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Volumn 7, Issue 9, 2012, Pages

Nemaline Myopathy-Related Skeletal Muscle α-Actin (ACTA1) Mutation, Asp286Gly, Prevents Proper Strong Myosin Binding and Triggers Muscle Weakness

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTIN; ASPARTIC ACID; GLYCINE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 84866645945     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0045923     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0034906020 scopus 로고    scopus 로고
    • Clinical and genetic heterogeneity in nemaline myopathy-a disease of skeletal muscle thin filaments
    • Sanoudou D, Beggs AH, (2001) Clinical and genetic heterogeneity in nemaline myopathy-a disease of skeletal muscle thin filaments. Trends Mol Med 7: 362-368.
    • (2001) Trends Mol Med , vol.7 , pp. 362-368
    • Sanoudou, D.1    Beggs, A.H.2
  • 2
    • 0032858915 scopus 로고    scopus 로고
    • Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy
    • Nowak KJ, Wattanasirichaigoon D, Goebel HH, Wilce M, Pelin K, et al. (1999) Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. Nat Genet 23: 208-212.
    • (1999) Nat Genet , vol.23 , pp. 208-212
    • Nowak, K.J.1    Wattanasirichaigoon, D.2    Goebel, H.H.3    Wilce, M.4    Pelin, K.5
  • 3
    • 13044312720 scopus 로고    scopus 로고
    • Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy
    • Pelin K, Hilpela P, Donner K, Sewry C, Akkari PA, et al. (1999) Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy. Proc Natl Acad Sci U S A 96: 2305-2310.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2305-2310
    • Pelin, K.1    Hilpela, P.2    Donner, K.3    Sewry, C.4    Akkari, P.A.5
  • 5
    • 0029317232 scopus 로고
    • A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1
    • Laing NG, Wilton SD, Akkari PA, Dorosz S, Boundy K, et al. (1995) A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1. Nat Genet 10: 249.
    • (1995) Nat Genet , vol.10 , pp. 249
    • Laing, N.G.1    Wilton, S.D.2    Akkari, P.A.3    Dorosz, S.4    Boundy, K.5
  • 7
    • 33845977054 scopus 로고    scopus 로고
    • Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2
    • Agrawal PB, Greenleaf RS, Tomczak KK, Lehtokari VL, Wallgren-Pettersson C, et al. (2007) Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 80: 162-167.
    • (2007) Am J Hum Genet , vol.80 , pp. 162-167
    • Agrawal, P.B.1    Greenleaf, R.S.2    Tomczak, K.K.3    Lehtokari, V.L.4    Wallgren-Pettersson, C.5
  • 8
    • 78649796274 scopus 로고    scopus 로고
    • Dominant mutations in KBTBD13, a member of the BTB/Kelch family, cause nemaline myopathy with cores
    • Sambuughin N, Yau KS, Olive M, Duff RM, Bayarsaikhan M, et al. (2010) Dominant mutations in KBTBD13, a member of the BTB/Kelch family, cause nemaline myopathy with cores. Am J Hum Genet 87: 842-847.
    • (2010) Am J Hum Genet , vol.87 , pp. 842-847
    • Sambuughin, N.1    Yau, K.S.2    Olive, M.3    Duff, R.M.4    Bayarsaikhan, M.5
  • 9
    • 79953663838 scopus 로고    scopus 로고
    • Mouse models of dominant ACTA1 disease recapitulate human disease and provide insight into therapies
    • Ravenscroft G, Jackaman C, Bringans S, Papadimitriou JM, Griffiths LM, et al. (2011) Mouse models of dominant ACTA1 disease recapitulate human disease and provide insight into therapies. Brain 134: 1101-1115.
    • (2011) Brain , vol.134 , pp. 1101-1115
    • Ravenscroft, G.1    Jackaman, C.2    Bringans, S.3    Papadimitriou, J.M.4    Griffiths, L.M.5
  • 10
    • 83055164378 scopus 로고    scopus 로고
    • Actin nemaline myopathy mouse reproduces disease, suggests other actin disease phenotypes and provides cautionary note on muscle transgene expression
    • Ravenscroft G, Jackaman C, Sewry CA, McNamara E, Squire SE, et al. (2011) Actin nemaline myopathy mouse reproduces disease, suggests other actin disease phenotypes and provides cautionary note on muscle transgene expression. PLoS One 6: e28699.
    • (2011) PLoS One , vol.6
    • Ravenscroft, G.1    Jackaman, C.2    Sewry, C.A.3    McNamara, E.4    Squire, S.E.5
  • 11
    • 0030741552 scopus 로고    scopus 로고
    • Contractile studies of single human skeletal muscle fibers: a comparison of different muscles, permeabilization procedures, and storage techniques
    • Frontera WR, Larsson L, (1997) Contractile studies of single human skeletal muscle fibers: a comparison of different muscles, permeabilization procedures, and storage techniques. Muscle Nerve 20: 948-952.
    • (1997) Muscle Nerve , vol.20 , pp. 948-952
    • Frontera, W.R.1    Larsson, L.2
  • 12
    • 0018333174 scopus 로고
    • Sarcomere length-tension relations of frog skinned muscle fibres during calcium activation at short lengths
    • Moss RL, (1979) Sarcomere length-tension relations of frog skinned muscle fibres during calcium activation at short lengths. J Physiol 292: 177-192.
    • (1979) J Physiol , vol.292 , pp. 177-192
    • Moss, R.L.1
  • 13
    • 0027763495 scopus 로고
    • Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles
    • Larsson L, Moss RL, (1993) Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. J Physiol 472: 595-614.
    • (1993) J Physiol , vol.472 , pp. 595-614
    • Larsson, L.1    Moss, R.L.2
  • 14
    • 77953088225 scopus 로고    scopus 로고
    • A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation
    • Ochala J, Iwamoto H, Larsson L, Yagi N, (2010) A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation. Proc Natl Acad Sci U S A 107: 9807-9812.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9807-9812
    • Ochala, J.1    Iwamoto, H.2    Larsson, L.3    Yagi, N.4
  • 15
    • 45249099152 scopus 로고    scopus 로고
    • Defective regulation of contractile function in muscle fibres carrying an E41K beta-tropomyosin mutation
    • Ochala J, Li M, Ohlsson M, Oldfors A, Larsson L, (2008) Defective regulation of contractile function in muscle fibres carrying an E41K beta-tropomyosin mutation. J Physiol 586: 2993-3004.
    • (2008) J Physiol , vol.586 , pp. 2993-3004
    • Ochala, J.1    Li, M.2    Ohlsson, M.3    Oldfors, A.4    Larsson, L.5
  • 16
    • 34250009728 scopus 로고    scopus 로고
    • Effects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibres
    • Ochala J, Li M, Tajsharghi H, Kimber E, Tulinius M, et al. (2007) Effects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibres. J Physiol 581: 1283-1292.
    • (2007) J Physiol , vol.581 , pp. 1283-1292
    • Ochala, J.1    Li, M.2    Tajsharghi, H.3    Kimber, E.4    Tulinius, M.5
  • 19
    • 0019305701 scopus 로고
    • All myosin heads form bonds with actin in rigor rabbit skeletal muscle
    • Cooke R, Franks K, (1980) All myosin heads form bonds with actin in rigor rabbit skeletal muscle. Biochemistry 19: 2265-2269.
    • (1980) Biochemistry , vol.19 , pp. 2265-2269
    • Cooke, R.1    Franks, K.2
  • 21
    • 72749126316 scopus 로고    scopus 로고
    • Nebulin plays a direct role in promoting strong actin-myosin interactions
    • Bang ML, Caremani M, Brunello E, Littlefield R, Lieber RL, et al. (2009) Nebulin plays a direct role in promoting strong actin-myosin interactions. FASEB J 23: 4117-4125.
    • (2009) FASEB J , vol.23 , pp. 4117-4125
    • Bang, M.L.1    Caremani, M.2    Brunello, E.3    Littlefield, R.4    Lieber, R.L.5
  • 22
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas
    • Linari M, Caremani M, Piperio C, Brandt P, Lombardi V, (2007) Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas. Biophys J 92: 2476-2490.
    • (2007) Biophys J , vol.92 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 23
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution
    • Brenner B, Eisenberg E, (1986) Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc Natl Acad Sci U S A 83: 3542-3546.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 24
    • 0031920485 scopus 로고    scopus 로고
    • Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle
    • Regnier M, Martyn DA, Chase PB, (1998) Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle. Biophys J 74: 2005-2015.
    • (1998) Biophys J , vol.74 , pp. 2005-2015
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 25
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres
    • Edman KA, (1979) The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J Physiol 291: 143-159.
    • (1979) J Physiol , vol.291 , pp. 143-159
    • Edman, K.A.1
  • 26
    • 58849125703 scopus 로고    scopus 로고
    • Genotype-phenotype correlations in ACTA1 mutations that cause congenital myopathies
    • Feng JJ, Marston S, (2009) Genotype-phenotype correlations in ACTA1 mutations that cause congenital myopathies. Neuromuscul Disord 19: 6-16.
    • (2009) Neuromuscul Disord , vol.19 , pp. 6-16
    • Feng, J.J.1    Marston, S.2
  • 28
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF, (1957) Muscle structure and theories of contraction. Prog Biophys Biophys Chem 7: 255-318.
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 29
    • 0024007477 scopus 로고
    • Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction
    • Brenner B, (1988) Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci U S A 85: 3265-3269.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 30
    • 54249099032 scopus 로고    scopus 로고
    • Thin filament proteins mutations associated with skeletal myopathies: defective regulation of muscle contraction
    • Ochala J, (2008) Thin filament proteins mutations associated with skeletal myopathies: defective regulation of muscle contraction. J Mol Med 86: 1197-1204.
    • (2008) J Mol Med , vol.86 , pp. 1197-1204
    • Ochala, J.1
  • 31
    • 79957918034 scopus 로고    scopus 로고
    • Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy
    • Ochala J, Lehtokari VL, Iwamoto H, Li M, Feng HZ,et al. (2011) Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy. FASEB J.
    • (2011) FASEB J.
    • Ochala, J.1    Lehtokari, V.L.2    Iwamoto, H.3    Li, M.4    Feng, H.Z.5
  • 32
    • 60849116181 scopus 로고    scopus 로고
    • Tropomyosin and the steric mechanism of muscle regulation
    • Lehman W, Craig R, (2008) Tropomyosin and the steric mechanism of muscle regulation. Adv Exp Med Biol 644: 95-109.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 95-109
    • Lehman, W.1    Craig, R.2
  • 33
    • 0000244537 scopus 로고
    • Structural changes in the actin- and myosin-containing filaments during contraction
    • Huxley HE, (1973) Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harbor Symp Quant Biol 37: 361-376.
    • (1973) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 34
    • 79951834827 scopus 로고    scopus 로고
    • Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry
    • Li XE, Tobacman LS, Mun JY, Craig R, Fischer S, et al. (2011) Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry. Biophys J 100: 1005-1013.
    • (2011) Biophys J , vol.100 , pp. 1005-1013
    • Li, X.E.1    Tobacman, L.S.2    Mun, J.Y.3    Craig, R.4    Fischer, S.5
  • 36
    • 56849111197 scopus 로고    scopus 로고
    • Cardiac ca(2+) signaling and ca(2+) sensitizers
    • Endoh M, (2008) Cardiac ca(2+) signaling and ca(2+) sensitizers. Circ J 72: 1915-1925.
    • (2008) Circ J , vol.72 , pp. 1915-1925
    • Endoh, M.1
  • 37
    • 79952781139 scopus 로고    scopus 로고
    • Cardiac myosin activation: a potential therapeutic approach for systolic heart failure
    • Malik FI, Hartman JJ, Elias KA, Morgan BP, Rodriguez H, et al. (2011) Cardiac myosin activation: a potential therapeutic approach for systolic heart failure. Science 331: 1439-1443.
    • (2011) Science , vol.331 , pp. 1439-1443
    • Malik, F.I.1    Hartman, J.J.2    Elias, K.A.3    Morgan, B.P.4    Rodriguez, H.5
  • 38
    • 80052806071 scopus 로고    scopus 로고
    • Cardiac myosin activation part 1: from concept to clinic
    • Malik FI, Morgan BP, (2011) Cardiac myosin activation part 1: from concept to clinic. J Mol Cell Cardiol 51: 454-461.
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 454-461
    • Malik, F.I.1    Morgan, B.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.