메뉴 건너뛰기




Volumn 586, Issue 19, 2012, Pages 3503-3507

Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac α-tropomyosin

Author keywords

Atomic force microscopy; Ca2+ regulation; Muscle thin filament; Persistence length

Indexed keywords

ALPHA TROPOMYOSIN; CALCIUM ION; COMPLEMENTARY DNA;

EID: 84866607365     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.08.005     Document Type: Article
Times cited : (26)

References (34)
  • 1
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • D.F. McKillop, and M.A. Geeves Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament Biophys. J. 65 1993 693 701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 2
    • 84864765314 scopus 로고    scopus 로고
    • 2+ regulatory unit dynamics: Implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy
    • 2+ regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy Front. Physiol. 3 2012 80
    • (2012) Front. Physiol. , vol.3 , pp. 80
    • Loong, C.K.P.1    Badr, M.A.2    Chase, P.B.3
  • 3
    • 84862687135 scopus 로고    scopus 로고
    • Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy
    • C.K.P. Loong, H.-X. Zhou, and P.B. Chase Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy PLoS One 7 2012 e39676
    • (2012) PLoS One , vol.7 , pp. 39676
    • Loong, C.K.P.1    Zhou, H.-X.2    Chase, P.B.3
  • 4
    • 0030761751 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy
    • B.J. Maron Hypertrophic cardiomyopathy Lancet 350 1997 127 133
    • (1997) Lancet , vol.350 , pp. 127-133
    • Maron, B.J.1
  • 6
    • 0033851629 scopus 로고    scopus 로고
    • Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle α-tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay
    • W. Bing, A. Knott, C. Redwood, G. Esposito, I. Purcell, H. Watkins, and S. Marston Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle α-tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay J. Mol. Cell. Cardiol. 32 2000 1489 1498
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1489-1498
    • Bing, W.1    Knott, A.2    Redwood, C.3    Esposito, G.4    Purcell, I.5    Watkins, H.6    Marston, S.7
  • 7
    • 17544393835 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy mutations in troponin i (K183Δ, G203S, K206Q) enhance filament sliding
    • J. Köhler Familial hypertrophic cardiomyopathy mutations in troponin I (K183Δ, G203S, K206Q) enhance filament sliding Physiol. Genomics 14 2003 117 128
    • (2003) Physiol. Genomics , vol.14 , pp. 117-128
    • Köhler, J.1
  • 8
    • 0037050022 scopus 로고    scopus 로고
    • The failing heart
    • J.A. Towbin, and N.E. Bowles The failing heart Nature 415 2002 227 233
    • (2002) Nature , vol.415 , pp. 227-233
    • Towbin, J.A.1    Bowles, N.E.2
  • 9
    • 0038637756 scopus 로고    scopus 로고
    • The role of tropomyosin in the regulation of myocardial contraction and relaxation
    • B.M. Wolska, and D.M.F. Wieczorek The role of tropomyosin in the regulation of myocardial contraction and relaxation Pflügers Arch. 446 2003 1 8
    • (2003) Pflügers Arch. , vol.446 , pp. 1-8
    • Wolska, B.M.1    Wieczorek, D.M.F.2
  • 11
    • 79953055654 scopus 로고    scopus 로고
    • Thin filament mutations: Developing an integrative approach to a complex disorder
    • J.C. Tardiff Thin filament mutations: developing an integrative approach to a complex disorder Circ. Res. 108 2011 765 782
    • (2011) Circ. Res. , vol.108 , pp. 765-782
    • Tardiff, J.C.1
  • 12
  • 13
    • 10044280728 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy mutations in α-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin
    • E. Kremneva, S. Boussouf, O. Nikolaeva, R. Maytum, M.A. Geeves, and D.I. Levitsky Effects of two familial hypertrophic cardiomyopathy mutations in α-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin Biophys. J. 87 2004 3922 3933
    • (2004) Biophys. J. , vol.87 , pp. 3922-3933
    • Kremneva, E.1    Boussouf, S.2    Nikolaeva, O.3    Maytum, R.4    Geeves, M.A.5    Levitsky, D.I.6
  • 14
    • 85066903478 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy-causing mutations on α-tropomyosin structure and function
    • N. Golitsina Effects of two familial hypertrophic cardiomyopathy-causing mutations on α-tropomyosin structure and function Biochemistry 38 1999 3850
    • (1999) Biochemistry , vol.38 , pp. 3850
    • Golitsina, N.1
  • 15
    • 79952189604 scopus 로고    scopus 로고
    • Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin
    • M.C. Mathur, P.B. Chase, and J.M. Chalovich Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin Biochem. Biophys. Res. Commun. 406 2011 74 78
    • (2011) Biochem. Biophys. Res. Commun. , vol.406 , pp. 74-78
    • Mathur, M.C.1    Chase, P.B.2    Chalovich, J.M.3
  • 16
    • 7044286437 scopus 로고    scopus 로고
    • Effects of cardiomyopathic mutations on the biochemical and biophysical properties of the human α-tropomyosin
    • E. Hilario, S.L. da Silva, C.H. Ramos, and M.C. Bertolini Effects of cardiomyopathic mutations on the biochemical and biophysical properties of the human α-tropomyosin Eur. J. Biochem. 271 2004 4132 4140
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4132-4140
    • Hilario, E.1    Da Silva, S.L.2    Ramos, C.H.3    Bertolini, M.C.4
  • 17
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in α-tropomyosin
    • A.N. Chang, K. Harada, M.J. Ackerman, and J.D. Potter Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in α-tropomyosin J. Biol. Chem. 280 2005 34343 34349
    • (2005) J. Biol. Chem. , vol.280 , pp. 34343-34349
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 18
    • 79951828756 scopus 로고    scopus 로고
    • Enhanced active cross-bridges during diastole: Molecular pathogenesis of tropomyosin's HCM mutations
    • F. Bai, A. Weis, A.K. Takeda, P.B. Chase, and M. Kawai Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations Biophys. J. 100 2011 1014 1023
    • (2011) Biophys. J. , vol.100 , pp. 1014-1023
    • Bai, F.1    Weis, A.2    Takeda, A.K.3    Chase, P.B.4    Kawai, M.5
  • 19
    • 84862907792 scopus 로고    scopus 로고
    • Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin
    • F. Wang Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin J. Biomed. Biotechnol. 2011 2011 435271
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 435271
    • Wang, F.1
  • 20
    • 34250174756 scopus 로고    scopus 로고
    • Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments
    • S.E. Boussouf, R. Maytum, K. Jaquet, and M.A. Geeves Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments J. Muscle Res. Cell Motil. 28 2007 49 58
    • (2007) J. Muscle Res. Cell Motil. , vol.28 , pp. 49-58
    • Boussouf, S.E.1    Maytum, R.2    Jaquet, K.3    Geeves, M.A.4
  • 22
    • 0031953771 scopus 로고    scopus 로고
    • Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning
    • T.L. Daniel, A.C. Trimble, and P.B. Chase Compliant realignment of binding sites in muscle: transient behavior and mechanical tuning Biophys. J. 74 1998 1611 1621
    • (1998) Biophys. J. , vol.74 , pp. 1611-1621
    • Daniel, T.L.1    Trimble, A.C.2    Chase, P.B.3
  • 24
    • 84863651301 scopus 로고    scopus 로고
    • Filament compliance influences cooperative activation of thin filaments and the dynamics of force production in skeletal muscle
    • B.C.W. Tanner, T.L. Daniel, and M. Regnier filament compliance influences cooperative activation of thin filaments and the dynamics of force production in skeletal muscle PLoS Comp. Biol. 8 2012 e1002506
    • (2012) PLoS Comp. Biol. , vol.8 , pp. 1002506
    • Tanner, B.C.W.1    Daniel, T.L.2    Regnier, M.3
  • 25
    • 0036924212 scopus 로고    scopus 로고
    • A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers
    • D.A. Martyn, P.B. Chase, M. Regnier, and A.M. Gordon A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers Biophys. J. 83 2002 3425 3434
    • (2002) Biophys. J. , vol.83 , pp. 3425-3434
    • Martyn, D.A.1    Chase, P.B.2    Regnier, M.3    Gordon, A.M.4
  • 26
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • H. Isambert, P. Venier, A.C. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M.F. Carlier Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins J. Biol. Chem. 270 1995 11437 11444
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.F.7
  • 27
    • 84872214935 scopus 로고    scopus 로고
    • Flexibility change in human cardiac α-tropomyosin e180g mutant: Possible link to cardiac hypertrophy
    • C. Loong, H.-X. Zhou, and P.B. Chase flexibility change in human cardiac α-tropomyosin e180g mutant: possible link to cardiac hypertrophy Biophys. J. 100 2011 586a
    • (2011) Biophys. J. , vol.100
    • Loong, C.1    Zhou, H.-X.2    Chase, P.B.3
  • 28
    • 33845326085 scopus 로고    scopus 로고
    • 2+ sensitivity of regulated cardiac thin filament sliding does not depend on myosin isoform
    • 2+ sensitivity of regulated cardiac thin filament sliding does not depend on myosin isoform J. Physiol. 577 2006 935 944
    • (2006) J. Physiol. , vol.577 , pp. 935-944
    • Schoffstall, B.1
  • 29
    • 0018488093 scopus 로고
    • An absolute method for the determination of the persistence length of native DNA from electron micrographs
    • C. Frontali, E. Dore, A. Ferrauto, E. Gratton, A. Bettini, M.R. Pozzan, and E. Valdevit An absolute method for the determination of the persistence length of native DNA from electron micrographs Biopolymers 18 1979 1353 1373
    • (1979) Biopolymers , vol.18 , pp. 1353-1373
    • Frontali, C.1    Dore, E.2    Ferrauto, A.3    Gratton, E.4    Bettini, A.5    Pozzan, M.R.6    Valdevit, E.7
  • 30
    • 0030245149 scopus 로고    scopus 로고
    • Radial distribution function of semiflexible polymers
    • J. Wilhelm, and E. Frey Radial distribution function of semiflexible polymers Phys. Rev. Lett. 77 1996 2581 2584
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 2581-2584
    • Wilhelm, J.1    Frey, E.2
  • 31
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • S.V. Perry Vertebrate tropomyosin: distribution, properties and function J. Muscle Res. Cell Motil. 22 2001 5 49
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 32
    • 34147172853 scopus 로고    scopus 로고
    • Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle
    • T.E. Gillis, D.A. Martyn, A.J. Rivera, and M. Regnier Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle J. Physiol. 580 2007 561 576
    • (2007) J. Physiol. , vol.580 , pp. 561-576
    • Gillis, T.E.1    Martyn, D.A.2    Rivera, A.J.3    Regnier, M.4
  • 33
    • 75949106516 scopus 로고    scopus 로고
    • Echocardiographic strain imaging to assess early and late consequences of sarcomere mutations in hypertrophic cardiomyopathy
    • C.Y. Ho Echocardiographic strain imaging to assess early and late consequences of sarcomere mutations in hypertrophic cardiomyopathy Circ. Cardiovasc. Genet. 2 2009 314 321
    • (2009) Circ. Cardiovasc. Genet. , vol.2 , pp. 314-321
    • Ho, C.Y.1
  • 34
    • 80054770583 scopus 로고    scopus 로고
    • Multi-scale computational models of familial hypertrophic cardiomyopathy: Genotype to phenotype
    • S.G. Campbell, and A.D. McCulloch Multi-scale computational models of familial hypertrophic cardiomyopathy: genotype to phenotype J. R. Soc. Interface 8 2011 1550 1561
    • (2011) J. R. Soc. Interface , vol.8 , pp. 1550-1561
    • Campbell, S.G.1    McCulloch, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.