메뉴 건너뛰기




Volumn 68, Issue 1, 2011, Pages 18-31

Force relaxation and thin filament protein phosphorylation during acute myocardial ischemia

Author keywords

Heart; Ischemia; PKA; Relaxation; Troponin

Indexed keywords

BETA ADRENERGIC RECEPTOR; CALCIUM ION; CONNECTIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; MYOSIN BINDING PROTEIN C; SERINE; TROPONIN I;

EID: 78650219273     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20491     Document Type: Article
Times cited : (6)

References (66)
  • 1
    • 0028004261 scopus 로고
    • Kinetics of tension development in skinned cardiac myocytes measured by photorelease of Ca2+
    • Araujo A, Walker JW. 1994. Kinetics of tension development in skinned cardiac myocytes measured by photorelease of Ca2+. Am J Physiol 267: H1643-H1653.
    • (1994) Am J Physiol , vol.267
    • Araujo, A.1    Walker, J.W.2
  • 2
    • 0025923244 scopus 로고
    • Ca2+ and activation mechanisms in skeletal muscle
    • Ashley CC, Mulligan IP, Lea TJ. 1991. Ca2+ and activation mechanisms in skeletal muscle. Q Rev Biophys 24: 1-73.
    • (1991) Q Rev Biophys , vol.24 , pp. 1-73
    • Ashley, C.C.1    Mulligan, I.P.2    Lea, T.J.3
  • 3
    • 48549105342 scopus 로고    scopus 로고
    • The familial hypertrophic cardiomyopathy-associated myosin mutation R403Q accelerates tension generation and relaxation of human cardiac myofibrils
    • Belus A, Piroddi N, Scellini B, Tesi C, Amati GD, Girolami F, Yacoub M, Cecchi F, Olivotto I, Poggesi C. 2008. The familial hypertrophic cardiomyopathy-associated myosin mutation R403Q accelerates tension generation and relaxation of human cardiac myofibrils. J Physiol 586: 3639-3644.
    • (2008) J Physiol , vol.586 , pp. 3639-3644
    • Belus, A.1    Piroddi, N.2    Scellini, B.3    Tesi, C.4    Amati, G.D.5    Girolami, F.6    Yacoub, M.7    Cecchi, F.8    Olivotto, I.9    Poggesi, C.10
  • 4
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers DM. 2002. Cardiac excitation-contraction coupling. Nature 415: 198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 5
    • 43549098268 scopus 로고    scopus 로고
    • Calcium cycling and signaling in cardiac myocytes
    • Bers DM. 2008. Calcium cycling and signaling in cardiac myocytes. Annu Rev Physiol 70: 23-49.
    • (2008) Annu Rev Physiol , vol.70 , pp. 23-49
    • Bers, D.M.1
  • 6
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation
    • Biesiadecki BJ, Kobayashi T, Walker JS, John Solaro R, de Tombe PP. 2007. The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation. Circ Res 100: 1486-1493.
    • (2007) Circ Res , vol.100 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    Walker, J.S.3    John Solaro, R.4    de Tombe, P.P.5
  • 8
    • 0032923593 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of myocardial stunning
    • Bolli R, Marban E. 1999. Molecular and cellular mechanisms of myocardial stunning. Physiol Rev 79: 609-634.
    • (1999) Physiol Rev , vol.79 , pp. 609-634
    • Bolli, R.1    Marban, E.2
  • 11
    • 33645456962 scopus 로고    scopus 로고
    • Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin
    • Chen FC, Ogut O. 2006. Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin. Am J Physiol Cell Physiol 290: C719-C727.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Chen, F.C.1    Ogut, O.2
  • 12
    • 69549116251 scopus 로고    scopus 로고
    • Reduced force production during low blood flow to the heart correlates with altered troponin I phosphorylation
    • Christopher B, Pizarro GO, Nicholson B, Yuen S, Hoit BD, Ogut O. 2009. Reduced force production during low blood flow to the heart correlates with altered troponin I phosphorylation. J Muscle Res Cell Motil 30: 111-123.
    • (2009) J Muscle Res Cell Motil , vol.30 , pp. 111-123
    • Christopher, B.1    Pizarro, G.O.2    Nicholson, B.3    Yuen, S.4    Hoit, B.D.5    Ogut, O.6
  • 17
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner
    • Fukuda N, Wu Y, Nair P, Granzier HL. 2005. Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner. J Gen Physiol 125: 257-271.
    • (2005) J Gen Physiol , vol.125 , pp. 257-271
    • Fukuda, N.1    Wu, Y.2    Nair, P.3    Granzier, H.L.4
  • 18
    • 0029028751 scopus 로고
    • Relationship between intracellular calcium and contractile force in stunned myocardium. Direct evidence for decreased myofilament Ca2+ responsiveness and altered diastolic function in intact ventricular muscle
    • Gao WD, Atar D, Backx PH, Marban E. 1995. Relationship between intracellular calcium and contractile force in stunned myocardium. Direct evidence for decreased myofilament Ca2+ responsiveness and altered diastolic function in intact ventricular muscle. Circ Res 76: 1036-1048.
    • (1995) Circ Res , vol.76 , pp. 1036-1048
    • Gao, W.D.1    Atar, D.2    Backx, P.H.3    Marban, E.4
  • 19
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts
    • Garvey JL, Kranias EG, Solaro RJ. 1988. Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. Biochem J 249: 709-714.
    • (1988) Biochem J , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 21
    • 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.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 22
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier HL, Irving TC. 1995. Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments. Biophys J 68: 1027-1044.
    • (1995) Biophys J , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 24
    • 77949675336 scopus 로고    scopus 로고
    • Regulation of fibre contraction in a rat model of myocardial ischemia
    • Han YS, Ogut O. 2010. Regulation of fibre contraction in a rat model of myocardial ischemia. PLoS One 5: e9528.
    • (2010) PLoS One , vol.5
    • Han, Y.S.1    Ogut, O.2
  • 26
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd MG, Dantzig JA, Trentham DR, Goldman YE. 1985. Phosphate release and force generation in skeletal muscle fibers. Science 228: 1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 27
    • 0034104565 scopus 로고    scopus 로고
    • Effects of controlled-release metoprolol on total mortality, hospitalizations, and well-being in patients with heart failure: the Metoprolol CR/XL Randomized Intervention Trial in congestive heart failure (MERIT-HF)
    • MERIT-HF Study Group
    • Hjalmarson A, Goldstein S, Fagerberg B, Wedel H, Waagstein F, Kjekshus J, Wikstrand J, El Allaf D, Vitovec J, Aldershvile J, et al. 2000. Effects of controlled-release metoprolol on total mortality, hospitalizations, and well-being in patients with heart failure: the Metoprolol CR/XL Randomized Intervention Trial in congestive heart failure (MERIT-HF). MERIT-HF Study Group. JAMA 283: 1295-1302.
    • (2000) JAMA , vol.283 , pp. 1295-1302
    • Hjalmarson, A.1    Goldstein, S.2    Fagerberg, B.3    Wedel, H.4    Waagstein, F.5    Kjekshus, J.6    Wikstrand, J.7    El Allaf, D.8    Vitovec, J.9    Aldershvile, J.10
  • 28
    • 0027306182 scopus 로고
    • Altered calcium sensitivity of isometric tension in myocyte-sized preparations of porcine postischemic stunned myocardium
    • Hofmann PA, Miller WP, Moss RL. 1993. Altered calcium sensitivity of isometric tension in myocyte-sized preparations of porcine postischemic stunned myocardium. Circ Res 72: 50-56.
    • (1993) Circ Res , vol.72 , pp. 50-56
    • Hofmann, P.A.1    Miller, W.P.2    Moss, R.L.3
  • 29
    • 0029154871 scopus 로고
    • In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency
    • Hoit BD, Khoury SF, Kranias EG, Ball N, Walsh RA. 1995. In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency. Circ Res 77: 632-637.
    • (1995) Circ Res , vol.77 , pp. 632-637
    • Hoit, B.D.1    Khoury, S.F.2    Kranias, E.G.3    Ball, N.4    Walsh, R.A.5
  • 30
    • 33750828132 scopus 로고    scopus 로고
    • Stability of high-energy phosphates in right ventricle: myocardial energetics during right coronary hypotension
    • Itoya M, Mallet RT, Gao ZP, Williams AGJ, Downey HF. 1996. Stability of high-energy phosphates in right ventricle: myocardial energetics during right coronary hypotension. Am J Physiol 271: H320-H328.
    • (1996) Am J Physiol , vol.271
    • Itoya, M.1    Mallet, R.T.2    Gao, Z.P.3    Williams, A.G.J.4    Downey, H.F.5
  • 31
    • 0030935930 scopus 로고    scopus 로고
    • Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae
    • Johns EC, Simnett SJ, Mulligan IP, Ashley CC. 1997. Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae. Pflugers Arch 433: 842-844.
    • (1997) Pflugers Arch , vol.433 , pp. 842-844
    • Johns, E.C.1    Simnett, S.J.2    Mulligan, I.P.3    Ashley, C.C.4
  • 32
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish JC, McCloskey DT, Layland J, Palmer S, Leiden JM, Martin AF, Solaro RJ. 2001. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ Res 88: 1059-1065.
    • (2001) Circ Res , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 33
    • 48549085587 scopus 로고    scopus 로고
    • Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle
    • Kreutziger KL, Piroddi N, Scellini B, Tesi C, Poggesi C, Regnier M. 2008. Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle. J Physiol 586: 3683-3700.
    • (2008) J Physiol , vol.586 , pp. 3683-3700
    • Kreutziger, K.L.1    Piroddi, N.2    Scellini, B.3    Tesi, C.4    Poggesi, C.5    Regnier, M.6
  • 35
    • 0025230883 scopus 로고
    • Excitation-contraction coupling in postischemic myocardium. Does failure of activator Ca2+ transients underlie stunning?
    • Kusuoka H, Koretsune Y, Chacko VP, Weisfeldt ML, Marban E. 1990. Excitation-contraction coupling in postischemic myocardium. Does failure of activator Ca2+ transients underlie stunning? Circ Res 66: 1268-1276.
    • (1990) Circ Res , vol.66 , pp. 1268-1276
    • Kusuoka, H.1    Koretsune, Y.2    Chacko, V.P.3    Weisfeldt, M.L.4    Marban, E.5
  • 36
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • Layland J, Solaro RJ, Shah AM. 2005. Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc Res 66: 12-21.
    • (2005) Cardiovasc Res , vol.66 , pp. 12-21
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 37
    • 0034103666 scopus 로고    scopus 로고
    • Phosphorylation of phospholamban and troponin I in beta-adrenergic-induced acceleration of cardiac relaxation
    • Li L, Desantiago J, Chu G, Kranias EG, Bers DM. 2000. Phosphorylation of phospholamban and troponin I in beta-adrenergic-induced acceleration of cardiac relaxation. Am J Physiol Heart Circ Physiol 278: H769-H779.
    • (2000) Am J Physiol Heart Circ Physiol , vol.278
    • Li, L.1    Desantiago, J.2    Chu, G.3    Kranias, E.G.4    Bers, D.M.5
  • 38
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo W, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG. 1994. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res 75: 401-409.
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 39
    • 0037115194 scopus 로고    scopus 로고
    • Determinants of relaxation rate in rabbit skinned skeletal muscle fibres
    • Luo Y, Davis JP, Smillie LB, Rall JA. 2002. Determinants of relaxation rate in rabbit skinned skeletal muscle fibres. J Physiol 545: 887-901.
    • (2002) J Physiol , vol.545 , pp. 887-901
    • Luo, Y.1    Davis, J.P.2    Smillie, L.B.3    Rall, J.A.4
  • 40
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • MacLennan DH, Kranias EG. 2003. Phospholamban: a crucial regulator of cardiac contractility. Nat Rev Mol Cell Biol 4: 566-577.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 41
    • 0028294216 scopus 로고
    • Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP
    • Martin H, Barsotti RJ. 1994. Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP. Biophys J 66: 1115-1128.
    • (1994) Biophys J , vol.66 , pp. 1115-1128
    • Martin, H.1    Barsotti, R.J.2
  • 42
    • 0032006553 scopus 로고    scopus 로고
    • Incorporation of the troponin regulatory complex of post-ischemic stunned porcine myocardium reduces myofilament calcium sensitivity in rabbit psoas skeletal muscle fibers
    • McDonald KS, Moss RL, Miller WP. 1998. Incorporation of the troponin regulatory complex of post-ischemic stunned porcine myocardium reduces myofilament calcium sensitivity in rabbit psoas skeletal muscle fibers. J Mol Cell Cardiol 30: 285-296.
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 285-296
    • McDonald, K.S.1    Moss, R.L.2    Miller, W.P.3
  • 43
    • 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. 1990. 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) J Biol Chem , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 46
    • 0032572414 scopus 로고    scopus 로고
    • Roles of Ca2+ and crossbridge kinetics in determining the maximum rates of Ca2+ activation and relaxation in rat and guinea pig skinned trabeculae
    • Palmer S, Kentish JC. 1998. Roles of Ca2+ and crossbridge kinetics in determining the maximum rates of Ca2+ activation and relaxation in rat and guinea pig skinned trabeculae. Circ Res 83: 179-186.
    • (1998) Circ Res , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 47
    • 0031972659 scopus 로고    scopus 로고
    • Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke
    • Pate E, Franks-Skiba K, Cooke R. 1998. Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke. Biophys J 74: 369-380.
    • (1998) Biophys J , vol.74 , pp. 369-380
    • Pate, E.1    Franks-Skiba, K.2    Cooke, R.3
  • 48
    • 0020069347 scopus 로고
    • The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin
    • Robertson SP, Johnson JD, Holroyde MJ, Kranias EG, Potter JD, Solaro RJ. 1982. The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin. J Biol Chem 257: 260-263.
    • (1982) J Biol Chem , vol.257 , pp. 260-263
    • Robertson, S.P.1    Johnson, J.D.2    Holroyde, M.J.3    Kranias, E.G.4    Potter, J.D.5    Solaro, R.J.6
  • 49
    • 0037050009 scopus 로고    scopus 로고
    • Seven-transmembrane-spanning receptors and heart function
    • Rockman HA, Koch WJ, Lefkowitz RJ. 2002. Seven-transmembrane-spanning receptors and heart function. Nature 415: 206-212.
    • (2002) Nature , vol.415 , pp. 206-212
    • Rockman, H.A.1    Koch, W.J.2    Lefkowitz, R.J.3
  • 51
    • 33750856767 scopus 로고    scopus 로고
    • Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo 2
    • Simnett SJ, Johns EC, Lipscomb S, Mulligan IP, Ashley CC. 1998. Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo 2. Am J Physiol 275: H951-H960.
    • (1998) Am J Physiol , vol.275
    • Simnett, S.J.1    Johns, E.C.2    Lipscomb, S.3    Mulligan, I.P.4    Ashley, C.C.5
  • 52
    • 0017143827 scopus 로고
    • Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart
    • Solaro RJ, Moir AJ, Perry SV. 1976. Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart. Nature 262: 615-617.
    • (1976) Nature , vol.262 , pp. 615-617
    • Solaro, R.J.1    Moir, A.J.2    Perry, S.V.3
  • 53
    • 34548356872 scopus 로고    scopus 로고
    • Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphorylation
    • Stelzer JE, Patel JR, Walker JW, Moss RL. 2007. Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphorylation. Circ Res 101: 503-511.
    • (2007) Circ Res , vol.101 , pp. 503-511
    • Stelzer, J.E.1    Patel, J.R.2    Walker, J.W.3    Moss, R.L.4
  • 54
    • 0028855384 scopus 로고
    • Detection of giant myofibrillar proteins connectin and nebulin by electrophoresis in 2% polyacrylamide slab gels strengthened with agarose
    • Tatsumi R, Hattori A. 1995. Detection of giant myofibrillar proteins connectin and nebulin by electrophoresis in 2% polyacrylamide slab gels strengthened with agarose. Anal Biochem 224: 28-31.
    • (1995) Anal Biochem , vol.224 , pp. 28-31
    • Tatsumi, R.1    Hattori, A.2
  • 55
    • 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. 2002. 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
  • 56
    • 0028898137 scopus 로고
    • Papillary muscle perfusion pattern. A hypothesis for ischemic papillary muscle dysfunction
    • Voci P, Bilotta F, Caretta Q, Mercanti C, Marino B. 1995. Papillary muscle perfusion pattern. A hypothesis for ischemic papillary muscle dysfunction. Circulation 91: 1714-1718.
    • (1995) Circulation , vol.91 , pp. 1714-1718
    • Voci, P.1    Bilotta, F.2    Caretta, Q.3    Mercanti, C.4    Marino, B.5
  • 57
    • 0036088350 scopus 로고    scopus 로고
    • The off rate of Ca(2+) from troponin C is regulated by force-generating cross bridges in skeletal muscle
    • Wang Y, Kerrick WG. 2002. The off rate of Ca(2+) from troponin C is regulated by force-generating cross bridges in skeletal muscle. J Appl Physiol 92: 2409-2418.
    • (2002) J Appl Physiol , vol.92 , pp. 2409-2418
    • Wang, Y.1    Kerrick, W.G.2
  • 58
    • 0038219368 scopus 로고    scopus 로고
    • Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins
    • Warren CM, Krzesinski PR, Greaser ML. 2003. Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins. Electrophoresis 24: 1695-1702.
    • (2003) Electrophoresis , vol.24 , pp. 1695-1702
    • Warren, C.M.1    Krzesinski, P.R.2    Greaser, M.L.3
  • 60
    • 0030015928 scopus 로고    scopus 로고
    • Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies: role of altered beta-adrenergically mediated protein phosphorylation
    • Wolff MR, Buck SH, Stoker SW, Greaser ML, Mentzer RM. 1996. Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies: role of altered beta-adrenergically mediated protein phosphorylation. J Clin Invest 98: 167-176.
    • (1996) J Clin Invest , vol.98 , pp. 167-176
    • Wolff, M.R.1    Buck, S.H.2    Stoker, S.W.3    Greaser, M.L.4    Mentzer, R.M.5
  • 61
    • 51749122229 scopus 로고    scopus 로고
    • Phosphate metabolite concentrations and ATP hydrolysis potential in normal and ischaemic hearts
    • Wu F, Zhang EY, Zhang J, Bache RJ, Beard DA. 2008. Phosphate metabolite concentrations and ATP hydrolysis potential in normal and ischaemic hearts. J Physiol 586: 4193-4208.
    • (2008) J Physiol , vol.586 , pp. 4193-4208
    • Wu, F.1    Zhang, E.Y.2    Zhang, J.3    Bache, R.J.4    Beard, D.A.5
  • 62
    • 34547951704 scopus 로고    scopus 로고
    • Cardiac transgenic and gene transfer strategies converge to support an important role for troponin I in regulating relaxation in cardiac myocytes
    • Yasuda S, Coutu P, Sadayappan S, Robbins J, Metzger JM. 2007. Cardiac transgenic and gene transfer strategies converge to support an important role for troponin I in regulating relaxation in cardiac myocytes. Circ Res 101: 377-386.
    • (2007) Circ Res , vol.101 , pp. 377-386
    • Yasuda, S.1    Coutu, P.2    Sadayappan, S.3    Robbins, J.4    Metzger, J.M.5
  • 63
    • 33750113347 scopus 로고    scopus 로고
    • Myosin binding protein C is differentially phosphorylated upon myocardial stunning in canine and rat hearts-evidence for novel phosphorylation sites
    • Yuan C, Guo Y, Ravi R, Przyklenk K, Shilkofski N, Diez R, Cole RN, Murphy AM. 2006. Myosin binding protein C is differentially phosphorylated upon myocardial stunning in canine and rat hearts-evidence for novel phosphorylation sites. Proteomics 6: 4176-4186.
    • (2006) Proteomics , vol.6 , pp. 4176-4186
    • Yuan, C.1    Guo, Y.2    Ravi, R.3    Przyklenk, K.4    Shilkofski, N.5    Diez, R.6    Cole, R.N.7    Murphy, A.M.8
  • 64
    • 0033514391 scopus 로고    scopus 로고
    • Protein kinase A (PKA)-dependent troponin-I phosphorylation and PKA regulatory subunits are decreased in human dilated cardiomyopathy
    • Zakhary DR, Moravec CS, Stewart RW, Bond M. 1999. Protein kinase A (PKA)-dependent troponin-I phosphorylation and PKA regulatory subunits are decreased in human dilated cardiomyopathy. Circulation 99: 505-510.
    • (1999) Circulation , vol.99 , pp. 505-510
    • Zakhary, D.R.1    Moravec, C.S.2    Stewart, R.W.3    Bond, M.4
  • 65
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang R, Zhao J, Mandveno A, Potter JD. 1995a. Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ Res 76: 1028-1035.
    • (1995) Circ Res , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 66
    • 0029559638 scopus 로고
    • Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C
    • Zhang R, Zhao J, Potter JD. 1995b. Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C. J Biol Chem 270: 30773-30780.
    • (1995) J Biol Chem , vol.270 , pp. 30773-30780
    • Zhang, R.1    Zhao, J.2    Potter, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.