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Volumn 682, Issue , 2010, Pages 163-174

Extraction and replacement of the tropomyosin-troponin complex in isolated myofibrils

Author keywords

Cardiac; Myofibrils; Regulatory proteins; Skeletal; Tropomyosin; Troponin

Indexed keywords

CALCIUM ION; TROPOMYOSIN; TROPONIN; CALCIUM; TROPONIN TROPOMYOSIN COMPLEX; TROPONIN-TROPOMYOSIN COMPLEX;

EID: 78349272063     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-6366-6_9     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0021755958 scopus 로고
    • The thin filament of vertebrate skeletal muscle co-operatively activates as a unit
    • Brandt PW, Diamond MS, Schachat FH (1984) The thin filament of vertebrate skeletal muscle co-operatively activates as a unit. J Mol Biol 180:379-84
    • (1984) J Mol Biol , vol.180 , pp. 379-84
    • Brandt, P.W.1    Diamond, M.S.2    Schachat, F.H.3
  • 2
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ 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
  • 3
    • 0032706180 scopus 로고    scopus 로고
    • Thin filament activation probed by fluorescence of N-((2- (lodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazolelabeled troponin I incorporated into skinned fibers of rabbit psoas muscle
    • Brenner B, Kraft T, Yu L, Chalovich JM (1999) Thin filament activation probed by fluorescence of N-((2-(Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz- 2-oxa-1, 3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle. Biophys J 77:2677-2691 (Pubitemid 29519513)
    • (1999) Biophysical Journal , vol.77 , Issue.5 , pp. 2677-2691
    • Brenner, B.1    Kraft, T.2    Yu, L.C.3    Chalovich, J.M.4
  • 4
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in alpha-tropomyosin
    • Chang AN, Harada K, Ackerman MJ, Potter JD (2005) Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin. J Biol Chem 280:34343-3439
    • (2005) J Biol Chem , vol.280 , pp. 34343-3439
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 5
    • 23744475805 scopus 로고    scopus 로고
    • Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force
    • DOI 10.1113/jphysiol.2005.084194
    • Clemmens EW, Entezari M, Martyn DA, Regnier M (2005) Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force. J Physiol 566:737-46 (Pubitemid 41122657)
    • (2005) Journal of Physiology , vol.566 , Issue.3 , pp. 737-746
    • Clemmens, E.W.1    Entezari, M.2    Martyn, D.A.3    Regnier, M.4
  • 6
    • 0030948459 scopus 로고    scopus 로고
    • Active and passive forces of isolated myofibrils from cardiac and fast skeletal muscle of the frog
    • Colomo F, Piroddi N, Poggesi C, te Kronnie G, Tesi C (1997) Active and passive forces of isolated myofibrils from cardiac and fast skeletal muscle of the frog. J Physiol 500:535-548 (Pubitemid 27193085)
    • (1997) Journal of Physiology , vol.500 , Issue.2 , pp. 535-548
    • Colomo, F.1    Piroddi, N.2    Poggesi, C.3    Te Kronnie, G.4    Tesi, C.5
  • 7
    • 0015840125 scopus 로고
    • The subunits and biological activity of polymorphic forms of tropomyosin
    • Cummins P, Perry SV (1973) The subunits and biological activity of polymorphic forms of tropomyosin. Biochem J 133:765-777
    • (1973) Biochem J , vol.133 , pp. 765-777
    • Cummins, P.1    Perry, S.V.2
  • 9
    • 0029909623 scopus 로고    scopus 로고
    • Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle
    • Fujita H, Yasuda K, Niitsu S, Funatsu T, Ishiwata S (1996) Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle. Biophys J 71:2307-2318 (Pubitemid 26367697)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2307-2318
    • Fujita, H.1    Yasuda, K.2    Niitsu, S.3    Funatsu, T.4    Ishiwata, S.5
  • 10
    • 0036156643 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins
    • Fujita H, Sasaki D, Ishiwata S, Kawai M (2002) Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. Biophys J 82:915-28 (Pubitemid 34111232)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 915-928
    • Fujita, H.1    Sasaki, D.2    Ishiwata, S.3    Kawai, M.4
  • 11
    • 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 80:853-924 (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 12
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning P, O'Neill G, Hardeman E (2008) Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol Rev 88: 1-835
    • (2008) Physiol Rev , vol.88 , pp. 1-835
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 14
    • 0014466702 scopus 로고
    • The influence of native tropomyosin on the ATP threshold for turbidity development of actomyosin and myofibril suspensions
    • Kominz DR, Yoshioka K (1969) The influence of native tropomyosin on the ATP threshold for turbidity development of actomyosin and myofibril suspensions. Arch Biochem Biophys 129:609-614
    • (1969) Arch Biochem Biophys , vol.129 , pp. 609-614
    • Kominz, D.R.1    Yoshioka, K.2
  • 15
    • 48549085587 scopus 로고    scopus 로고
    • 2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle
    • 2+binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle. J Physiol 586:3683-700
    • (2008) J Physiol , vol.586 , pp. 3683-700
    • Kreutziger, K.L.1    Piroddi, N.2    Scellini, B.3    Tesi, C.4    Poggesi, C.5    Regnier, M.6
  • 16
    • 17844363735 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in alpha-tropomyosin
    • Kruger M, Zittrich S, Redwood C, Blaudeck N, James J, Robbins J, Pfitzer G, Stehle R (2005) Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin. J Physiol 564:347-357
    • (2005) J Physiol , vol.564 , pp. 347-357
    • Kruger, M.1    Zittrich, S.2    Redwood, C.3    Blaudeck, N.4    James, J.5    Robbins, J.6    Pfitzer, G.7    Stehle, R.8
  • 17
    • 0022491789 scopus 로고
    • Effects of partial extraction of troponin complex upon the tension-pCa relation in rabbit skeletal muscle. Further evidence that tension development involves cooperative effects within the thin filament
    • Moss RL, Allen JD, Greaser ML (1986) Effects of partial extraction of troponin complex upon the tension-pCa relation in rabbit skeletal muscle. Further evidence that tension development involves cooperative effects within the thin filament. J Gen Physiol 87:761-74 (Pubitemid 16071645)
    • (1986) Journal of General Physiology , vol.87 , Issue.5 , pp. 761-774
    • Moss, R.L.1    Allen, J.D.2    Greaser, M.L.3
  • 20
    • 45249099152 scopus 로고    scopus 로고
    • Defective regulation of contractile function in muscle fibres carrying an E41K β-tropomyosin mutation
    • DOI 10.1113/jphysiol.2008.153650
    • 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 (Pubitemid 351837290)
    • (2008) Journal of Physiology , vol.586 , Issue.12 , pp. 2993-3004
    • Ochala, J.1    Li, M.2    Ohlsson, M.3    Oldfors, A.4    Larsson, L.5
  • 21
    • 0003759921 scopus 로고
    • Extraction of proteins other than myosin from the isolated rabbit myofibril
    • Perry SV, Corsi A (1958) Extraction of proteins other than myosin from the isolated rabbit myofibril. Biochem J. 68:5-12
    • (1958) Biochem J , vol.68 , pp. 5-12
    • Perry, S.V.1    Corsi, A.2
  • 23
    • 0242475138 scopus 로고    scopus 로고
    • Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils
    • DOI 10.1113/jphysiol.2003.051615
    • Piroddi N, Tesi C, Pellegrino MA, Tobacman LS, Homsher E, Poggesi C (2003) Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils. J Physiol 552:917-931 (Pubitemid 37428430)
    • (2003) Journal of Physiology , vol.552 , Issue.3 , pp. 917-931
    • Piroddi, N.1    Tesi, C.2    Pellegrino, M.A.3    Tobacman, L.S.4    Homsher, E.5    Poggesi, C.6
  • 26
    • 0020352953 scopus 로고
    • Polymorphism of myofibrillar proteins of rabbit skeletal muscle fibres. An electrophoretic study of single fibres
    • Salviati G, Betto R, Danieli Betto D (1982) Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres. Biochem J. 207:261-272 (Pubitemid 13208161)
    • (1982) Biochemical Journal , vol.207 , Issue.2 , pp. 261-272
    • Salviati, G.1    Betto, R.2    Danieli Betto, D.3
  • 28
    • 67649878819 scopus 로고    scopus 로고
    • Mechanical and kinetic effects of shortened tropomyosin reconstituted into myofibrils
    • Siththanandan VB, Tobacman LS, Van Gorder N, Homsher E (2009) Mechanical and kinetic effects of shortened tropomyosin reconstituted into myofibrils. Pflugers Arch 458:761-776
    • (2009) Pflugers Arch , vol.458 , pp. 761-776
    • Siththanandan, V.B.1    Tobacman, L.S.2    Van Gorder, N.3    Homsher, E.4
  • 29
    • 0033136005 scopus 로고    scopus 로고
    • Modulation by substrate concentration of maximal shortening velocity and isometric force in single myofibrils from frog and rabbit fast skeletal muscle
    • DOI 10.1111/j.1469-7793.1999.0847u.x
    • Tesi C, Colomo F, Nencini S, Piroddi N, Poggesi C (1999) Modulation by substrate concentration of maximal shortening velocity and isometric force in single myofibrils from frog and rabbit fast skeletal muscle. J Physiol 516:847-853 (Pubitemid 29201907)
    • (1999) Journal of Physiology , vol.516 , Issue.3 , pp. 847-853
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 30
    • 0034084354 scopus 로고    scopus 로고
    • The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle
    • Tesi C, Colomo F, Nencini S, Piroddi N, Poggesi C (2000) The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophys J 78:3081-3092 (Pubitemid 30396937)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 31
    • 0037095908 scopus 로고    scopus 로고
    • Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles
    • DOI 10.1113/jphysiol.2001.013418
    • Tesi C, Colomo F, Piroddi N, Poggesi C (2002a) Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles. J Physiol. 541:187-99 (Pubitemid 35190193)
    • (2002) Journal of Physiology , vol.541 , Issue.1 , pp. 187-199
    • Tesi, C.1    Colomo, F.2    Piroddi, N.3    Poggesi, C.4
  • 32
    • 0036787723 scopus 로고    scopus 로고
    • Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle
    • Tesi C, Piroddi N, Colomo F, Poggesi C (2002b) Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle. Biophys J 83:2142-2151
    • (2002) Biophys J , vol.83 , pp. 2142-2151
    • Tesi, C.1    Piroddi, N.2    Colomo, F.3    Poggesi, C.4
  • 34
    • 68949123236 scopus 로고    scopus 로고
    • Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrils
    • Yang Z, Yamazaki M, Shen QW, Swartz DR (2009) Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrils. Biophys J 97:183-94
    • (2009) Biophys J , vol.97 , pp. 183-94
    • Yang, Z.1    Yamazaki, M.2    Shen, Q.W.3    Swartz, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.