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Volumn 51, Issue 3, 2011, Pages 409-418

Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin t mutations

Author keywords

Cardiac hypertrophy; Confocal microscopy; Mesoscopic measurements; Polarization of fluorescence; Troponin T

Indexed keywords

MYOSIN;

EID: 79960926449     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2011.06.001     Document Type: Article
Times cited : (4)

References (33)
  • 1
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves M.A., Holmes K.C. The molecular mechanism of muscle contraction. Adv Protein Chem 2005, 71(24):161-193.
    • (2005) Adv Protein Chem , vol.71 , Issue.24 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 2
    • 0032486127 scopus 로고    scopus 로고
    • Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibres
    • Sabido-David C., Hopkins S.C., Saraswat L.D., Lowey S., Goldman Y.E., Irving M. Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibres. J Mol Biol 1998, 279(2):387-402.
    • (1998) J Mol Biol , vol.279 , Issue.2 , pp. 387-402
    • Sabido-David, C.1    Hopkins, S.C.2    Saraswat, L.D.3    Lowey, S.4    Goldman, Y.E.5    Irving, M.6
  • 3
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • Hopkins S.C., Sabido-David C., Corrie J.E., Irving M., Goldman Y.E. Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys J 1998, 74(6):3093-3110.
    • (1998) Biophys J , vol.74 , Issue.6 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.3    Irving, M.4    Goldman, Y.E.5
  • 4
    • 18444403111 scopus 로고    scopus 로고
    • Orientation changes of the myosin light chain domain during filament sliding in active and rigor muscle
    • Hopkins S.C., Sabido-David C., van der Heide U.A., Ferguson R.E., Brandmeier B.D., Dale R.E., et al. Orientation changes of the myosin light chain domain during filament sliding in active and rigor muscle. J Mol Biol 2002, 318(5):1275-1291.
    • (2002) J Mol Biol , vol.318 , Issue.5 , pp. 1275-1291
    • Hopkins, S.C.1    Sabido-David, C.2    van der Heide, U.A.3    Ferguson, R.E.4    Brandmeier, B.D.5    Dale, R.E.6
  • 5
    • 0035830841 scopus 로고    scopus 로고
    • Abnormal contractile function in transgenic mice expressing a familial hypertrophic cardiomyopathy-linked troponin T (I79N) mutation
    • Epub 2000
    • Miller T., Szczesna D., Housmans P.R., Zhao J., de Freitas F., Gomes A.V., et al. Abnormal contractile function in transgenic mice expressing a familial hypertrophic cardiomyopathy-linked troponin T (I79N) mutation. J Biol Chem Nov 1 2001, 276(6):3743-3755. Epub 2000.
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 3743-3755
    • Miller, T.1    Szczesna, D.2    Housmans, P.R.3    Zhao, J.4    de Freitas, F.5    Gomes, A.V.6
  • 6
    • 27744558988 scopus 로고    scopus 로고
    • F110I and R278C troponin T mutations that cause familial hypertrophic cardiomyopathy affect muscle contraction in transgenic mice and reconstituted human cardiac fibers
    • Hernandez O.M., Szczesna-Cordary D., Knollmann B.C., Miller T., Bell M., Zhao J., et al. F110I and R278C troponin T mutations that cause familial hypertrophic cardiomyopathy affect muscle contraction in transgenic mice and reconstituted human cardiac fibers. J Biol Chem 2005, 280(44):37183-37194.
    • (2005) J Biol Chem , vol.280 , Issue.44 , pp. 37183-37194
    • Hernandez, O.M.1    Szczesna-Cordary, D.2    Knollmann, B.C.3    Miller, T.4    Bell, M.5    Zhao, J.6
  • 7
    • 3042718653 scopus 로고    scopus 로고
    • Molecular and cellular aspects of troponin cardiomyopathies
    • Gomes A.V., Potter J.D. Molecular and cellular aspects of troponin cardiomyopathies. Ann N Y Acad Sci 2004, 1015:214-224.
    • (2004) Ann N Y Acad Sci , vol.1015 , pp. 214-224
    • Gomes, A.V.1    Potter, J.D.2
  • 8
    • 34250029399 scopus 로고    scopus 로고
    • Tropomyosin in the groove? Molecular insights into an inherited myopathy
    • Chase P.B. Tropomyosin in the groove? Molecular insights into an inherited myopathy. J Physiol 2007, 581(Pt 3):889.
    • (2007) J Physiol , vol.581 , Issue.PART 3 , pp. 889
    • Chase, P.B.1
  • 9
    • 66149090351 scopus 로고    scopus 로고
    • Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state
    • Mathur M.C., Kobayashi T., Chalovich J.M. Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state. Biophys J 2009, 96(6):2237-2244.
    • (2009) Biophys J , vol.96 , Issue.6 , pp. 2237-2244
    • Mathur, M.C.1    Kobayashi, T.2    Chalovich, J.M.3
  • 10
    • 77951621530 scopus 로고    scopus 로고
    • Mutations in Troponin that cause HCM, DCM AND RCM: what can we learn about thin filament function?
    • Willott R.H., Gomes A.V., Chang A.N., Parvatiyar M.S., Pinto J.R., Potter J.D. Mutations in Troponin that cause HCM, DCM AND RCM: what can we learn about thin filament function?. J Mol Cell Cardiol 2010, 48(5):882-892.
    • (2010) J Mol Cell Cardiol , vol.48 , Issue.5 , pp. 882-892
    • Willott, R.H.1    Gomes, A.V.2    Chang, A.N.3    Parvatiyar, M.S.4    Pinto, J.R.5    Potter, J.D.6
  • 11
    • 70149123629 scopus 로고    scopus 로고
    • Functional effects of a restrictive-cardiomyopathy-linked cardiac troponin I mutation (R145W) in transgenic mice
    • Wen Y., Xu Y., Wang Y., Pinto J.R., Potter J.D., Kerrick W.G. Functional effects of a restrictive-cardiomyopathy-linked cardiac troponin I mutation (R145W) in transgenic mice. J Mol Biol 2009, 392(5):1158-1167.
    • (2009) J Mol Biol , vol.392 , Issue.5 , pp. 1158-1167
    • Wen, Y.1    Xu, Y.2    Wang, Y.3    Pinto, J.R.4    Potter, J.D.5    Kerrick, W.G.6
  • 12
    • 0036679175 scopus 로고    scopus 로고
    • Concentration fluctuations in a mesoscopic oscillating chemical reaction system
    • Epub 2002
    • Qian H., Saffarian S., Elson E.L. Concentration fluctuations in a mesoscopic oscillating chemical reaction system. Proc Natl Acad Sci USA Jul 17 2002, 99(16):10376-10381. Epub 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.16 , pp. 10376-10381
    • Qian, H.1    Saffarian, S.2    Elson, E.L.3
  • 13
    • 0015257784 scopus 로고
    • Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state
    • Dos Remedios C.G., Millikan R.G., Morales M.F. Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state. J Gen Physiol 1972, 59:103-120.
    • (1972) J Gen Physiol , vol.59 , pp. 103-120
    • Dos Remedios, C.G.1    Millikan, R.G.2    Morales, M.F.3
  • 15
    • 0015948545 scopus 로고
    • Use of fluorescence polarization to observe changes in attitude of S1 moieties in muscle fibers
    • Nihei T., Mendelson R.A., Botts J. Use of fluorescence polarization to observe changes in attitude of S1 moieties in muscle fibers. Biophys J 1974, 14:236-242.
    • (1974) Biophys J , vol.14 , pp. 236-242
    • Nihei, T.1    Mendelson, R.A.2    Botts, J.3
  • 16
    • 0016756968 scopus 로고
    • Polarization from a helix of fluorophores and its relation to that obtained from muscle
    • Tregear R.T., Mendelson R.A. Polarization from a helix of fluorophores and its relation to that obtained from muscle. Biophys J 1975, 15:455-467.
    • (1975) Biophys J , vol.15 , pp. 455-467
    • Tregear, R.T.1    Mendelson, R.A.2
  • 17
    • 0021367313 scopus 로고
    • Calculation of the polarized fluorescence from a labeled muscle fiber
    • Morales M.F. Calculation of the polarized fluorescence from a labeled muscle fiber. Proc Natl Acad Sci USA 1984, 81:145-149.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 145-149
    • Morales, M.F.1
  • 18
    • 0028240680 scopus 로고
    • Following the rotational trajectory of the principal hydrodynamic frame of a protein using multiple probes
    • Burghardt T.P., Ajtai K. Following the rotational trajectory of the principal hydrodynamic frame of a protein using multiple probes. Biochemistry 1994, 33:5376-5381.
    • (1994) Biochemistry , vol.33 , pp. 5376-5381
    • Burghardt, T.P.1    Ajtai, K.2
  • 19
    • 77951622927 scopus 로고    scopus 로고
    • Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart
    • Muthu P., Mettikolla P., Calander N., Luchowski R., Gryczynski I., Gryczynski I., et al. Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart. J Mol Cell Cardiol 2009, 48(6):1264-1271.
    • (2009) J Mol Cell Cardiol , vol.48 , Issue.6 , pp. 1264-1271
    • Muthu, P.1    Mettikolla, P.2    Calander, N.3    Luchowski, R.4    Gryczynski, I.5    Gryczynski, I.6
  • 20
    • 79951829380 scopus 로고    scopus 로고
    • Evidence for pre-and post-power stroke of cross-bridges of contracting skeletal myofibrils
    • Midde K., Luchowski R., Das H.K., Fedorick J., Dumka V., Gryczynski I., et al. Evidence for pre-and post-power stroke of cross-bridges of contracting skeletal myofibrils. Biophys J 2011, 100(4):1024-1033.
    • (2011) Biophys J , vol.100 , Issue.4 , pp. 1024-1033
    • Midde, K.1    Luchowski, R.2    Das, H.K.3    Fedorick, J.4    Dumka, V.5    Gryczynski, I.6
  • 21
    • 0029863187 scopus 로고    scopus 로고
    • Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle
    • Ling N., Shrimpton C., Sleep J., Kendrick-Jones J., Irving M. Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle. Biophys J 1996, 70:1836-1846.
    • (1996) Biophys J , vol.70 , pp. 1836-1846
    • Ling, N.1    Shrimpton, C.2    Sleep, J.3    Kendrick-Jones, J.4    Irving, M.5
  • 22
    • 0028208001 scopus 로고
    • Correlation of ActoS1, myofibrillar, and muscle fiber ATPases
    • Herrmann C., Lionne C., Travers F., Barman T. Correlation of ActoS1, myofibrillar, and muscle fiber ATPases. Biochemistry 1994, 33(14):4148-4154.
    • (1994) Biochemistry , vol.33 , Issue.14 , pp. 4148-4154
    • Herrmann, C.1    Lionne, C.2    Travers, F.3    Barman, T.4
  • 23
    • 0032976537 scopus 로고    scopus 로고
    • Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers
    • Tsaturyan A.K., Bershitsky S.Y., Burns R., Ferenczi M.A. Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers. Biophys J 1999, 77(1):354-372.
    • (1999) Biophys J , vol.77 , Issue.1 , pp. 354-372
    • Tsaturyan, A.K.1    Bershitsky, S.Y.2    Burns, R.3    Ferenczi, M.A.4
  • 24
    • 34247648050 scopus 로고    scopus 로고
    • Rotation of Actin monomers during isometric contraction of skeletal muscle
    • Borejdo J., Muthu P., Talent J., Akopova I., Burghardt T.P. Rotation of Actin monomers during isometric contraction of skeletal muscle. J Biomed Optics 2007, 12(1):014013.
    • (2007) J Biomed Optics , vol.12 , Issue.1 , pp. 014013
    • Borejdo, J.1    Muthu, P.2    Talent, J.3    Akopova, I.4    Burghardt, T.P.5
  • 25
    • 57449095883 scopus 로고    scopus 로고
    • Myofilament Ca2+ sensitization causes susceptibility to cardiac arrhythmia in mice
    • Baudenbacher F., Schober T., Pinto J.R., Sidorov V.Y., Hilliard F., Solaro R.J., et al. Myofilament Ca2+ sensitization causes susceptibility to cardiac arrhythmia in mice. J Clin Invest 2008, 118(12):3893-3903.
    • (2008) J Clin Invest , vol.118 , Issue.12 , pp. 3893-3903
    • Baudenbacher, F.1    Schober, T.2    Pinto, J.R.3    Sidorov, V.Y.4    Hilliard, F.5    Solaro, R.J.6
  • 26
    • 0027716901 scopus 로고
    • The binding of fluorescent phallotoxins to actin in myofibrils
    • Szczesna D., Lehrer S.S. The binding of fluorescent phallotoxins to actin in myofibrils. J Muscle Res Cell Motil 1993, 14(6):594-597.
    • (1993) J Muscle Res Cell Motil , vol.14 , Issue.6 , pp. 594-597
    • Szczesna, D.1    Lehrer, S.S.2
  • 27
    • 0028811462 scopus 로고
    • Phalloidin unzips nebulin from thin filaments in skeletal myofibrils
    • Ao X., Lehrer S.S. Phalloidin unzips nebulin from thin filaments in skeletal myofibrils. J Cell Sci 1995, 108(Pt 11):3397-3403.
    • (1995) J Cell Sci , vol.108 , Issue.PART 11 , pp. 3397-3403
    • Ao, X.1    Lehrer, S.S.2
  • 28
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • Magde D., Elson E.L., Webb W.W. Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 1974, 13(1):29-61.
    • (1974) Biopolymers , vol.13 , Issue.1 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 30
    • 77953910875 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules
    • Borejdo J., Szczesna-Cordary D., Muthu P., Calander N. Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules. Biochemistry 2010, 49:5269-5277.
    • (2010) Biochemistry , vol.49 , pp. 5269-5277
    • Borejdo, J.1    Szczesna-Cordary, D.2    Muthu, P.3    Calander, N.4
  • 31
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • Coureux P.D., Sweeney H.L., Houdusse A. Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J 2004, 23(23):4527-4537.
    • (2004) EMBO J , vol.23 , Issue.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 32
    • 0016379116 scopus 로고
    • Fluorescence correlation spectroscopy: conceptual basis and theory
    • Elson E.L., Magde D. Fluorescence correlation spectroscopy: conceptual basis and theory. Biopolymers 1974, 13:1-28.
    • (1974) Biopolymers , vol.13 , pp. 1-28
    • Elson, E.L.1    Magde, D.2
  • 33
    • 0023645610 scopus 로고
    • Effect of rigor and cycling cross-bridges on the structure of troponin C and on the Ca2+ affinity of the Ca2+-specific regulatory sites in skinned rabbit psoas fibers
    • Guth K., Potter J.D. Effect of rigor and cycling cross-bridges on the structure of troponin C and on the Ca2+ affinity of the Ca2+-specific regulatory sites in skinned rabbit psoas fibers. J Biol Chem 1987, 262(28):13627-13635.
    • (1987) J Biol Chem , vol.262 , Issue.28 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2


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