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Volumn 23, Issue 22, 2014, Pages 5879-5892

Disruption of both nesprin 1 and desmin results in nuclear anchorage defects and fibrosis in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; DESMIN; HETEROCHROMATIN PROTEIN 1; HETEROCHROMATIN PROTEIN 1BETA; MEMBRANE PROTEIN; NESPRIN 1; UNCLASSIFIED DRUG; NERVE PROTEIN; NUCLEAR PROTEIN; SYNE1 PROTEIN, MOUSE;

EID: 84911394363     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu310     Document Type: Article
Times cited : (47)

References (42)
  • 2
    • 0036021778 scopus 로고    scopus 로고
    • Functional characteristics of dystrophic skeletal muscle: insights from animal models
    • Watchko, J.F., O'Day, T.L. and Hoffman, E.P. (2002) Functional characteristics of dystrophic skeletal muscle: insights from animal models. J. Appl. Physiol., 93, 407-417.
    • (2002) J. Appl. Physiol. , vol.93 , pp. 407-417
    • Watchko, J.F.1    O'Day, T.L.2    Hoffman, E.P.3
  • 3
    • 77956187161 scopus 로고    scopus 로고
    • Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis
    • Brosig, M., Ferralli, J., Gelman, L., Chiquet, M. and Chiquet-Ehrismann, R. (2010) Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis. Int. J. Biochem. Cell Biol., 42, 1717-1728.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 1717-1728
    • Brosig, M.1    Ferralli, J.2    Gelman, L.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 4
    • 34247505044 scopus 로고    scopus 로고
    • Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength
    • Houben, F., Ramaekers, F.C.S., Snoeckx, L.H.E.H. and Broers, J.L.V. (2007) Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength. Biochim. Biophys. Acta, 1773, 675-686.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 675-686
    • Houben, F.1    Ramaekers, F.C.S.2    Snoeckx, L.H.E.H.3    Broers, J.L.V.4
  • 6
    • 84901682377 scopus 로고    scopus 로고
    • Targeted Ablation of Nesprin 1 and Nesprin 2 from murine myocardium results in cardiomyopathy, altered nuclear morphology and inhibition of the biomechanical gene response
    • Banerjee, I., Zhang, J., Moore-Morris, T., Pfeiffer, E., Buchholz, K.S., Liu, A., Ouyang, K., Stroud, M.J., Gerace, L., Evans, S.M. et al. (2014) Targeted Ablation of Nesprin 1 and Nesprin 2 from murine myocardium results in cardiomyopathy, altered nuclear morphology and inhibition of the biomechanical gene response. PLoS Genet., 10, e1004114.
    • (2014) PLoS Genet. , vol.10 , pp. e1004114
    • Banerjee, I.1    Zhang, J.2    Moore-Morris, T.3    Pfeiffer, E.4    Buchholz, K.S.5    Liu, A.6    Ouyang, K.7    Stroud, M.J.8    Gerace, L.9    Evans, S.M.10
  • 8
    • 84894136024 scopus 로고    scopus 로고
    • Linker of nucleoskeleton and cytoskeleton complex proteins in cardiac structure, function, and disease
    • Stroud, M.J., Banerjee, I., Veevers, J. and Chen, J. (2014) Linker of nucleoskeleton and cytoskeleton complex proteins in cardiac structure, function, and disease. Circ. Res., 114, 538-548.
    • (2014) Circ. Res. , vol.114 , pp. 538-548
    • Stroud, M.J.1    Banerjee, I.2    Veevers, J.3    Chen, J.4
  • 9
    • 0042164479 scopus 로고    scopus 로고
    • 108th ENMC international workshop, 3rd workshop of the MYO-CLUSTER project: EUROMEN, 7th international emery-dreifuss muscular dystrophy (EDMD) workshop, 13-15 September 2002, Naarden, The Netherlands
    • Bonne, G., Yaou, R.Ben, Béroud, C., Boriani, G., Brown, S., De Visser, M., Duboc, D., Ellis, J., Hausmanowa-Petrusewicz, I., Lattanzi, G. et al. (2003) 108th ENMC international workshop, 3rd workshop of the MYO-CLUSTER project: EUROMEN, 7th international emery-dreifuss muscular dystrophy (EDMD) workshop, 13-15 September 2002, Naarden, The Netherlands. Neuromuscul. Disord., 13, 508-515.
    • (2003) Neuromuscul. Disord. , vol.13 , pp. 508-515
    • Bonne, G.1    Yaou, R.B.2    Béroud, C.3    Boriani, G.4    Brown, S.5    De Visser, M.6    Duboc, D.7    Ellis, J.8    Hausmanowa-Petrusewicz, I.9    Lattanzi, G.10
  • 11
    • 35748935532 scopus 로고    scopus 로고
    • Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity
    • Zhang, Q., Bethmann, C., Worth, N.F., Davies, J.D., Wasner, C., Feuer, A., Ragnauth, C.D., Yi, Q., Mellad, J.a., Warren, D.T. et al. (2007) Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity. Hum. Mol. Gen., 16, 2816-2833.
    • (2007) Hum. Mol. Gen. , vol.16 , pp. 2816-2833
    • Zhang, Q.1    Bethmann, C.2    Worth, N.F.3    Davies, J.D.4    Wasner, C.5    Feuer, A.6    Ragnauth, C.D.7    Yi, Q.8    Mellad, J.A.9    Warren, D.T.10
  • 12
    • 84861843663 scopus 로고    scopus 로고
    • Skeletal muscle fibrosis develops in response to desmin deletion
    • Meyer, G.A. and Lieber, R.L. (2012) Skeletal muscle fibrosis develops in response to desmin deletion. Am. J. Physiol. Cell Physiol., 302, C1609-C1620.
    • (2012) Am. J. Physiol. Cell Physiol. , vol.302 , pp. C1609-C1620
    • Meyer, G.A.1    Lieber, R.L.2
  • 13
    • 30844461349 scopus 로고    scopus 로고
    • Nesprins: intracellular scaffolds that maintain cell architecture and coordinate cell function? Expert Rev
    • Warren, D.T., Zhang, Q., Weissberg, P.L. and Shanahan, C.M. (2005) Nesprins: intracellular scaffolds that maintain cell architecture and coordinate cell function? Expert Rev. Mol. Med., 7, 1-15.
    • (2005) Mol. Med. , vol.7 , pp. 1-15
    • Warren, D.T.1    Zhang, Q.2    Weissberg, P.L.3    Shanahan, C.M.4
  • 14
    • 14944383270 scopus 로고    scopus 로고
    • Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle
    • Zhang, Q., Ragnauth, C.D., Skepper, J.N., Worth, N.F., Warren, D.T., Roberts, R.G., Weissberg, P.L., Ellis, J.a. and Shanahan, C.M. (2005) Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle. J. Cell Sci., 118, 673-687.
    • (2005) J. Cell Sci. , vol.118 , pp. 673-687
    • Zhang, Q.1    Ragnauth, C.D.2    Skepper, J.N.3    Worth, N.F.4    Warren, D.T.5    Roberts, R.G.6    Weissberg, P.L.7    Ellis, J.A.8    Shanahan, C.M.9
  • 15
    • 59149085789 scopus 로고    scopus 로고
    • Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms
    • Simpson, J.G. and Roberts, R.G. (2008) Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms. Biochem. Soc. Trans., 36, 1359-1367.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1359-1367
    • Simpson, J.G.1    Roberts, R.G.2
  • 16
    • 84863613755 scopus 로고    scopus 로고
    • Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds
    • Rajgor, D., Mellad, J.a., Autore, F., Zhang, Q. and Shanahan, C.M. (2012) Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds. PLOS ONE, 7, e40098.
    • (2012) PLOS ONE , vol.7
    • Rajgor, D.1    Mellad, J.A.2    Autore, F.3    Zhang, Q.4    Shanahan, C.M.5
  • 17
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Zhen, Y.-Y., Libotte, T., Munck,M., Noegel, A.a. and Korenbaum, E. (2002) NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J. Cell Sci., 115, 3207-3222.
    • (2002) J. Cell Sci. , vol.115 , pp. 3207-3222
    • Zhen, Y.-Y.1    Libotte, T.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 20
    • 81855220949 scopus 로고    scopus 로고
    • Nesprin-3: a versatile connector between the nucleus and the cytoskeleton
    • Ketema, M. and Sonnenberg, A. (2011) Nesprin-3: a versatile connector between the nucleus and the cytoskeleton. Biochem. Soc. Trans., 39, 1719-1724.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1719-1724
    • Ketema, M.1    Sonnenberg, A.2
  • 22
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner, D.J., Weitzer, G., Tran, D., Bradley, A. and Capetanaki, Y. (1996) Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol., 134, 1255-1270.
    • (1996) J. Cell Biol. , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 23
    • 0030879081 scopus 로고    scopus 로고
    • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle
    • Li, Z., Mericskay, M., Agbulut, O., Butler-Browne, G., Carlsson, L., Thornell, L.E., Babinet, C. and Paulin, D. (1997) Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J. Cell Biol., 139, 129-144.
    • (1997) J. Cell Biol. , vol.139 , pp. 129-144
    • Li, Z.1    Mericskay, M.2    Agbulut, O.3    Butler-Browne, G.4    Carlsson, L.5    Thornell, L.E.6    Babinet, C.7    Paulin, D.8
  • 24
    • 6344260556 scopus 로고    scopus 로고
    • Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle
    • Paulin, D. and Li, Z. (2004) Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp. Cell Res., 301, 1-7.
    • (2004) Exp. Cell Res. , vol.301 , pp. 1-7
    • Paulin, D.1    Li, Z.2
  • 25
    • 0030966537 scopus 로고    scopus 로고
    • Desmin in muscle formation and maintenance: knockouts and consequences
    • Capetanaki, Y., Milner, D.J. and Weitzer, G. (1997) Desmin in muscle formation and maintenance: knockouts and consequences. Cell Struct. Funct., 22, 103-116.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 103-116
    • Capetanaki, Y.1    Milner, D.J.2    Weitzer, G.3
  • 26
    • 0018869798 scopus 로고
    • Modified assay for determination in a tissue hydrolyzate of hydroxyproline
    • Edwards, C. and O'Brien, W. (1980) Modified assay for determination in a tissue hydrolyzate of hydroxyproline. Clin. Chim. Acta, 104, 161-167.
    • (1980) Clin. Chim. Acta , vol.104 , pp. 161-167
    • Edwards, C.1    O'Brien, W.2
  • 27
    • 69549133935 scopus 로고    scopus 로고
    • Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum
    • Lange, S., Ouyang, K., Meyer, G., Cui, L., Cheng, H., Lieber, R.L. and Chen, J. (2009) Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum. J. Cell Sci., 122, 2640-2650.
    • (2009) J. Cell Sci. , vol.122 , pp. 2640-2650
    • Lange, S.1    Ouyang, K.2    Meyer, G.3    Cui, L.4    Cheng, H.5    Lieber, R.L.6    Chen, J.7
  • 28
    • 1842733449 scopus 로고    scopus 로고
    • HP1 and the dynamics of heterochromatin maintenance
    • Maison, C. and Almouzni, G. (2004) HP1 and the dynamics of heterochromatin maintenance. Nat. Rev. Mol. Cell Biol., 5, 296-304.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 296-304
    • Maison, C.1    Almouzni, G.2
  • 32
    • 13844280986 scopus 로고    scopus 로고
    • Mutations in the heterochromatin protein 1 (HP1) hinge domain affect HP1 protein interactions and chromosomal distribution
    • Badugu, R., Yoo, Y., Singh, P.B. and Kellum, R. (2005) Mutations in the heterochromatin protein 1 (HP1) hinge domain affect HP1 protein interactions and chromosomal distribution. Chromosoma, 113, 370-384.
    • (2005) Chromosoma , vol.113 , pp. 370-384
    • Badugu, R.1    Yoo, Y.2    Singh, P.B.3    Kellum, R.4
  • 33
    • 2142646426 scopus 로고    scopus 로고
    • TGF-beta signaling and the fibrotic response
    • Leask, A. and Abraham, D.J. (2004) TGF-beta signaling and the fibrotic response. FASEB J., 18, 816-827.
    • (2004) FASEB J. , vol.18 , pp. 816-827
    • Leask, A.1    Abraham, D.J.2
  • 34
    • 0025098828 scopus 로고
    • Collagen cross-linking in adult patients with acute and chronic fibrotic lung disease: molecular markers for fibrotic collagen
    • Last, J.A., King, T.E., Nerlich, A.G. and Reiser, K.M. (1990) Collagen cross-linking in adult patients with acute and chronic fibrotic lung disease: molecular markers for fibrotic collagen. Am. J. Respir. Crit. Care Med., 141, 307-313.
    • (1990) Am. J. Respir. Crit. Care Med. , vol.141 , pp. 307-313
    • Last, J.A.1    King, T.E.2    Nerlich, A.G.3    Reiser, K.M.4
  • 35
    • 84865497468 scopus 로고    scopus 로고
    • Collagen cross-linking but not collagen amount associates with elevated filling pressures in hypertensive patients with stage C heart failure: potential role of lysyl oxidase
    • López, B., Querejeta, R., González, A., Larman, M. and Díez, J. (2012) Collagen cross-linking but not collagen amount associates with elevated filling pressures in hypertensive patients with stage C heart failure: potential role of lysyl oxidase. Hypertension, 60, 677-683.
    • (2012) Hypertension , vol.60 , pp. 677-683
    • López, B.1    Querejeta, R.2    González, A.3    Larman, M.4    Díez, J.5
  • 36
    • 0141746289 scopus 로고    scopus 로고
    • Number and spatial distribution of nuclei in the muscle fibres of normal mice studied in vivo
    • Bruusgaard, J.C., Liestøl, K., Ekmark, M., Kollstad, K. and Gundersen, K. (2003) Number and spatial distribution of nuclei in the muscle fibres of normal mice studied in vivo. J. Physiol., 551, 467-478.
    • (2003) J. Physiol. , vol.551 , pp. 467-478
    • Bruusgaard, J.C.1    Liestøl, K.2    Ekmark, M.3    Kollstad, K.4    Gundersen, K.5
  • 37
    • 0033679588 scopus 로고    scopus 로고
    • Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles
    • Sam, M., Shah, S., Fridén, J., Milner, D.J., Capetanaki, Y. and Lieber, R.L. (2000) Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles. Am. J. Physiol. Cell Physiol., 279, C1116-C1122.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279 , pp. C1116-C1122
    • Sam, M.1    Shah, S.2    Fridén, J.3    Milner, D.J.4    Capetanaki, Y.5    Lieber, R.L.6
  • 38
    • 0037310975 scopus 로고    scopus 로고
    • Spastic muscle cells are shorter and stiffer than normal cells
    • Friden, J. and Lieber, R.L. (2003) Spastic muscle cells are shorter and stiffer than normal cells. Muscle Nerve, 26, 157-164.
    • (2003) Muscle Nerve , vol.26 , pp. 157-164
    • Friden, J.1    Lieber, R.L.2
  • 39
    • 79955482311 scopus 로고    scopus 로고
    • Muscle extracellular matrix applies a transverse stress on fibers with axial strain
    • Smith, L.R., Fowler-Gerace, L.H., Gerace-Fowler, L. and Lieber, R.L. (2011) Muscle extracellular matrix applies a transverse stress on fibers with axial strain. J. Biomech., 44, 1618-1620.
    • (2011) J. Biomech. , vol.44 , pp. 1618-1620
    • Smith, L.R.1    Fowler-Gerace, L.H.2    Gerace-Fowler, L.3    Lieber, R.L.4
  • 42
    • 0037252444 scopus 로고    scopus 로고
    • Simultaneous imaging and functional assessment of cytoskeletal protein connections in passively loaded single muscle cells
    • Shah, S.B. and Lieber, R.L. (2003) Simultaneous imaging and functional assessment of cytoskeletal protein connections in passively loaded single muscle cells. J. Histochem. Cytochem., 51, 19-29.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 19-29
    • Shah, S.B.1    Lieber, R.L.2


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