx-2.1 homeodomain transcription factor in differentiated thyroid cells
    • Dentice, M., Luongo, C., Elefante, A., Ambrosio, R., Salzano, S., Zannini, M., Nitsch, R., Di Lauro, R., Rossi, G., Fenzi, G. et al. (2005) Pendrin is a novel in vivo downstream target gene of the TTF-1/Nkx-2.1 homeodomain transcription factor in differentiated thyroid cells. Mol. Cell. Biol., 25, 10171-10182.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10171-10182
    • Dentice, M.1    Luongo, C.2    Elefante, A.3    Ambrosio, R.4    Salzano, S.5    Zannini, M.6    Nitsch, R.7    Di Lauro, R.8    Rossi, G.9    Fenzi, G.10
  • 26
    • 77954053278 scopus 로고    scopus 로고
    • LSD1-mediated demethylation of histone H3 lysine 4 triggers Myc-induced transcription
    • Amente, S., Bertoni, A., Morano, A., Lania, L., Avvedimento, E.V. and Majello,B. LSD1-mediated demethylation of histone H3 lysine 4 triggers Myc-induced transcription. Oncogene, 29, 3691-3702.
    • Oncogene , vol.29 , pp. 3691-3702
    • Amente, S.1    Bertoni, A.2    Morano, A.3    Lania, L.4    Avvedimento, E.V.5    Majello, B.6
  • 29
    • 79952638585 scopus 로고    scopus 로고
    • Hedgehog-mediated regulation of thyroid hormone action through iodothyronine deiodinases
    • Dentice,M. Hedgehog-mediated regulation of thyroid hormone action through iodothyronine deiodinases. Expert Opin. Ther. Targets, 15, 493-504.
    • Expert Opin. Ther. Targets , vol.15 , pp. 493-504
    • Dentice, M.1
  • 30
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris, F., Binda, C., Adamo, A., Battaglioli,E. and Mattevi, A. (2007) Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem., 282, 20070-20074.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 31
    • 0035794552 scopus 로고    scopus 로고
    • A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: Inhibition of the myogenic program
    • Mal, A., Sturniolo, M., Schiltz, R.L., Ghosh, M.K. and Harter, M.L. (2001) A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program. EMBO J., 20, 1739-1753.
    • (2001) EMBO J. , vol.20 , pp. 1739-1753
    • Mal, A.1    Sturniolo, M.2    Schiltz, R.L.3    Ghosh, M.K.4    Harter, M.L.5
  • 32
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska, E.A., Karlsson, C., Langley, E., Nielsen, S.J., Pines,J. and Kouzarides, T. (1999) HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J., 18, 5099-5107.
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1    Karlsson, C.2    Langley, E.3    Nielsen, S.J.4    Pines, J.5    Kouzarides, T.6
  • 33
    • 0033635242 scopus 로고    scopus 로고
    • Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases
    • Lu, J., McKinsey, T.A., Zhang, C.L. and Olson, E.N. (2000) Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell, 6, 233-244.
    • (2000) Mol. Cell , vol.6 , pp. 233-244
    • Lu, J.1    McKinsey, T.A.2    Zhang, C.L.3    Olson, E.N.4
  • 34
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey, T.A., Zhang, C.L., Lu,J. and Olson, E.N. (2000) Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature, 408, 106-111.
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 35
    • 0037188532 scopus 로고    scopus 로고
    • Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases
    • Iezzi, S., Cossu, G., Nervi, C., Sartorelli,V. and Puri, P.L. (2002) Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases. Proc. Natl Acad. Sci. USA, 99, 7757-7762.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7757-7762
    • Iezzi, S.1    Cossu, G.2    Nervi, C.3    Sartorelli, V.4    Puri, P.L.5
  • 36
    • 2342627231 scopus 로고    scopus 로고
    • Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin
    • Iezzi, S., Di Padova, M., Serra, C., Caretti, G., Simone, C., Maklan, E., Minetti, G., Zhao, P., Hoffman, E.P., Puri, P.L. et al. (2004) Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin. Dev. Cell, 6, 673-684.
    • (2004) Dev. Cell , vol.6 , pp. 673-684
    • Iezzi, S.1    Di Padova, M.2    Serra, C.3    Caretti, G.4    Simone, C.5    Maklan, E.6    Minetti, G.7    Zhao, P.8    Hoffman, E.P.9    Puri, P.L.10
  • 39
    • 53249095869 scopus 로고    scopus 로고
    • Codependent activators direct myoblast-specific MyoD transcription
    • Hu, P., Geles, K.G., Paik, J.H., DePinho, R.A. and Tjian, R. (2008) Codependent activators direct myoblast-specific MyoD transcription. Dev. Cell, 15, 534-546.
    • (2008) Dev. Cell , vol.15 , pp. 534-546
    • Hu, P.1    Geles, K.G.2    Paik, J.H.3    Depinho, R.A.4    Tjian, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.