메뉴 건너뛰기




Volumn 24, Issue 16, 2015, Pages 4636-4647

Epigenetic changes as a common trigger of muscle weakness in congenital myopathies

(18)  Rokach, Ori a   Sekulic Jablanovic, Marijana a   Voermans, Nicol b   Wilmshurst, Jo c   Pillay, Komala c,d   Heytens, Luc e   Zhou, Haiyan f   Muntoni, Francesco f   Gautel, Mathias g   Nevo, Yoram h   Mitrani Rosenbaum, Stella h   Attali, Ruben h   Finotti, Alessia i   Gambari, Roberto i   Mosca, Barbara i   Jungbluth, Heinz j,k   Zorzato, Francesco a,i   Treves, Susan a,i  


Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; MICRORNA; MICRORNA 1; MICRORNA 124; MICRORNA 126; MICRORNA 133; MICRORNA 22; MICRORNA 221; MICRORNA 486; RYANODINE RECEPTOR 1; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; HDAC5 PROTEIN, MOUSE; HISTONE DEACETYLASE; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1, MOUSE;

EID: 84938523445     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv195     Document Type: Article
Times cited : (42)

References (58)
  • 1
    • 85027947938 scopus 로고    scopus 로고
    • Congenital myopathies-clinical features and frequency of individual subtypes diagnosed over a 5-year period in the United Kingdom
    • Maggi, L., Scoto, M., Cirak, S., Robb, S.A., Klein, A., Lillis, S., Cullup, T., Feng, L., Manzur, A.Y., Sewry, C.A. et al. (2013) Congenital myopathies-clinical features and frequency of individual subtypes diagnosed over a 5-year period in the United Kingdom. Neuromuscul. Disord., 23, 195-205.
    • (2013) Neuromuscul. Disord , vol.23 , pp. 195-205
    • Maggi, L.1    Scoto, M.2    Cirak, S.3    Robb, S.A.4    Klein, A.5    Lillis, S.6    Cullup, T.7    Feng, L.8    Manzur, A.Y.9    Sewry, C.A.10
  • 5
    • 0030789142 scopus 로고    scopus 로고
    • Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions
    • Franzini-Armstrong, C. and Protasi, F.G. (1997) Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions. Physiol. Rev., 77, 699-729.
    • (1997) Physiol. Rev , vol.77 , pp. 699-729
    • Franzini-Armstrong, C.1    Protasi, F.G.2
  • 6
    • 44649184084 scopus 로고    scopus 로고
    • Congenital muscle disorders with cores: the ryanodine receptor calcium channel paradigm
    • Treves, S., Jungbluth, H., Muntoni, F. and Zorzato, F. (2008) Congenital muscle disorders with cores: the ryanodine receptor calcium channel paradigm. Curr. Opin. Pharmacol., 8, 319-326.
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 319-326
    • Treves, S.1    Jungbluth, H.2    Muntoni, F.3    Zorzato, F.4
  • 9
    • 0025998134 scopus 로고
    • Population frequencies of inheritedneuromuscular diseases-aworld survey
    • Emery, A.E. (1991) Population frequencies of inheritedneuromuscular diseases-aworld survey. Neuromuscul. Disord., 1, 19-29.
    • (1991) Neuromuscul. Disord , vol.1 , pp. 19-29
    • Emery, A.E.1
  • 12
    • 33748102321 scopus 로고    scopus 로고
    • Muscle-specific microRNA miR-206 promotes muscle differentiation
    • Kim, H.K., Lee, Y.S., Sivaprasad, U., Malhotra, A. and Dutta, A. (2006) Muscle-specific microRNA miR-206 promotes muscle differentiation. J. Cell. Biol., 174, 677-687.
    • (2006) J. Cell. Biol , vol.174 , pp. 677-687
    • Kim, H.K.1    Lee, Y.S.2    Sivaprasad, U.3    Malhotra, A.4    Dutta, A.5
  • 14
    • 84895779700 scopus 로고    scopus 로고
    • Deregulated microRNAs in gastric cancer tissue-derived mesenchymal stem cells: novel biomarkers and a mechanism for gastric cancer
    • Wang, M., Zhao, C., Shi, H., Zhang, B., Zhang, L., Zhang, X., Wang, S., Wu, X., Yang, T., Huang, F. et al. (2014) Deregulated microRNAs in gastric cancer tissue-derived mesenchymal stem cells: novel biomarkers and a mechanism for gastric cancer. Br. J. Cancer., 110, 1199-1210.
    • (2014) Br. J. Cancer , vol.110 , pp. 1199-1210
    • Wang, M.1    Zhao, C.2    Shi, H.3    Zhang, B.4    Zhang, L.5    Zhang, X.6    Wang, S.7    Wu, X.8    Yang, T.9    Huang, F.10
  • 15
    • 84899073542 scopus 로고    scopus 로고
    • MicroRNA-126 modulates the tumor microenvironment by targeting calmodulin-regulated spectrin-associated protein 1 (Camsap1)
    • Sun, X., Wang, Z.M., Song, Y., Tai, X.H., Ji, W.Y. and Gu, H. (2014) MicroRNA-126 modulates the tumor microenvironment by targeting calmodulin-regulated spectrin-associated protein 1 (Camsap1). Int. J. Oncol., 44, 1678-1684.
    • (2014) Int. J. Oncol , vol.44 , pp. 1678-1684
    • Sun, X.1    Wang, Z.M.2    Song, Y.3    Tai, X.H.4    Ji, W.Y.5    Gu, H.6
  • 17
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workmann, J.L. and Kingston, R.E. (1998) Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem., 67, 545-579.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 545-579
    • Workmann, J.L.1    Kingston, R.E.2
  • 18
    • 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
  • 19
    • 77957982588 scopus 로고    scopus 로고
    • microRNA-22, downregulated in hepatocellular carcinoma and correlated with prognosis, suppresses cell proliferation and tumourigenicity
    • Zhang, J., Yang, Y., Yang, T., Liu, Y., Li, A., Fu, S., Wu, M., Pan, Z. and Zhou, W. (2010) microRNA-22, downregulated in hepatocellular carcinoma and correlated with prognosis, suppresses cell proliferation and tumourigenicity. Br. J. Cancer, 103, 1215-1220.
    • (2010) Br. J. Cancer , vol.103 , pp. 1215-1220
    • Zhang, J.1    Yang, Y.2    Yang, T.3    Liu, Y.4    Li, A.5    Fu, S.6    Wu, M.7    Pan, Z.8    Zhou, W.9
  • 21
    • 34447508210 scopus 로고    scopus 로고
    • Mef2s are required for thick filament formation in nascent muscle fibres
    • Hinits, Y. and Hughes, S.M. (2007) Mef2s are required for thick filament formation in nascent muscle fibres. Development, 134, 2511-2519.
    • (2007) Development , vol.134 , pp. 2511-2519
    • Hinits, Y.1    Hughes, S.M.2
  • 22
    • 0032705145 scopus 로고    scopus 로고
    • MEF2: a transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation
    • Naya, F.J. and Olson, E. (1999) MEF2: a transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation. Curr. Opin. Cell Biol., 11, 683-688.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 683-688
    • Naya, F.J.1    Olson, E.2
  • 23
    • 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
  • 24
    • 0030003498 scopus 로고    scopus 로고
    • Regulation of tissue-specific expression of the skeletal muscle ryanodine receptor gene
    • Schmoelzl, S., Leeb, T., Brinkmeier, H., Brem, G. and Brenig, B. (1996) Regulation of tissue-specific expression of the skeletal muscle ryanodine receptor gene. J. Biol. Chem., 271, 4763-4769.
    • (1996) J. Biol. Chem , vol.271 , pp. 4763-4769
    • Schmoelzl, S.1    Leeb, T.2    Brinkmeier, H.3    Brem, G.4    Brenig, B.5
  • 26
    • 77950517340 scopus 로고    scopus 로고
    • Multiminicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene
    • Zhou, H., Lillis, S., Loy, R.E., Ghassemi, F., Rose, M.R., Norwood, F., Mills, K., Al-Sarraj, S., Lane, R.J., Feng, L. et al. (2010) Multiminicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul. Disord., 20, 166-173.
    • (2010) Neuromuscul. Disord , vol.20 , pp. 166-173
    • Zhou, H.1    Lillis, S.2    Loy, R.E.3    Ghassemi, F.4    Rose, M.R.5    Norwood, F.6    Mills, K.7    Al-Sarraj, S.8    Lane, R.J.9    Feng, L.10
  • 27
    • 42949120159 scopus 로고    scopus 로고
    • Nullmutations causing depletion of the type 1 ryanodine receptor (RYR1) are commonly associated with recessive structural congenitalmyopathies with cores
    • Monnier, N., Marty, I., Faure, J., Castiglioni, C., Desnuelle, C., Sacconi, S., Estournet, B., Ferreiro, A., Romero, N., Laquerriere, A. et al. (2008) Nullmutations causing depletion of the type 1 ryanodine receptor (RYR1) are commonly associated with recessive structural congenitalmyopathies with cores. Hum. Mutat., 29, 670-678.
    • (2008) Hum. Mutat , vol.29 , pp. 670-678
    • Monnier, N.1    Marty, I.2    Faure, J.3    Castiglioni, C.4    Desnuelle, C.5    Sacconi, S.6    Estournet, B.7    Ferreiro, A.8    Romero, N.9    Laquerriere, A.10
  • 30
    • 84880960483 scopus 로고    scopus 로고
    • Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression
    • Bruneteau, G., Simonet, T., Bauché, S., Mandjee, N., Malfatti, E., Girard, E., Tanguy, M.L., Behin, A., Khiami, F., Sariali, E. et al. (2013) Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression. Brain, 136, 2359-2368.
    • (2013) Brain , vol.136 , pp. 2359-2368
    • Bruneteau, G.1    Simonet, T.2    Bauché, S.3    Mandjee, N.4    Malfatti, E.5    Girard, E.6    Tanguy, M.L.7    Behin, A.8    Khiami, F.9    Sariali, E.10
  • 32
    • 36348988617 scopus 로고    scopus 로고
    • The histone deacetylase HDAC4 connects neural activity to muscle transcriptional reprogramming
    • Cohen, T.J., Waddell, D.S., Barrientos, T., Lu, Z., Feng, G., Cox, G.A., Bodine, S.C. and Yao, T.P. (2007) The histone deacetylase HDAC4 connects neural activity to muscle transcriptional reprogramming. J. Biol. Chem., 282, 33752-33759.
    • (2007) J. Biol. Chem , vol.282 , pp. 33752-33759
    • Cohen, T.J.1    Waddell, D.S.2    Barrientos, T.3    Lu, Z.4    Feng, G.5    Cox, G.A.6    Bodine, S.C.7    Yao, T.P.8
  • 33
    • 79957948651 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in the treatment of muscular dystrophies: epigenetic drugs for genetic diseases
    • Consalvi, S., Saccone, V., Giordani, L., Minetti, G., Mozzetta, C. and Puri, P.L. (2011) Histone deacetylase inhibitors in the treatment of muscular dystrophies: epigenetic drugs for genetic diseases. Mol. Med., 17, 457-465.
    • (2011) Mol. Med , vol.17 , pp. 457-465
    • Consalvi, S.1    Saccone, V.2    Giordani, L.3    Minetti, G.4    Mozzetta, C.5    Puri, P.L.6
  • 34
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancers, neurological dieases and immune disorders
    • Falkenberg, K.J. and Johnstone, R.W. (2014) Histone deacetylases and their inhibitors in cancers, neurological dieases and immune disorders. Nature Rev. Drug. Discov., 13, 673-691.
    • (2014) Nature Rev. Drug. Discov , vol.13 , pp. 673-691
    • Falkenberg, K.J.1    Johnstone, R.W.2
  • 35
    • 84895440984 scopus 로고    scopus 로고
    • HDAC4: mechanism of regulation and biological functions
    • Wang, Z., Qin, G. and Zhao, T.C. (2014) HDAC4: mechanism of regulation and biological functions. Epigenomics, 6, 139-150.
    • (2014) Epigenomics , vol.6 , pp. 139-150
    • Wang, Z.1    Qin, G.2    Zhao, T.C.3
  • 37
    • 0034635987 scopus 로고    scopus 로고
    • Signal dependent activation of the MEF2 transcription factor by dissociation from histone deacytlases
    • Lu, J., McKinsey, T.A., Nicolm, R.L. and Olson, E.N. (2000) Signal dependent activation of the MEF2 transcription factor by dissociation from histone deacytlases. Proc. Natl Acad. Sci. USA, 97, 4070-4075.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Nicolm, R.L.3    Olson, E.N.4
  • 38
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor MEF2 transcription factor
    • Miska, E.A., Karlsson, C., Langley, E., Nielesen, S.J., Pines, J. and Kouzaridesm, T. (1999) HDAC4 deacetylase associates with and represses the MEF2 transcription factor 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    Nielesen, S.J.4    Pines, J.5    Kouzaridesm, T.6
  • 41
    • 0037064089 scopus 로고    scopus 로고
    • Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells
    • Won, J., Yim, J. and Kim, T.K. (2002) Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells. J. Biol. Chem., 277, 38230-38238.
    • (2002) J. Biol. Chem , vol.277 , pp. 38230-38238
    • Won, J.1    Yim, J.2    Kim, T.K.3
  • 43
    • 79959990071 scopus 로고    scopus 로고
    • Regulation of mammalian DNA methyltransferases: a route to new mechanisms
    • Denis, H., Ndlovu, M.N. and Fuks, F. (2011) Regulation of mammalian DNA methyltransferases: a route to new mechanisms. EMBO Reports, 12, 647-656.
    • (2011) EMBO Reports , vol.12 , pp. 647-656
    • Denis, H.1    Ndlovu, M.N.2    Fuks, F.3
  • 44
    • 84904647822 scopus 로고    scopus 로고
    • DNA methyltransferases: a novel target for prevention and therapy
    • Subramaniam, D., Thombre, R.T., Dhar, A. and Anant, S. (2014) DNA methyltransferases: a novel target for prevention and therapy. Front. Oncol., 4. doi:10.3389/fonc.2014.00080.
    • (2014) Front. Oncol , vol.4
    • Subramaniam, D.1    Thombre, R.T.2    Dhar, A.3    Anant, S.4
  • 47
    • 84877583076 scopus 로고    scopus 로고
    • MicroRNA-22 regulates cardiac hypertrophy and remodeling in response to stress
    • Huang, Z.P., Chen, J., Seok, H.Y., Zhang, Z., Kataoka, M., Hu, X. and Wang, D.Z. (2013) MicroRNA-22 regulates cardiac hypertrophy and remodeling in response to stress. Circ. Res., 112, 1234-1243.
    • (2013) Circ. Res , vol.112 , pp. 1234-1243
    • Huang, Z.P.1    Chen, J.2    Seok, H.Y.3    Zhang, Z.4    Kataoka, M.5    Hu, X.6    Wang, D.Z.7
  • 50
    • 62149107959 scopus 로고    scopus 로고
    • microRNAs and muscle disorders
    • Chen, J.F., Callis, T.E. and Wang, D.Z. (2009) microRNAs and muscle disorders. J. Cell Sci., 122, 13-20.
    • (2009) J. Cell Sci , vol.122 , pp. 13-20
    • Chen, J.F.1    Callis, T.E.2    Wang, D.Z.3
  • 52
    • 84925362874 scopus 로고    scopus 로고
    • Exercise training and DNA methylation in humans
    • Vosin, S., Eynon, N., Yan, X. and Bishop, D.J. (2014) Exercise training and DNA methylation in humans. Acta. Physiol., doi:10.1111/apha.12414.
    • (2014) Acta. Physiol
    • Vosin, S.1    Eynon, N.2    Yan, X.3    Bishop, D.J.4
  • 53
    • 84903786303 scopus 로고    scopus 로고
    • Epigenetic adaptation to regular exercise in humans
    • Ling, C. and Rönn, T. (2014) Epigenetic adaptation to regular exercise in humans. Drug Discov. Today, 19, 1015-1018.
    • (2014) Drug Discov. Today , vol.19 , pp. 1015-1018
    • Ling, C.1    Rönn, T.2
  • 55
    • 0030954428 scopus 로고    scopus 로고
    • CG island methylation changes near the GSTP1 gene in prostatic carcinoma cells detected using the polymerase chain reaction: a new prostate cancer biomarker
    • Lee, W.H., Isaacs, W.B., Bova, G.S. and Nelson, W.G. (1997) CG island methylation changes near the GSTP1 gene in prostatic carcinoma cells detected using the polymerase chain reaction: a new prostate cancer biomarker. Cancer Epidemiol. Biomarkers Prev., 6, 443-450.
    • (1997) Cancer Epidemiol. Biomarkers Prev , vol.6 , pp. 443-450
    • Lee, W.H.1    Isaacs, W.B.2    Bova, G.S.3    Nelson, W.G.4
  • 56
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomericMband: localization of defined domains of myomesin, M-protein and the 250 kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann, W.M.J., Gautel, M., Steiner, F., van der Ven, P.F., Weber, K. and Fürst, D.O. (1996) The structure of the sarcomericMband: localization of defined domains of myomesin, M-protein and the 250 kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol., 134, 1441-1453.
    • (1996) J. Cell Biol , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    van der Ven, P.F.4    Weber, K.5    Fürst, D.O.6
  • 57
    • 80055107411 scopus 로고    scopus 로고
    • DNA transfection of mammalian skeletal muscles using in vivo electroporation
    • DiFranco, M., Quinonez, M., Capote, J. and Vergara, J. (2009) DNA transfection of mammalian skeletal muscles using in vivo electroporation. J. Vis. Exp., pii: 1520. doi:10.3791/1520.
    • (2009) J. Vis. Exp
    • DiFranco, M.1    Quinonez, M.2    Capote, J.3    Vergara, J.4
  • 58
    • 6344278673 scopus 로고    scopus 로고
    • Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease
    • Ducreux, S., Zorzato, F., Müller, C., Sewry, C., Muntoni, F., Quinlivan, R., Restagno, G., Girard, T. and Treves, S. (2004) Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease. J Biol. Chem., 279, 43838-43846.
    • (2004) J Biol. Chem , vol.279 , pp. 43838-43846
    • Ducreux, S.1    Zorzato, F.2    Müller, C.3    Sewry, C.4    Muntoni, F.5    Quinlivan, R.6    Restagno, G.7    Girard, T.8    Treves, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.