메뉴 건너뛰기




Volumn 35, Issue 2, 2014, Pages 161-178

Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies

Author keywords

Cardiac troponin C; Dilated cardiomyopathy; Hypertrophic cardiomyopathy; TnI phosphorylation

Indexed keywords

CALCIUM; TROPOMYOSIN; TROPONIN C;

EID: 84904264796     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-014-9382-0     Document Type: Review
Times cited : (27)

References (68)
  • 1
    • 84873025551 scopus 로고    scopus 로고
    • Effect of hypertrophic cardiomyopathy-linked troponin C mutations on the response of reconstituted thin filaments to calcium upon troponin i phosphorylation
    • 1:CAS:528:DC%2BC38Xlt1Ggt7Y%3D 3341542 22489623 10.1021/bi300187k
    • Albury AN, Swindle N, Swartz DR, Tikunova SB (2012) Effect of hypertrophic cardiomyopathy-linked troponin C mutations on the response of reconstituted thin filaments to calcium upon troponin I phosphorylation. Biochemistry 51(17):3614-3621
    • (2012) Biochemistry , vol.51 , Issue.17 , pp. 3614-3621
    • Albury, A.N.1    Swindle, N.2    Swartz, D.R.3    Tikunova, S.B.4
  • 2
    • 37349117667 scopus 로고    scopus 로고
    • Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: Influence of PKA phosphorylation and involvement in cardiomyopathies
    • 1:CAS:528:DC%2BD2sXhsVOlt7rL 18042489 10.1016/j.jmb.2007.10.062
    • Baryshnikova OK, Li MX, Sykes BD (2008a) Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: influence of PKA phosphorylation and involvement in cardiomyopathies. J Mol Biol 375(3):735-751
    • (2008) J Mol Biol , vol.375 , Issue.3 , pp. 735-751
    • Baryshnikova, O.K.1    Li, M.X.2    Sykes, B.D.3
  • 3
    • 53749092307 scopus 로고    scopus 로고
    • The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin i
    • 1:CAS:528:DC%2BD1cXhtFelt7nE 18803402 10.1021/bi801165c
    • Baryshnikova OK, Robertson IM, Mercier P, Sykes BD (2008b) The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I. Biochemistry 47(41):10950-10960
    • (2008) Biochemistry , vol.47 , Issue.41 , pp. 10950-10960
    • Baryshnikova, O.K.1    Robertson, I.M.2    Mercier, P.3    Sykes, B.D.4
  • 4
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin i Ser23/24 phosphorylation
    • 1:CAS:528:DC%2BD2sXltl2nsbk%3D 17446435 10.1161/01.RES.0000267744.92677. 7f
    • Biesiadecki BJ, Kobayashi T, Walker JS, Solaro RJ, de Tombe PP (2007) The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation. Circ Res 100(10):1486-1493
    • (2007) Circ Res , vol.100 , Issue.10 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    Walker, J.S.3    Solaro, R.J.4    De Tombe, P.P.5
  • 5
    • 70349250125 scopus 로고    scopus 로고
    • Identification and functional characterization of cardiac troponin i as a novel disease gene in autosomal dominant dilated cardiomyopathy
    • 1:CAS:528:DC%2BD1MXpsVamsbw%3D 19590045 10.1161/CIRCRESAHA.109.196055
    • Carballo S, Robinson P, Otway R, Fatkin D, Jongbloed JD, de Jonge N, Watkins H (2009) Identification and functional characterization of cardiac troponin I as a novel disease gene in autosomal dominant dilated cardiomyopathy. Circ Res 105(4):375-382
    • (2009) Circ Res , vol.105 , Issue.4 , pp. 375-382
    • Carballo, S.1    Robinson, P.2    Otway, R.3    Fatkin, D.4    Jongbloed, J.D.5    De Jonge, N.6    Watkins, H.7
  • 6
    • 0023007377 scopus 로고
    • The effect of troponin-tropomyosin on the binding of heavy meromyosin to actin in the presence of ATP
    • 1:CAS:528:DyaL28XitVaqtLs%3D 1262680 2937784
    • Chalovich JM, Eisenberg E (1986) The effect of troponin-tropomyosin on the binding of heavy meromyosin to actin in the presence of ATP. J Biol Chem 261(11):5088-5093
    • (1986) J Biol Chem , vol.261 , Issue.11 , pp. 5088-5093
    • Chalovich, J.M.1    Eisenberg, E.2
  • 7
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in alpha-tropomyosin
    • 1:CAS:528:DC%2BD2MXhtVKitrzP 16043485 10.1074/jbc.M505014200
    • Chang AN, Harada K, Ackerman MJ, Potter JD (2005) Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin. J Biol Chem 280(40):34343-34349
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 34343-34349
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 8
    • 84875416080 scopus 로고    scopus 로고
    • Effects of calcium binding and the hypertrophic cardiomyopathy A8V mutation on the dynamic equilibrium between closed and open conformations of the regulatory N-domain of isolated cardiac troponin C
    • 1:CAS:528:DC%2BC3sXivFChu7Y%3D 23425245 10.1021/bi4000172
    • Cordina NM, Liew CK, Gell DA, Fajer PG, Mackay JP, Brown LJ (2013) Effects of calcium binding and the hypertrophic cardiomyopathy A8V mutation on the dynamic equilibrium between closed and open conformations of the regulatory N-domain of isolated cardiac troponin C. Biochemistry 52(11):1950-1962
    • (2013) Biochemistry , vol.52 , Issue.11 , pp. 1950-1962
    • Cordina, N.M.1    Liew, C.K.2    Gell, D.A.3    Fajer, P.G.4    Mackay, J.P.5    Brown, L.J.6
  • 10
    • 0038701678 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy due to sarcomeric gene mutations is characterized by impaired energy metabolism irrespective of the degree of hypertrophy
    • 1:CAS:528:DC%2BD3sXks1ymt7o%3D 12767664 10.1016/S0735-1097(02)03009-7
    • Crilley JG, Boehm EA, Blair E, Rajagopalan B, Blamire AM, Styles P, Watkins H (2003) Hypertrophic cardiomyopathy due to sarcomeric gene mutations is characterized by impaired energy metabolism irrespective of the degree of hypertrophy. J Am Coll Cardiol 41(10):1776-1782
    • (2003) J Am Coll Cardiol , vol.41 , Issue.10 , pp. 1776-1782
    • Crilley, J.G.1    Boehm, E.A.2    Blair, E.3    Rajagopalan, B.4    Blamire, A.M.5    Styles, P.6    Watkins, H.7
  • 11
    • 34247642743 scopus 로고    scopus 로고
    • Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C
    • 1:CAS:528:DC%2BD2sXkvVSmtbc%3D 1852344 17293397 10.1529/biophysj.106. 095406
    • Davis JP, Norman C, Kobayashi T, Solaro RJ, Swartz DR, Tikunova SB (2007) Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C. Biophys J 92(9):3195-3206
    • (2007) Biophys J , vol.92 , Issue.9 , pp. 3195-3206
    • Davis, J.P.1    Norman, C.2    Kobayashi, T.3    Solaro, R.J.4    Swartz, D.R.5    Tikunova, S.B.6
  • 12
    • 41249091458 scopus 로고    scopus 로고
    • Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes
    • 1:CAS:528:DC%2BD1cXhtlyis7o%3D 18063575 10.1074/jbc.M703822200
    • Dong WJ, Xing J, Ouyang Y, An J, Cheung HC (2008) Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes. J Biol Chem 283(6):3424-3432
    • (2008) J Biol Chem , vol.283 , Issue.6 , pp. 3424-3432
    • Dong, W.J.1    Xing, J.2    Ouyang, Y.3    An, J.4    Cheung, H.C.5
  • 13
    • 57749102820 scopus 로고    scopus 로고
    • Challenging current paradigms related to cardiomyopathies. Are changes in the Ca2 + sensitivity of myofilaments containing cardiac troponin C mutations (G159D and L29Q) good predictors of the phenotypic outcomes?
    • 1:CAS:528:DC%2BD1cXhsVSgtrfE 2586272 18820258 10.1074/jbc.M804070200
    • Dweck D, Hus N, Potter JD (2008) Challenging current paradigms related to cardiomyopathies. Are changes in the Ca2 + sensitivity of myofilaments containing cardiac troponin C mutations (G159D and L29Q) good predictors of the phenotypic outcomes? J Biol Chem 283(48):33119-33128
    • (2008) J Biol Chem , vol.283 , Issue.48 , pp. 33119-33128
    • Dweck, D.1    Hus, N.2    Potter, J.D.3
  • 14
    • 77952903869 scopus 로고    scopus 로고
    • A dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin binding
    • 1:CAS:528:DC%2BC3cXmslSnur4%3D 2878500 20371872 10.1074/jbc.M109.064105
    • Dweck D, Reynaldo DP, Pinto JR, Potter JD (2010) A dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin binding. J Biol Chem 285(23):17371-17379
    • (2010) J Biol Chem , vol.285 , Issue.23 , pp. 17371-17379
    • Dweck, D.1    Reynaldo, D.P.2    Pinto, J.R.3    Potter, J.D.4
  • 15
    • 70350448975 scopus 로고    scopus 로고
    • Functional analysis of a unique troponin c mutation, GLY159ASP, that causes familial dilated cardiomyopathy, studied in explanted heart muscle
    • 1:CAS:528:DC%2BD1MXhtV2qs73I 19808376 10.1161/CIRCHEARTFAILURE.108.818237
    • Dyer EC, Jacques AM, Hoskins AC, Ward DG, Gallon CE, Messer AE, Marston SB (2009) Functional analysis of a unique troponin c mutation, GLY159ASP, that causes familial dilated cardiomyopathy, studied in explanted heart muscle. Circ Heart Fail 2(5):456-464
    • (2009) Circ Heart Fail , vol.2 , Issue.5 , pp. 456-464
    • Dyer, E.C.1    Jacques, A.M.2    Hoskins, A.C.3    Ward, D.G.4    Gallon, C.E.5    Messer, A.E.6    Marston, S.B.7
  • 16
    • 0001714579 scopus 로고
    • Third component participating in the superprecipitation of 'natural actomyosin'
    • 1:CAS:528:DyaF2cXisVeksg%3D%3D 14097720 10.1038/2001010a0
    • Ebashi S (1963) Third component participating in the superprecipitation of 'natural actomyosin'. Nature 200:1010
    • (1963) Nature , vol.200 , pp. 1010
    • Ebashi, S.1
  • 17
    • 0013790350 scopus 로고
    • A new protein factor promoting aggregation of tropomyosin
    • 1:CAS:528:DyaF2MXks1Cmsbs%3D 5857096
    • Ebashi S, Kodama A (1965) A new protein factor promoting aggregation of tropomyosin. J Biochem 58(1):107-108
    • (1965) J Biochem , vol.58 , Issue.1 , pp. 107-108
    • Ebashi, S.1    Kodama, A.2
  • 18
    • 0022378036 scopus 로고
    • Calcium-insensitive binding of heavy meromyosin to regulated actin at physiological ionic strength
    • 1:CAS:528:DyaL2MXlslChsb8%3D 2932449
    • el-Saleh SC, Potter JD (1985) Calcium-insensitive binding of heavy meromyosin to regulated actin at physiological ionic strength. J Biol Chem 260(27):14775-14779
    • (1985) J Biol Chem , vol.260 , Issue.27 , pp. 14775-14779
    • El-Saleh, S.C.1    Potter, J.D.2
  • 19
    • 77949366363 scopus 로고    scopus 로고
    • The C terminus of cardiac troponin i stabilizes the Ca2 + -activated state of tropomyosin on actin filaments
    • 1:CAS:528:DC%2BC3cXivV2ks7g%3D 2834238 20035081 10.1161/CIRCRESAHA.109. 210047
    • Galinska A, Hatch V, Craig R, Murphy AM, Van Eyk JE, Wang CL, Foster DB (2010) The C terminus of cardiac troponin I stabilizes the Ca2 + -activated state of tropomyosin on actin filaments. Circ Res 106(4):705-711
    • (2010) Circ Res , vol.106 , Issue.4 , pp. 705-711
    • Galinska, A.1    Hatch, V.2    Craig, R.3    Murphy, A.M.4    Van Eyk, J.E.5    Wang, C.L.6    Foster, D.B.7
  • 20
    • 84867344248 scopus 로고    scopus 로고
    • Cardiomyopathy-related mutations in cardiac troponin C, L29Q and G159D, have divergent effects on rat cardiac myofiber contractile dynamics
    • 3447348 23008774 10.1155/2012/824068
    • Gollapudi SK, Chandra M (2012) Cardiomyopathy-related mutations in cardiac troponin C, L29Q and G159D, have divergent effects on rat cardiac myofiber contractile dynamics. Biochem Res Int 2012:824068
    • (2012) Biochem Res Int , vol.2012 , pp. 824068
    • Gollapudi, S.K.1    Chandra, M.2
  • 21
    • 12544260027 scopus 로고    scopus 로고
    • Inherited cardiomyopathies as a troponin disease
    • 1:CAS:528:DC%2BD2MXotFGisA%3D%3D 15631686 10.2170/jjphysiol.54.307
    • Harada K, Morimoto S (2004) Inherited cardiomyopathies as a troponin disease. Jpn J Physiol 54(4):307-318
    • (2004) Jpn J Physiol , vol.54 , Issue.4 , pp. 307-318
    • Harada, K.1    Morimoto, S.2
  • 22
    • 0035109415 scopus 로고
    • Potter JD (2001) "invited review: Pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation."
    • Hernandez OM, Housmans PR (1985) Potter JD (2001) "Invited review: pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation.". J Appl Physiol 90(3):1125-1136
    • (1985) J Appl Physiol , vol.90 , Issue.3 , pp. 1125-1136
    • Hernandez, O.M.1    Housmans, P.R.2
  • 23
    • 77953023261 scopus 로고    scopus 로고
    • Coding sequence rare variants identified in MYBPC3, MYH6, TPM1, TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated cardiomyopathy
    • 1:CAS:528:DC%2BC3cXmvF2murY%3D 2908892 20215591 10.1161/CIRCGENETICS.109. 912345
    • Hershberger RE, Norton N, Morales A, Li D, Siegfried JD, Gonzalez-Quintana J (2010) Coding sequence rare variants identified in MYBPC3, MYH6, TPM1, TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated cardiomyopathy. Circ Cardiovasc Genet 3(2):155-161
    • (2010) Circ Cardiovasc Genet , vol.3 , Issue.2 , pp. 155-161
    • Hershberger, R.E.1    Norton, N.2    Morales, A.3    Li, D.4    Siegfried, J.D.5    Gonzalez-Quintana, J.6
  • 24
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution
    • 1:CAS:528:DyaL2MXht1Omt7w%3D 3974698 10.1038/313653a0
    • Herzberg O, James MN (1985) Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution. Nature 313(6004):653-659
    • (1985) Nature , vol.313 , Issue.6004 , pp. 653-659
    • Herzberg, O.1    James, M.N.2
  • 25
    • 0035378612 scopus 로고    scopus 로고
    • First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy
    • 1:STN:280:DC%2BD3MzkvVWqsw%3D%3D 11385718 10.1002/humu.1143
    • Hoffmann B, Schmidt-Traub H, Perrot A, Osterziel KJ, Gessner R (2001) First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy. Hum Mutat 17(6):524
    • (2001) Hum Mutat , vol.17 , Issue.6 , pp. 524
    • Hoffmann, B.1    Schmidt-Traub, H.2    Perrot, A.3    Osterziel, K.J.4    Gessner, R.5
  • 26
    • 0028173158 scopus 로고
    • Cytoplasmic free Mg2 + in rat ventricular myocytes studied with the fluorescent indicator furaptra
    • 1:CAS:528:DyaK2MXitFCgtbc%3D 7869599 10.2170/jjphysiol.44.357
    • Hongo K, Konishi M, Kurihara S (1994) Cytoplasmic free Mg2 + in rat ventricular myocytes studied with the fluorescent indicator furaptra. Jpn J Physiol 44(4):357-378
    • (1994) Jpn J Physiol , vol.44 , Issue.4 , pp. 357-378
    • Hongo, K.1    Konishi, M.2    Kurihara, S.3
  • 27
    • 34748913759 scopus 로고    scopus 로고
    • Mutations in the cardiac Troponin C gene are a cause of idiopathic dilated cardiomyopathy in childhood
    • 17977476 10.1017/S1047951107001291
    • Kaski JP, Burch M, Elliott PM (2007) Mutations in the cardiac Troponin C gene are a cause of idiopathic dilated cardiomyopathy in childhood. Cardiol Young 17(6):675-677
    • (2007) Cardiol Young , vol.17 , Issue.6 , pp. 675-677
    • Kaski, J.P.1    Burch, M.2    Elliott, P.M.3
  • 28
    • 0020477578 scopus 로고
    • Phosphorylation of troponin i and phospholamban during catecholamine stimulation of rabbit heart
    • 1:CAS:528:DyaL38XlslCrsbs%3D 6211626 10.1038/298182a0
    • Kranias EG, Solaro RJ (1982) Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature 298(5870):182-184
    • (1982) Nature , vol.298 , Issue.5870 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 29
    • 48849100715 scopus 로고    scopus 로고
    • Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C
    • 1:CAS:528:DC%2BD1cXhtVSjs7bL 2627482 18572189 10.1016/j.yjmcc.2008.05.003
    • Landstrom AP, Parvatiyar MS, Pinto JR, Marquardt ML, Bos JM, Tester DJ, Ackerman MJ (2008) Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C. J Mol Cell Cardiol 45(2):281-288
    • (2008) J Mol Cell Cardiol , vol.45 , Issue.2 , pp. 281-288
    • Landstrom, A.P.1    Parvatiyar, M.S.2    Pinto, J.R.3    Marquardt, M.L.4    Bos, J.M.5    Tester, D.J.6    Ackerman, M.J.7
  • 30
    • 0034671767 scopus 로고    scopus 로고
    • Calcium affinity of regulatory sites in skeletal troponin-C is attenuated by N-cap mutations of helix C
    • 1:CAS:528:DC%2BD3cXoslKmtbY%3D 11368316 10.1006/abbi.2000.2103
    • Leblanc L, Bennet A, Borgford T (2000) Calcium affinity of regulatory sites in skeletal troponin-C is attenuated by N-cap mutations of helix C. Arch Biochem Biophys 384(2):296-304
    • (2000) Arch Biochem Biophys , vol.384 , Issue.2 , pp. 296-304
    • Leblanc, L.1    Bennet, A.2    Borgford, T.3
  • 31
    • 60849116181 scopus 로고    scopus 로고
    • Tropomyosin and the steric mechanism of muscle regulation
    • 1:CAS:528:DC%2BC3cXhsFyjsb%2FL 19209816 10.1007/978-0-387-85766-4-8
    • 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
  • 32
    • 84894137070 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy related cardiac troponin C L29Q mutation alters length-dependent activation and functional effects of phosphomimetic troponin I
    • 3832503 24260207 10.1371/journal.pone.0079363
    • Li AY, Stevens CM, Liang B, Rayani K, Little S, Davis J, Tibbits GF (2013) Familial hypertrophic cardiomyopathy related cardiac troponin C L29Q mutation alters length-dependent activation and functional effects of phosphomimetic troponin I. PLoS ONE 8(11):e79363
    • (2013) PLoS ONE , vol.8 , Issue.11 , pp. 79363
    • Li, A.Y.1    Stevens, C.M.2    Liang, B.3    Rayani, K.4    Little, S.5    Davis, J.6    Tibbits, G.F.7
  • 33
    • 43049104563 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy-related cardiac troponin C mutation L29Q affects Ca2 + binding and myofilament contractility
    • 1:CAS:528:DC%2BD1cXmt1WisLw%3D 18285522 10.1152/physiolgenomics.00154. 2007
    • Liang B, Chung F, Qu Y, Pavlov D, Gillis TE, Tikunova SB, Tibbits GF (2008) Familial hypertrophic cardiomyopathy-related cardiac troponin C mutation L29Q affects Ca2 + binding and myofilament contractility. Physiol Genomics 33(2):257-266
    • (2008) Physiol Genomics , vol.33 , Issue.2 , pp. 257-266
    • Liang, B.1    Chung, F.2    Qu, Y.3    Pavlov, D.4    Gillis, T.E.5    Tikunova, S.B.6    Tibbits, G.F.7
  • 34
    • 43649089498 scopus 로고    scopus 로고
    • A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility
    • 1:CAS:528:DC%2BD1cXltVOhtb8%3D 2292379 18212018 10.1529/biophysj.107. 112896
    • Lim CC, Yang H, Yang M, Wang CK, Shi J, Berg EA, Liao R (2008) A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility. Biophys J 94(9):3577-3589
    • (2008) Biophys J , vol.94 , Issue.9 , pp. 3577-3589
    • Lim, C.C.1    Yang, H.2    Yang, M.3    Wang, C.K.4    Shi, J.5    Berg, E.A.6    Liao, R.7
  • 35
    • 84878956600 scopus 로고    scopus 로고
    • Inherited cardiomyopathies caused by troponin mutations
    • 1:CAS:528:DC%2BC3sXnvVagsb0%3D 3627712 23610579
    • Lu QW, Wu XY, Morimoto S (2013) Inherited cardiomyopathies caused by troponin mutations. J Geriatr Cardiol 10(1):91-101
    • (2013) J Geriatr Cardiol , vol.10 , Issue.1 , pp. 91-101
    • Lu, Q.W.1    Wu, X.Y.2    Morimoto, S.3
  • 36
    • 33646693410 scopus 로고    scopus 로고
    • Contemporary definitions and classification of the cardiomyopathies: An American Heart Association Scientific Statement from the Council on Clinical Cardiology, Heart Failure and Transplantation Committee; Quality of Care and Outcomes Research and Functional Genomics and Translational Biology Interdisciplinary Working Groups; And Council on Epidemiology and Prevention
    • 16567565 10.1161/CIRCULATIONAHA.106.174287
    • Maron BJ, Towbin JA, Thiene G, Antzelevitch C, Corrado D, Arnett D, Young JB (2006) Contemporary definitions and classification of the cardiomyopathies: an American Heart Association Scientific Statement from the Council on Clinical Cardiology, Heart Failure and Transplantation Committee; Quality of Care and Outcomes Research and Functional Genomics and Translational Biology Interdisciplinary Working Groups; and Council on Epidemiology and Prevention. Circulation 113(14):1807-1816
    • (2006) Circulation , vol.113 , Issue.14 , pp. 1807-1816
    • Maron, B.J.1    Towbin, J.A.2    Thiene, G.3    Antzelevitch, C.4    Corrado, D.5    Arnett, D.6    Young, J.B.7
  • 37
    • 85046111726 scopus 로고
    • Images in cardiovascular medicine. Extreme left ventricular hypertrophy
    • 1:STN:280:DyaK28%2FmvFaquw%3D%3D 7586380 10.1161/01.CIR.92.9.2748
    • Maron BJ, Gross BW, Stark SI (1995) Images in cardiovascular medicine. Extreme left ventricular hypertrophy. Circulation 92(9):2748
    • (1995) Circulation , vol.92 , Issue.9 , pp. 2748
    • Maron, B.J.1    Gross, B.W.2    Stark, S.I.3
  • 38
    • 79960564849 scopus 로고    scopus 로고
    • How do mutations in contractile proteins cause the primary familial cardiomyopathies?
    • 21424860 10.1007/s12265-011-9266-2
    • Marston SB (2011) How do mutations in contractile proteins cause the primary familial cardiomyopathies? J Cardiovasc Transl Res 4(3):245-255
    • (2011) J Cardiovasc Transl Res , vol.4 , Issue.3 , pp. 245-255
    • Marston, S.B.1
  • 39
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • 1:CAS:528:DyaK2cXhsFKqs7k%3D 1225772 8218897 10.1016/S0006-3495(93)81110- X
    • McKillop DF, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65(2):693-701
    • (1993) Biophys J , vol.65 , Issue.2 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 40
    • 84879390656 scopus 로고    scopus 로고
    • Familial dilated cardiomyopathy mutations uncouple troponin i phosphorylation from changes in myofibrillar Ca(2)(+) sensitivity
    • 1:CAS:528:DC%2BC3sXpvFakurk%3D 23539503 10.1093/cvr/cvt071
    • Memo M, Leung MC, Ward DG, dos Remedios C, Morimoto S, Zhang L, Messer AE (2013) Familial dilated cardiomyopathy mutations uncouple troponin I phosphorylation from changes in myofibrillar Ca(2)(+) sensitivity. Cardiovasc Res 99(1):65-73
    • (2013) Cardiovasc Res , vol.99 , Issue.1 , pp. 65-73
    • Memo, M.1    Leung, M.C.2    Ward, D.G.3    Dos Remedios, C.4    Morimoto, S.5    Zhang, L.6    Messer, A.E.7
  • 41
    • 23344452467 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype
    • 1:CAS:528:DC%2BD2MXmvFSnsLo%3D 15923195 10.1074/jbc.M412281200
    • Mirza M, Marston S, Willott R, Ashley C, Mogensen J, McKenna W, Watkins H (2005) Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype. J Biol Chem 280(31):28498-28506
    • (2005) J Biol Chem , vol.280 , Issue.31 , pp. 28498-28506
    • Mirza, M.1    Marston, S.2    Willott, R.3    Ashley, C.4    Mogensen, J.5    McKenna, W.6    Watkins, H.7
  • 42
    • 8144224216 scopus 로고    scopus 로고
    • Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy
    • 1:CAS:528:DC%2BD2cXpslGnsrs%3D 15542288 10.1016/j.jacc.2004.08.027
    • Mogensen J, Murphy RT, Shaw T, Bahl A, Redwood C, Watkins H, McKenna WJ (2004) Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J Am Coll Cardiol 44(10):2033-2040
    • (2004) J Am Coll Cardiol , vol.44 , Issue.10 , pp. 2033-2040
    • Mogensen, J.1    Murphy, R.T.2    Shaw, T.3    Bahl, A.4    Redwood, C.5    Watkins, H.6    McKenna, W.J.7
  • 43
    • 70349652425 scopus 로고    scopus 로고
    • The cardiac troponin C mutation Leu29Gln found in a patient with hypertrophic cardiomyopathy does not alter contractile parameters in skinned murine myocardium
    • 2758205 19506933 10.1007/s00395-009-0038-y
    • Neulen A, Stehle R, Pfitzer G (2009) The cardiac troponin C mutation Leu29Gln found in a patient with hypertrophic cardiomyopathy does not alter contractile parameters in skinned murine myocardium. Basic Res Cardiol 104(6):751-760
    • (2009) Basic Res Cardiol , vol.104 , Issue.6 , pp. 751-760
    • Neulen, A.1    Stehle, R.2    Pfitzer, G.3
  • 44
    • 0034759429 scopus 로고    scopus 로고
    • Disease-causing mutations in cardiac troponin T: Identification of a critical tropomyosin-binding region
    • 1:CAS:528:DC%2BD3MXotFais78%3D 1301748 11606294 10.1016/S0006-3495(01) 75924-3
    • Palm T, Graboski S, Hitchcock-DeGregori SE, Greenfield NJ (2001) Disease-causing mutations in cardiac troponin T: identification of a critical tropomyosin-binding region. Biophys J 81(5):2827-2837
    • (2001) Biophys J , vol.81 , Issue.5 , pp. 2827-2837
    • Palm, T.1    Graboski, S.2    Hitchcock-Degregori, S.E.3    Greenfield, N.J.4
  • 45
    • 84866431330 scopus 로고    scopus 로고
    • A mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillation
    • 1:CAS:528:DC%2BC38XhtlGgtr3E 3442518 22815480 10.1074/jbc.M112.377713
    • Parvatiyar MS, Landstrom AP, Figueiredo-Freitas C, Potter JD, Ackerman MJ, Pinto JR (2012) A mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillation. J Biol Chem 287(38):31845-31855
    • (2012) J Biol Chem , vol.287 , Issue.38 , pp. 31845-31855
    • Parvatiyar, M.S.1    Landstrom, A.P.2    Figueiredo-Freitas, C.3    Potter, J.D.4    Ackerman, M.J.5    Pinto, J.R.6
  • 46
    • 78651397869 scopus 로고    scopus 로고
    • (2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: A fast kinetic approach
    • 1:CAS:528:DC%2BC3MXjtFartg%3D%3D 3020707 21056975 10.1074/jbc.M110.168583
    • (2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: a fast kinetic approach. J Biol Chem 286(2):1005-1013
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1005-1013
    • Pinto, J.R.1    Reynaldo, D.P.2    Parvatiyar, M.S.3    Dweck, D.4    Liang, J.5    Jones, M.A.6    Potter, J.D.7
  • 47
    • 80053195075 scopus 로고    scopus 로고
    • Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy
    • 1:CAS:528:DC%2BC3MXht1ajtbrM 3190822 21832052 10.1074/jbc.M111.267211
    • Pinto JR, Siegfried JD, Parvatiyar MS, Li D, Norton N, Jones MA, Hershberger RE (2011b) Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy. J Biol Chem 286(39):34404-34412
    • (2011) J Biol Chem , vol.286 , Issue.39 , pp. 34404-34412
    • Pinto, J.R.1    Siegfried, J.D.2    Parvatiyar, M.S.3    Li, D.4    Norton, N.5    Jones, M.A.6    Hershberger, R.E.7
  • 48
    • 67650544956 scopus 로고    scopus 로고
    • A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD1MXotVKnt7k%3D 2707221 19439414 10.1074/jbc.M109.007021
    • Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD (2009) A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy. J Biol Chem 284(28):19090-19100
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 19090-19100
    • Pinto, J.R.1    Parvatiyar, M.S.2    Jones, M.A.3    Liang, J.4    Ackerman, M.J.5    Potter, J.D.6
  • 49
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • 1:CAS:528:DyaE2MXksleqsrs%3D 124731
    • Potter JD, Gergely J (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 250(12):4628-4633
    • (1975) J Biol Chem , vol.250 , Issue.12 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 50
    • 33847116576 scopus 로고    scopus 로고
    • Functional effects of the DCM mutant Gly159Asp troponin C in skinned muscle fibres
    • 1:CAS:528:DC%2BD2sXhvVeiurc%3D 17021793 10.1007/s00424-006-0161-7
    • Preston LC, Lipscomb S, Robinson P, Mogensen J, McKenna WJ, Watkins H, Redwood CS (2007a) Functional effects of the DCM mutant Gly159Asp troponin C in skinned muscle fibres. Pflugers Arch 453(6):771-776
    • (2007) Pflugers Arch , vol.453 , Issue.6 , pp. 771-776
    • Preston, L.C.1    Lipscomb, S.2    Robinson, P.3    Mogensen, J.4    McKenna, W.J.5    Watkins, H.6    Redwood, C.S.7
  • 51
    • 34250825315 scopus 로고    scopus 로고
    • DCM troponin C mutant Gly159Asp blunts the response to troponin phosphorylation
    • 1:CAS:528:DC%2BD2sXntFamtL4%3D 17577574 10.1016/j.bbrc.2007.05.221
    • Preston LC, Ashley CC, Redwood CS (2007b) DCM troponin C mutant Gly159Asp blunts the response to troponin phosphorylation. Biochem Biophys Res Commun 360(1):27-32
    • (2007) Biochem Biophys Res Commun , vol.360 , Issue.1 , pp. 27-32
    • Preston, L.C.1    Ashley, C.C.2    Redwood, C.S.3
  • 52
    • 0033214976 scopus 로고    scopus 로고
    • Properties of mutant contractile proteins that cause hypertrophic cardiomyopathy
    • 1:CAS:528:DyaK1MXmtVyisrs%3D 10615387 10.1016/S0008-6363(99)00213-8
    • Redwood CS, Moolman-Smook JC, Watkins H (1999) Properties of mutant contractile proteins that cause hypertrophic cardiomyopathy. Cardiovasc Res 44(1):20-36
    • (1999) Cardiovasc Res , vol.44 , Issue.1 , pp. 20-36
    • Redwood, C.S.1    Moolman-Smook, J.C.2    Watkins, H.3
  • 53
    • 0037174918 scopus 로고    scopus 로고
    • Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD38XnvFyntLc%3D 12186860 10.1074/jbc.M203446200
    • Robinson P, Mirza M, Knott A, Abdulrazzak H, Willott R, Marston S, Redwood C (2002) Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy. J Biol Chem 277(43):40710-40716
    • (2002) J Biol Chem , vol.277 , Issue.43 , pp. 40710-40716
    • Robinson, P.1    Mirza, M.2    Knott, A.3    Abdulrazzak, H.4    Willott, R.5    Marston, S.6    Redwood, C.7
  • 54
    • 37349042936 scopus 로고    scopus 로고
    • Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments
    • 1:CAS:528:DC%2BD2sXhtlOjsLzK 17932326 10.1161/CIRCRESAHA.107.156380
    • Robinson P, Griffiths PJ, Watkins H, Redwood CS (2007) Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments. Circ Res 101(12):1266-1273
    • (2007) Circ Res , vol.101 , Issue.12 , pp. 1266-1273
    • Robinson, P.1    Griffiths, P.J.2    Watkins, H.3    Redwood, C.S.4
  • 55
    • 28244469709 scopus 로고    scopus 로고
    • Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin i to C
    • 1:CAS:528:DC%2BD2MXhtlSqsbbF 16302972 10.1111/j.1742-4658.2005.05001.x
    • Schmidtmann A, Lindow C, Villard S, Heuser A, Mugge A, Gessner R, Jaquet K (2005) Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin I to C. FEBS J 272(23):6087-6097
    • (2005) FEBS J , vol.272 , Issue.23 , pp. 6087-6097
    • Schmidtmann, A.1    Lindow, C.2    Villard, S.3    Heuser, A.4    Mugge, A.5    Gessner, R.6    Jaquet, K.7
  • 56
    • 0028364242 scopus 로고
    • The effects of deletion of the amino-terminal helix on troponin C function and stability
    • 1:CAS:528:DyaK2cXkt12nt7s%3D 8144578
    • Smith L, Greenfield NJ, Hitchcock-DeGregori SE (1994) The effects of deletion of the amino-terminal helix on troponin C function and stability. J Biol Chem 269(13):9857-9863
    • (1994) J Biol Chem , vol.269 , Issue.13 , pp. 9857-9863
    • Smith, L.1    Greenfield, N.J.2    Hitchcock-Degregori, S.E.3
  • 57
    • 40849096222 scopus 로고    scopus 로고
    • The unique functions of cardiac troponin i in the control of cardiac muscle contraction and relaxation
    • 1:CAS:528:DC%2BD1cXjs12rsbw%3D 2365727 18162178 10.1016/j.bbrc.2007.12. 114
    • Solaro RJ, Rosevear P, Kobayashi T (2008) The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation. Biochem Biophys Res Commun 369(1):82-87
    • (2008) Biochem Biophys Res Commun , vol.369 , Issue.1 , pp. 82-87
    • Solaro, R.J.1    Rosevear, P.2    Kobayashi, T.3
  • 58
    • 58149305398 scopus 로고    scopus 로고
    • Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle
    • 1:CAS:528:DC%2BD1MXhtVKlsL8%3D 2670030 19015190 10.1113/jphysiol.2008. 164707
    • Sun YB, Lou F, Irving M (2009) Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle. J Physiol 587(Pt 1):155-163
    • (2009) J Physiol , vol.587 , Issue.PART 1 , pp. 155-163
    • Sun, Y.B.1    Lou, F.2    Irving, M.3
  • 59
    • 77953240679 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy-linked mutation D145E drastically alters calcium binding by the C-domain of cardiac troponin C
    • 1:CAS:528:DC%2BC3cXmt1Krtb8%3D 2883812 20459070 10.1021/bi100400h
    • Swindle N, Tikunova SB (2010) Hypertrophic cardiomyopathy-linked mutation D145E drastically alters calcium binding by the C-domain of cardiac troponin C. Biochemistry 49(23):4813-4820
    • (2010) Biochemistry , vol.49 , Issue.23 , pp. 4813-4820
    • Swindle, N.1    Tikunova, S.B.2
  • 60
    • 0016803961 scopus 로고
    • Calcium regulation of muscle contraction
    • 1:CAS:528:DyaE2MXkslKjsr0%3D 1334730 806311 10.1016/S0006-3495(75)85849-8
    • Szent-Gyorgyi AG (1975) Calcium regulation of muscle contraction. Biophys J 15(7):707-723
    • (1975) Biophys J , vol.15 , Issue.7 , pp. 707-723
    • Szent-Gyorgyi, A.G.1
  • 61
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca2 + -saturated form
    • 1:CAS:528:DC%2BD3sXltVelsbk%3D 12840750 10.1038/nature01780
    • Takeda S, Yamashita A, Maeda K, Maeda Y (2003) Structure of the core domain of human cardiac troponin in the Ca2 + -saturated form. Nature 424(6944):35-41
    • (2003) Nature , vol.424 , Issue.6944 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 62
    • 4143085980 scopus 로고    scopus 로고
    • Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C
    • 1:CAS:528:DC%2BD2cXmsl2iu70%3D 15205455 10.1074/jbc.M405413200
    • Tikunova SB, Davis JP (2004) Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C. J Biol Chem 279(34):35341-35352
    • (2004) J Biol Chem , vol.279 , Issue.34 , pp. 35341-35352
    • Tikunova, S.B.1    Davis, J.P.2
  • 63
    • 0031554903 scopus 로고    scopus 로고
    • Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2 + -dependent regulation of muscle contraction
    • 1:CAS:528:DyaK2sXlvFymt7o%3D 9299323 10.1006/jmbi.1997.1200
    • Tripet B, Van Eyk JE, Hodges RS (1997) Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2 + -dependent regulation of muscle contraction. J Mol Biol 271(5):728-750
    • (1997) J Mol Biol , vol.271 , Issue.5 , pp. 728-750
    • Tripet, B.1    Van Eyk, J.E.2    Hodges, R.S.3
  • 66
    • 0028844204 scopus 로고
    • Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy
    • 1:CAS:528:DyaK2MXpvVCksb4%3D 7493025 10.1038/ng1295-434
    • Watkins H, Conner D, Thierfelder L, Jarcho JA, MacRae C, McKenna WJ, Seidman CE (1995) Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy. Nat Genet 11(4):434-437
    • (1995) Nat Genet , vol.11 , Issue.4 , pp. 434-437
    • Watkins, H.1    Conner, D.2    Thierfelder, L.3    Jarcho, J.A.4    Macrae, C.5    McKenna, W.J.6    Seidman, C.E.7
  • 67
    • 0033605422 scopus 로고    scopus 로고
    • 2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy
    • 1:CAS:528:DyaK1MXitFyrt7c%3D 10085122 10.1074/jbc.274.13.8806
    • 2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy. J Biol Chem 274(13):8806-8812
    • (1999) J Biol Chem , vol.274 , Issue.13 , pp. 8806-8812
    • Yanaga, F.1    Morimoto, S.2    Ohtsuki, I.3
  • 68
    • 0020000247 scopus 로고
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils
    • 1:CAS:528:DyaL38XkvVOgsrc%3D 6211445
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J Biol Chem 257(13):7678-7683
    • (1982) J Biol Chem , vol.257 , Issue.13 , pp. 7678-7683
    • Zot, H.G.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.