메뉴 건너뛰기




Volumn 66, Issue 4, 2009, Pages 179-192

α-skeletal muscle actin mutants causing different congenital myopathies induce similar cytoskeletal defects in cell line cultures

Author keywords

actin mutation; Central core disease; Congenital fibre type disproportion; Muscle cells; Nemaline myopathy

Indexed keywords

ALPHA ACTIN; RYANODINE RECEPTOR;

EID: 63849265594     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20340     Document Type: Article
Times cited : (7)

References (52)
  • 2
    • 33846847708 scopus 로고    scopus 로고
    • Phenotypes of myop- athy-related actin mutants in differentiated C2C12 myotubes
    • Bathe FS, Rommelaere H, Machesky LM. 2007. Phenotypes of myop- athy-related actin mutants in differentiated C2C12 myotubes. BMC Cell Biol 8:2.
    • (2007) BMC Cell Biol , vol.8 , pp. 2
    • Bathe, F.S.1    Rommelaere, H.2    Machesky, L.M.3
  • 3
    • 0035968086 scopus 로고    scopus 로고
    • Disruption of actin filaments causes redistribution of ryanodine receptor Ca2+ channels in honeybee photoreceptor cells
    • Baumann O. 2001. Disruption of actin filaments causes redistribution of ryanodine receptor Ca2+ channels in honeybee photoreceptor cells. Neurosci Lett 306(3):181-184.
    • (2001) Neurosci Lett , vol.306 , Issue.3 , pp. 181-184
    • Baumann, O.1
  • 4
    • 0000792635 scopus 로고
    • Congenital fibre type disproportion
    • Kakulas BA, editor. Clinical studies in myology. International, Amsterdam: Excerpta Medica. p
    • Brooke M. 1973. Congenital fibre type disproportion. In: Kakulas BA, editor. Clinical studies in myology. International Congress Series No. 295. Amsterdam: Excerpta Medica. p 147-159.
    • (1973) Congress Series , vol.295 , pp. 147-159
    • Brooke, M.1
  • 5
    • 0029893860 scopus 로고    scopus 로고
    • Remodeling of cytoskeleton and triads following activation of v-Src tyrosine kinase in quail myotubes
    • Castellani L, Reedy M, Airey JA, Gallo R, Ciotti MT, Falcone G, Alema S. 1996. Remodeling of cytoskeleton and triads following activation of v-Src tyrosine kinase in quail myotubes. J Cell Sci 109(Part 6):1335-1346.
    • (1996) J Cell Sci , vol.109 , Issue.PART 6 , pp. 1335-1346
    • Castellani, L.1    Reedy, M.2    Airey, J.A.3    Gallo, R.4    Ciotti, M.T.5    Falcone, G.6    Alema, S.7
  • 6
    • 27644471429 scopus 로고    scopus 로고
    • A novel X-linked form of congenital fiber-type disproportion
    • Clarke NF, Smith RL, Bahlo M, North KN. 2005. A novel X-linked form of congenital fiber-type disproportion. Ann Neurol 58(5):767-772.
    • (2005) Ann Neurol , vol.58 , Issue.5 , pp. 767-772
    • Clarke, N.F.1    Smith, R.L.2    Bahlo, M.3    North, K.N.4
  • 8
    • 7944229031 scopus 로고    scopus 로고
    • Congenital myopathies: Diseases of the actin cytoskeleton
    • Clarkson E, Costa CF, Machesky LM. 2004. Congenital myopathies: diseases of the actin cytoskeleton. J Pathol 204(4):407-417.
    • (2004) J Pathol , vol.204 , Issue.4 , pp. 407-417
    • Clarkson, E.1    Costa, C.F.2    Machesky, L.M.3
  • 11
    • 0027221634 scopus 로고
    • Missense mutations in the beta-myosin heavy-chain gene cause central core disease in hypertrophic cardiomyopathy
    • Fananapazir L, Dalakas MC, Cyran F, Cohn G, Epstein ND. 1993. Missense mutations in the beta-myosin heavy-chain gene cause central core disease in hypertrophic cardiomyopathy. Proc Natl Acad Sci USA 90(9):3993-3997.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.9 , pp. 3993-3997
    • Fananapazir, L.1    Dalakas, M.C.2    Cyran, F.3    Cohn, G.4    Epstein, N.D.5
  • 12
    • 19044375929 scopus 로고    scopus 로고
    • Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: Reassessing the nosology of early-onset myopathies
    • Ferreiro A, Quijano-Roy S, Pichereau C, Moghadaszadeh B, Goemans N, Bonnemann C, Jungbluth H, Straub V, Villanova M, Leroy JP, et al. 2002. Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am J Hum Genet 71(4):739- 749.
    • (2002) Am J Hum Genet , vol.71 , Issue.4 , pp. 739-749
    • Ferreiro, A.1    Quijano-Roy, S.2    Pichereau, C.3    Moghadaszadeh, B.4    Goemans, N.5    Bonnemann, C.6    Jungbluth, H.7    Straub, V.8    Villanova, M.9    Leroy, J.P.10
  • 13
    • 0027386042 scopus 로고
    • Triad formation: Organization and function of the sarcoplasmic reticulum calcium release channel and triadin in normal and dysgenic muscle in vitro
    • Flucher BE, Andrews SB, Fleicher S, Marks AR, Caswell A, Powell JA. 1993. Triad formation: organization and function of the sarcoplasmic reticulum calcium release channel and triadin in normal and dysgenic muscle in vitro. J Cell Biol 123(5):1161- 1174.
    • (1993) J Cell Biol , vol.123 , Issue.5 , pp. 1161-1174
    • Flucher, B.E.1    Andrews, S.B.2    Fleicher, S.3    Marks, A.R.4    Caswell, A.5    Powell, J.A.6
  • 14
    • 0027986710 scopus 로고
    • Molecular organization of transverse tubule/sarcoplasmic reticulum junctions during development of excitation-contraction coupling in skeletal muscle
    • Flucher BE, Andrews SB, Daniels MP. 1994. Molecular organization of transverse tubule/sarcoplasmic reticulum junctions during development of excitation-contraction coupling in skeletal muscle. Mol Biol Cell 5(10):1105-1118.
    • (1994) Mol Biol Cell , vol.5 , Issue.10 , pp. 1105-1118
    • Flucher, B.E.1    Andrews, S.B.2    Daniels, M.P.3
  • 15
    • 0026776331 scopus 로고
    • A cytoplas- mic chaperonin that catalyzes beta-actin folding
    • Gao Y, Thomas JO, Chow RL, Lee GH, Cowan NJ. 1992. A cytoplas- mic chaperonin that catalyzes beta-actin folding. Cell 69(6):1043-1050.
    • (1992) Cell , vol.69 , Issue.6 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 18
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M. 2000. Regulation of contraction in striated muscle. Physiol Rev 80(2):853-924.
    • (2000) Physiol Rev , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 20
    • 33746009957 scopus 로고    scopus 로고
    • Coordination of metabolic plasticity in skeletal muscle
    • Hood DA, Irrcher I, Ljubicic V, Joseph AM. 2006. Coordination of metabolic plasticity in skeletal muscle. J Exp Biol 209(Part12):2265-2275.
    • (2006) J Exp Biol , vol.209 , Issue.PART12 , pp. 2265-2275
    • Hood, D.A.1    Irrcher, I.2    Ljubicic, V.3    Joseph, A.M.4
  • 21
    • 31944440024 scopus 로고    scopus 로고
    • Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred
    • Hutchinson DO, Charlton A, Laing NG, Ilkovski B, North KN. 2006. Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: clinical and pathological variability within a kindred. Neuromuscul Disord 16(2):113-121.
    • (2006) Neuromuscul Disord , vol.16 , Issue.2 , pp. 113-121
    • Hutchinson, D.O.1    Charlton, A.2    Laing, N.G.3    Ilkovski, B.4    North, K.N.5
  • 22
    • 0028989926 scopus 로고
    • Minicores and con- gential fibre type disproportion observed in a family
    • Jongpiputvanich S, Walsh PJ, Kakulas BA. 1995. Minicores and con- gential fibre type disproportion observed in a family. J Paediatr Child Health 31(3):253-257.
    • (1995) J Paediatr Child Health , vol.31 , Issue.3 , pp. 253-257
    • Jongpiputvanich, S.1    Walsh, P.J.2    Kakulas, B.A.3
  • 24
    • 0024988340 scopus 로고    scopus 로고
    • Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. 1990. Atomic structure of the actin:DNase I complex. Nature 347(6288):37-44. Kaindl AM, Ruschendorf F, Krause S, Goebel HH, Koehler K, Becker C, Pongratz D, Muller-Hocker J, Nurnberg P, Stoltenburg- Didinger G, et al. 2004. Missense mutations of ACTA1 cause dominant congenital myopathy with cores. J Med Genet 41(11):842-848.
    • Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. 1990. Atomic structure of the actin:DNase I complex. Nature 347(6288):37-44. Kaindl AM, Ruschendorf F, Krause S, Goebel HH, Koehler K, Becker C, Pongratz D, Muller-Hocker J, Nurnberg P, Stoltenburg- Didinger G, et al. 2004. Missense mutations of ACTA1 cause dominant congenital myopathy with cores. J Med Genet 41(11):842-848.
  • 26
    • 2942549631 scopus 로고    scopus 로고
    • A novel role for non-muscle gamma-actin in skeletal muscle sarcomere assembly
    • Lloyd CM, Berendse M, Lloyd DG, Schevzov G, Grounds MD. 2004. A novel role for non-muscle gamma-actin in skeletal muscle sarcomere assembly. Exp Cell Res 297(1):82-96.
    • (2004) Exp Cell Res , vol.297 , Issue.1 , pp. 82-96
    • Lloyd, C.M.1    Berendse, M.2    Lloyd, D.G.3    Schevzov, G.4    Grounds, M.D.5
  • 27
    • 0035783077 scopus 로고    scopus 로고
    • Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT
    • McCormack EA, Rohman MJ, Willison KR. 2001. Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT. J Struct Biol 135(2):185-197.
    • (2001) J Struct Biol , vol.135 , Issue.2 , pp. 185-197
    • McCormack, E.A.1    Rohman, M.J.2    Willison, K.R.3
  • 28
    • 0033405787 scopus 로고    scopus 로고
    • A nemaline myopathy mutation in alpha-tropomyosin causes defective regulation of striated muscle force production
    • Michele DE, Albayya FP, Metzger JM. 1999. A nemaline myopathy mutation in alpha-tropomyosin causes defective regulation of striated muscle force production. J Clin Invest 104(11):1575-1581.
    • (1999) J Clin Invest , vol.104 , Issue.11 , pp. 1575-1581
    • Michele, D.E.1    Albayya, F.P.2    Metzger, J.M.3
  • 29
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR. 2000. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2(9):628-636.
    • (2000) Nat Cell Biol , vol.2 , Issue.9 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 30
    • 0034326318 scopus 로고    scopus 로고
    • An autosomal dominant congenital myopathy with cores and rods is associated with a neomuta- tion in the RYR1 gene encoding the skeletal muscle ryanodine receptor
    • Monnier N, Romero NB, Lerale J, Nivoche Y, Qi D, MacLennan DH, Fardeau M, Lunardi J. 2000. An autosomal dominant congenital myopathy with cores and rods is associated with a neomuta- tion in the RYR1 gene encoding the skeletal muscle ryanodine receptor. Hum Mol Genet 9(18):2599-2608.
    • (2000) Hum Mol Genet , vol.9 , Issue.18 , pp. 2599-2608
    • Monnier, N.1    Romero, N.B.2    Lerale, J.3    Nivoche, Y.4    Qi, D.5    MacLennan, D.H.6    Fardeau, M.7    Lunardi, J.8
  • 31
    • 0023802199 scopus 로고
    • Calcitonin gene-related peptide enhances the rate of desensitization of the nicotinic acetylcholine receptor in cultured mouse muscle cells
    • Mulle C, Benoit P, Pinset C, Roa M, Changeux JP. 1988. Calcitonin gene-related peptide enhances the rate of desensitization of the nicotinic acetylcholine receptor in cultured mouse muscle cells. Proc Natl Acad Sci USA 85(15):5728-5732.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.15 , pp. 5728-5732
    • Mulle, C.1    Benoit, P.2    Pinset, C.3    Roa, M.4    Changeux, J.P.5
  • 33
    • 28844496012 scopus 로고    scopus 로고
    • Actin interacts with CCT via discrete binding sites: A binding transition-release model for CCT-mediated actin folding
    • Neirynck K, Waterschoot D, Vandekerckhove J, Ampe C, Romme- laere H. 2006. Actin interacts with CCT via discrete binding sites: a binding transition-release model for CCT-mediated actin folding. J Mol Biol 355(1):124-138.
    • (2006) J Mol Biol , vol.355 , Issue.1 , pp. 124-138
    • Neirynck, K.1    Waterschoot, D.2    Vandekerckhove, J.3    Ampe, C.4    Romme- laere, H.5
  • 35
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein LR, Graceffa P, Dominguez R. 2001. The crystal structure of uncomplexed actin in the ADP state. Science 293(5530):708-711.
    • (2001) Science , vol.293 , Issue.5530 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 36
    • 0034723175 scopus 로고    scopus 로고
    • Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors
    • Rochard P, Rodier A, Casas F, Cassar-Malek I, Marchal-Victorion S, Daury L, Wrutniak C, Cabello G. 2000. Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors. J Biol Chem 275(4):2733-2744.
    • (2000) J Biol Chem , vol.275 , Issue.4 , pp. 2733-2744
    • Rochard, P.1    Rodier, A.2    Casas, F.3    Cassar-Malek, I.4    Marchal-Victorion, S.5    Daury, L.6    Wrutniak, C.7    Cabello, G.8
  • 39
    • 0141706541 scopus 로고    scopus 로고
    • Structural plasticity of functional actin: Pictures of actin binding protein and polymer interfaces
    • Rommelaere H, Waterschoot D, Neirynck K, Vandekerckhove J, Ampe C. 2003. Structural plasticity of functional actin: pictures of actin binding protein and polymer interfaces. Structure11(10):1279-1289.
    • (2003) Structure11 , pp. 1279-1289
    • Rommelaere, H.1    Waterschoot, D.2    Neirynck, K.3    Vandekerckhove, J.4    Ampe, C.5
  • 42
    • 0024543601 scopus 로고
    • An electrophoretic procedure for detecting proteins that bind actin monomers
    • Safer D. 1989. An electrophoretic procedure for detecting proteins that bind actin monomers. Anal Biochem 178(1):32-37.
    • (1989) Anal Biochem , vol.178 , Issue.1 , pp. 32-37
    • Safer, D.1
  • 45
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166(2):368-379.
    • (1987) Anal Biochem , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 46
    • 4444326252 scopus 로고    scopus 로고
    • Actin myopathy with nema- line bodies, intranuclear rods, and a heterozygous mutation in ACTA1 (Asp154Asn)
    • Schroder JM, Durling H, Laing N. 2004. Actin myopathy with nema- line bodies, intranuclear rods, and a heterozygous mutation in ACTA1 (Asp154Asn). Acta Neuropathol (Berl) 108(3):250-256.
    • (2004) Acta Neuropathol (Berl) , vol.108 , Issue.3 , pp. 250-256
    • Schroder, J.M.1    Durling, H.2    Laing, N.3
  • 49
    • 30644474315 scopus 로고    scopus 로고
    • 138th ENMC Workshop: Nemaline myopathy, 20-22 May 2005, Naarden, The Netherlands
    • Wallgren-Pettersson C, Laing NG. 2006. 138th ENMC Workshop: nemaline myopathy, 20-22 May 2005, Naarden, The Netherlands. Neuromuscul Disord 16(1):54-60.
    • (2006) Neuromuscul Disord , vol.16 , Issue.1 , pp. 54-60
    • Wallgren-Pettersson, C.1    Laing, N.G.2
  • 50
    • 0036678723 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release is modulated by actin polymerization
    • Wang Y, Mattson MP, Furukawa K. 2002. Endoplasmic reticulum calcium release is modulated by actin polymerization. J Neuro- chem 82(4):945-952.
    • (2002) J Neuro- chem , vol.82 , Issue.4 , pp. 945-952
    • Wang, Y.1    Mattson, M.P.2    Furukawa, K.3
  • 51
    • 0026083971 scopus 로고
    • Biogenesis of transverse tubules and triads: Immunolocalization of the 1, 4-dihydropyri- dine receptor. TS28, and the ryanodine receptor in rabbit skeletal muscle developing in situ
    • Yuan SH, Arnold W, Jorgensen AO. 1991. Biogenesis of transverse tubules and triads: immunolocalization of the 1, 4-dihydropyri- dine receptor. TS28, and the ryanodine receptor in rabbit skeletal muscle developing in situ. J Cell Biol 112(2):289-301.
    • (1991) J Cell Biol , vol.112 , Issue.2 , pp. 289-301
    • Yuan, S.H.1    Arnold, W.2    Jorgensen, A.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.