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Volumn 293, Issue 4, 2007, Pages

Modulation of the rate of cardiac muscle contraction by troponin C constructs with various calcium binding affinities

Author keywords

Force; Thin filament

Indexed keywords

CALCIUM; MUTANT PROTEIN; PHOSPHATE; TROPONIN C;

EID: 35348992614     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00039.2007     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 4444343856 scopus 로고    scopus 로고
    • Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling
    • Adhikari BB, Regnier M, Rivera AJ, Kreutziger KL, Martyn DA. Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling. Biophys J 87: 1784-1794, 2004.
    • (2004) Biophys J , vol.87 , pp. 1784-1794
    • Adhikari, B.B.1    Regnier, M.2    Rivera, A.J.3    Kreutziger, K.L.4    Martyn, D.A.5
  • 2
    • 0029924005 scopus 로고    scopus 로고
    • Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium
    • Araujo A, Walker JW. Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium. Biophys J 70: 2316-2326, 1996.
    • (1996) Biophys J , vol.70 , pp. 2316-2326
    • Araujo, A.1    Walker, J.W.2
  • 3
    • 0023006793 scopus 로고
    • The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution
    • Brenner B. The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution. Basic Res Cardiol 81, Suppl 1: 1-15, 1986.
    • (1986) Basic Res Cardiol , vol.81 , Issue.SUPPL. 1 , pp. 1-15
    • Brenner, B.1
  • 4
    • 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 USA 85: 3265-3269, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 5
    • 0031038445 scopus 로고    scopus 로고
    • Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics
    • Campbell K. Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics. Biophys J 72: 254-262, 1997.
    • (1997) Biophys J , vol.72 , pp. 254-262
    • Campbell, K.1
  • 7
    • 0023839774 scopus 로고
    • The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate
    • Cooke R, Franks K, Luciani GB, Pate E. The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate. J Physiol 395: 77-97, 1988.
    • (1988) J Physiol , vol.395 , pp. 77-97
    • Cooke, R.1    Franks, K.2    Luciani, G.B.3    Pate, E.4
  • 8
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • Cooke R, Pate E. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys J 48: 789-798, 1985.
    • (1985) Biophys J , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 11
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves MA, Lehrer SS. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys J 67: 273-282, 1994.
    • (1994) Biophys J , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 12
    • 34147172853 scopus 로고    scopus 로고
    • Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle
    • Gillis TE, Martyn DA, Rivera AJ, Regnier M. Investigation of thin filament near-neighbour regulatory unit interactions during force development in skinned cardiac and skeletal muscle. J Physiol 580: 561-576, 2007.
    • (2007) J Physiol , vol.580 , pp. 561-576
    • Gillis, T.E.1    Martyn, D.A.2    Rivera, A.J.3    Regnier, M.4
  • 13
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M. Regulation of contraction in striated muscle. Physiol Rev 80: 853-924, 2000.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 14
    • 0031055303 scopus 로고    scopus 로고
    • Calcium regulation of skeletal muscle thin filament motility in vitro
    • Gordon AM, LaMadrid MA, Chen Y, Luo Z, Chase PB. Calcium regulation of skeletal muscle thin filament motility in vitro. Biophys J 72: 1295-1307, 1997.
    • (1997) Biophys J , vol.72 , pp. 1295-1307
    • Gordon, A.M.1    LaMadrid, M.A.2    Chen, Y.3    Luo, Z.4    Chase, P.B.5
  • 16
    • 3242733977 scopus 로고    scopus 로고
    • Inorganic phosphate speeds loaded shortening in rat skinned cardiac myocytes
    • Hinken AC, McDonald KS. Inorganic phosphate speeds loaded shortening in rat skinned cardiac myocytes. Am J Physiol Cell Physiol 287: C500-C507, 2004.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Hinken, A.C.1    McDonald, K.S.2
  • 17
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • Homsher E, Kim B, Bobkova A, Tobacman LS. Calcium regulation of thin filament movement in an in vitro motility assay. Biophys J 70: 1881-1892, 1996.
    • (1996) Biophys J , vol.70 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bobkova, A.3    Tobacman, L.S.4
  • 18
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF. Muscle structure and theories of contraction. Prog Biophys Biophys Chem 7: 255-318, 1957.
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 19
    • 33644997173 scopus 로고    scopus 로고
    • Mechanisms and use of calcium-sensitizing agents in the failing heart
    • Kass DA, Solaro RJ. Mechanisms and use of calcium-sensitizing agents in the failing heart. Circulation 113: 305-315, 2006.
    • (2006) Circulation , vol.113 , pp. 305-315
    • Kass, D.A.1    Solaro, R.J.2
  • 20
    • 0022560216 scopus 로고
    • The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle
    • Kentish JC. The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle. J Physiol 370: 585-604, 1986.
    • (1986) J Physiol , vol.370 , pp. 585-604
    • Kentish, J.C.1
  • 21
    • 4043077144 scopus 로고    scopus 로고
    • Inorganic phosphate affects the pCa-force relationship more than the pCa-ATPase by increasing the rate of dissociation of force generating cross-bridges in skinned fibers from both EDL and soleus muscles of the rat
    • Kerrick WG, Xu Y. Inorganic phosphate affects the pCa-force relationship more than the pCa-ATPase by increasing the rate of dissociation of force generating cross-bridges in skinned fibers from both EDL and soleus muscles of the rat. J Muscle Res Cell Motil 25: 107-117, 2004.
    • (2004) J Muscle Res Cell Motil , vol.25 , pp. 107-117
    • Kerrick, W.G.1    Xu, Y.2
  • 22
    • 0027298766 scopus 로고    scopus 로고
    • Kluwe L, Maeda K, Maeda Y. E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted. FEBS Lett 323: 83-88, 1993.
    • Kluwe L, Maeda K, Maeda Y. E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted. FEBS Lett 323: 83-88, 1993.
  • 23
    • 0037115194 scopus 로고    scopus 로고
    • Determinants of relaxation rate in rabbit skinned skeletal muscle fibres
    • Luo Y, Davis JP, Smillie LB, Rall JA. Determinants of relaxation rate in rabbit skinned skeletal muscle fibres. J Physiol 545: 887-901, 2002.
    • (2002) J Physiol , vol.545 , pp. 887-901
    • Luo, Y.1    Davis, J.P.2    Smillie, L.B.3    Rall, J.A.4
  • 24
    • 0026646783 scopus 로고
    • Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle
    • Metzger JM, Moss RL. Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys J 63: 460-468, 1992.
    • (1992) Biophys J , vol.63 , pp. 460-468
    • Metzger, J.M.1    Moss, R.L.2
  • 25
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady-state and transient kinetic study
    • Millar NC, Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady-state and transient kinetic study. J Biol Chem 265: 20234-20240, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 27
    • 0035827552 scopus 로고    scopus 로고
    • Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C mutant
    • Morris CA, Tobacman LS, Homsher E. Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C mutant. J Biol Chem 276: 20245-20251, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20245-20251
    • Morris, C.A.1    Tobacman, L.S.2    Homsher, E.3
  • 28
    • 0032572414 scopus 로고    scopus 로고
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae. Circ Res 83: 179-186, 1998.
    • (1998) Circ Res , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 32
    • 0242475138 scopus 로고    scopus 로고
    • Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils
    • Piroddi N, Tesi C, Pellegrino MA, Tobacman LS, Homsher E, Poggesi C. Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils. J Physiol 552: 917-931, 2003.
    • (2003) J Physiol , vol.552 , pp. 917-931
    • Piroddi, N.1    Tesi, C.2    Pellegrino, M.A.3    Tobacman, L.S.4    Homsher, E.5    Poggesi, C.6
  • 33
    • 17444431193 scopus 로고    scopus 로고
    • Sarcomeric determinants of striated muscle relaxation kinetics
    • Poggesi C, Tesi C, Stehle R. Sarcomeric determinants of striated muscle relaxation kinetics. Pflügers Arch 449: 505-517, 2005.
    • (2005) Pflügers Arch , vol.449 , pp. 505-517
    • Poggesi, C.1    Tesi, C.2    Stehle, R.3
  • 34
    • 0032410877 scopus 로고    scopus 로고
    • Role of calcium and crossbridges in modulation of rates of force development and relaxation in skinned muscle fibers
    • Rall JA, Wahr PA. Role of calcium and crossbridges in modulation of rates of force development and relaxation in skinned muscle fibers. Adv Exp Med Biol 453: 219-228, 1998.
    • (1998) Adv Exp Med Biol , vol.453 , pp. 219-228
    • Rall, J.A.1    Wahr, P.A.2
  • 35
    • 4444334713 scopus 로고    scopus 로고
    • Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle
    • Regnier M, Martin H, Barsotti RJ, Rivera AJ, Martyn DA, Clemmens E. Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys J 87: 1815-1824, 2004.
    • (2004) Biophys J , vol.87 , pp. 1815-1824
    • Regnier, M.1    Martin, H.2    Barsotti, R.J.3    Rivera, A.J.4    Martyn, D.A.5    Clemmens, E.6
  • 36
    • 0029657778 scopus 로고    scopus 로고
    • 2+ regulation of tension redevelopment rate in skinned skeletal muscle
    • 2+ regulation of tension redevelopment rate in skinned skeletal muscle. Biophys J 71: 2786-2794, 1996.
    • (1996) Biophys J , vol.71 , pp. 2786-2794
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 38
    • 0036278593 scopus 로고    scopus 로고
    • Isometric force kinetics upon rapid activation and relaxation of mouse, guinea pig and human heart muscle studied on the subcellular myofibrillar level
    • Stehle R, Kruger M, Scherer P, Brixius K, Schwinger RH, Pfitzer G. Isometric force kinetics upon rapid activation and relaxation of mouse, guinea pig and human heart muscle studied on the subcellular myofibrillar level. Basic Res Cardiol 97, Suppl 1: I127-I135, 2002.
    • (2002) Basic Res Cardiol , vol.97 , Issue.SUPPL. 1
    • Stehle, R.1    Kruger, M.2    Scherer, P.3    Brixius, K.4    Schwinger, R.H.5    Pfitzer, G.6
  • 40
    • 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. The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophys J 78: 3081-3092, 2000.
    • (2000) Biophys J , vol.78 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 41
    • 4143085980 scopus 로고    scopus 로고
    • Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C
    • Tikunova SB, Davis JP. Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C. J Biol Chem 279: 35341-35352, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 35341-35352
    • Tikunova, S.B.1    Davis, J.P.2
  • 42
    • 0037188409 scopus 로고    scopus 로고
    • 2+ binding and exchange with the N-domain of troponin C
    • 2+ binding and exchange with the N-domain of troponin C. Biochemistry 41: 6697-6705, 2002.
    • (2002) Biochemistry , vol.41 , pp. 6697-6705
    • Tikunova, S.B.1    Rall, J.A.2    Davis, J.P.3
  • 43
    • 0023664228 scopus 로고
    • Isolation and functional comparison of bovine cardiac troponin T isoforms
    • Tobacman LS, Lee R. Isolation and functional comparison of bovine cardiac troponin T isoforms. J Biol Chem 262: 4059-4064, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 4059-4064
    • Tobacman, L.S.1    Lee, R.2
  • 45
    • 0026609631 scopus 로고
    • 2+ on the kinetics of phosphate release in skeletal muscle
    • 2+ on the kinetics of phosphate release in skeletal muscle. J Biol Chem 267: 2459-2466, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 2459-2466
    • Walker, J.W.1    Lu, Z.2    Moss, R.L.3
  • 46
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff MR, McDonald KS, Moss RL. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ Res 76: 154-160, 1995.
    • (1995) Circ Res , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.