메뉴 건너뛰기




Volumn 61, Issue 4, 2004, Pages 756-763

Troponin I phosphorylation plays an important role in the relaxant effect of β-adrenergic stimulation in mouse hearts

Author keywords

Adrenergic stimulation; Phospholamban; Relaxation; Troponin I

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; ISOPRENALINE; ISOPROTEIN; PHOSPHOLAMBAN; TROPONIN I;

EID: 1342324065     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2003.12.019     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo W.S., Grupp I.L., Harrer J., Ponniah S., Grupp G., Duffy J.J., et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ. Res. 75:1994;401-409.
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.S.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6
  • 3
    • 0034103666 scopus 로고    scopus 로고
    • Phosphorylation of phospholamban and troponin I in β-adrenergic- induced acceleration of cardiac relaxation
    • Li L., Desantiago J., Chu G., Kranias E.G., Bers D.M. Phosphorylation of phospholamban and troponin I in β-adrenergic-induced acceleration of cardiac relaxation. Am. J. Physiol. Heart Circ. Physiol. 278:2000;H769-H779.
    • (2000) Am. J. Physiol. Heart Circ. Physiol. , vol.278 , pp. 769-H779
    • Li, L.1    Desantiago, J.2    Chu, G.3    Kranias, E.G.4    Bers, D.M.5
  • 4
    • 0034509410 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractile function
    • Brittsan A.G., Kranias E.G. Phospholamban and cardiac contractile function. J. Mol. Cell. Cardiol. 32:2000;2131-2139.
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 2131-2139
    • Brittsan, A.G.1    Kranias, E.G.2
  • 5
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase a phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • Yamasaki R., Wu Y., McNabb M., Greaser M., Labeit S., Granzier H. Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ. Res. 90:2002;1181-1188.
    • (2002) Circ. Res. , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Labeit, S.5    Granzier, H.6
  • 7
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts
    • Garvey J.L., Kranias E.G., Solaro R.J. Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. Biochem. J. 249:1988;709-714.
    • (1988) Biochem. J. , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 8
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang R., Zhao J., Mandveno A., Potter J.D. Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ. Res. 76:1995;1028-1035.
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 9
    • 0033563035 scopus 로고    scopus 로고
    • Impaired cardiomyocyte relaxation and diastolic function in transgenic mice expressing slow skeletal troponin I in the heart
    • Fentzke R.C., Buck S.H., Patel J.R., Lin H., Wolska B.M., Stojanovic M.O., et al. Impaired cardiomyocyte relaxation and diastolic function in transgenic mice expressing slow skeletal troponin I in the heart. J. Physiol. 517:1999;143-157.
    • (1999) J. Physiol. , vol.517 , pp. 143-157
    • Fentzke, R.C.1    Buck, S.H.2    Patel, J.R.3    Lin, H.4    Wolska, B.M.5    Stojanovic, M.O.6
  • 10
    • 0025348807 scopus 로고
    • Adrenaline increases the rate of cross-bridge cycling in rat cardiac muscle
    • Saeki Y., Shiozawa K., Yanagisawa K., Shibata T. Adrenaline increases the rate of cross-bridge cycling in rat cardiac muscle. J. Mol. Cell. Cardiol. 22:1990;453-460.
    • (1990) J. Mol. Cell. Cardiol. , vol.22 , pp. 453-460
    • Saeki, Y.1    Shiozawa, K.2    Yanagisawa, K.3    Shibata, T.4
  • 11
    • 0028174245 scopus 로고
    • β-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats
    • Strang K.T., Sweitzer N.K., Greaser M.L., Moss R.L. β-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats. Circ. Res. 74:1994;542-549.
    • (1994) Circ. Res. , vol.74 , pp. 542-549
    • Strang, K.T.1    Sweitzer, N.K.2    Greaser, M.L.3    Moss, R.L.4
  • 12
    • 0031172311 scopus 로고    scopus 로고
    • Protein kinase a increases the tension cost and unloaded shortening velocity in skinned rat cardiac muscle
    • Saeki Y., Kobayashi T., Minamisawa S., Sugi H. Protein kinase A increases the tension cost and unloaded shortening velocity in skinned rat cardiac muscle. J. Mol. Cell. Cardiol. 29:1997;1655-1663.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 1655-1663
    • Saeki, Y.1    Kobayashi, T.2    Minamisawa, S.3    Sugi, H.4
  • 13
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase a accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish J.C., McCloskey D.T., Layland J., Palmer S., Leiden J.M., Martin A.F., et al. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ. Res. 88:2001;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
  • 14
    • 0036687680 scopus 로고    scopus 로고
    • Troponin I phosphorylation enhances crossbridge kinetics during beta-adrenergic stimulation in rat cardiac tissue
    • Turnbull L., Hoh J.F., Ludowyke R.I., Rossmanith G.H. Troponin I phosphorylation enhances crossbridge kinetics during beta-adrenergic stimulation in rat cardiac tissue. J. Physiol. 542:2002;911-920.
    • (2002) J. Physiol. , vol.542 , pp. 911-920
    • Turnbull, L.1    Hoh, J.F.2    Ludowyke, R.I.3    Rossmanith, G.H.4
  • 15
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross-bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • Weisberg A., Winegrad S. Alteration of myosin cross-bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc. Natl. Acad. Sci. U. S. A. 93:1996;8999-9003.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 16
    • 0034900675 scopus 로고    scopus 로고
    • Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions
    • Levine R., Weisberg A., Kulikovskaya I., McClellan G., Winegrad S. Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions. Biophys. J. 81:2001;1070-1082.
    • (2001) Biophys. J. , vol.81 , pp. 1070-1082
    • Levine, R.1    Weisberg, A.2    Kulikovskaya, I.3    McClellan, G.4    Winegrad, S.5
  • 17
    • 0033612182 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C
    • Winegrad S. Cardiac myosin binding protein C. Circ. Res. 84:1999;1117-1126.
    • (1999) Circ. Res. , vol.84 , pp. 1117-1126
    • Winegrad, S.1
  • 18
    • 0034907680 scopus 로고    scopus 로고
    • Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C
    • McClellan G., Kulikovskaya I., Winegrad S. Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C. Biophys. J. 81:2001;1083-1092.
    • (2001) Biophys. J. , vol.81 , pp. 1083-1092
    • McClellan, G.1    Kulikovskaya, I.2    Winegrad, S.3
  • 19
    • 0037013173 scopus 로고    scopus 로고
    • Expression of slow skeletal troponin I in hearts of phospholamban knockout mice alters the relaxant effect of β-adrenergic stimulation
    • Wolska B.M., Arteaga G.M., Pena J.R., Nowak G., Phillips R.M., Sahai S., et al. Expression of slow skeletal troponin I in hearts of phospholamban knockout mice alters the relaxant effect of β-adrenergic stimulation. Circ. Res. 90:2002;882-888.
    • (2002) Circ. Res. , vol.90 , pp. 882-888
    • Wolska, B.M.1    Arteaga, G.M.2    Pena, J.R.3    Nowak, G.4    Phillips, R.M.5    Sahai, S.6
  • 20
    • 0036793158 scopus 로고    scopus 로고
    • Myofilament-based relaxant effect of isoprenaline revealed during work-loop contractions in rat cardiac trabeculae
    • Layland J., Kentish J.C. Myofilament-based relaxant effect of isoprenaline revealed during work-loop contractions in rat cardiac trabeculae. J. Physiol. 544:2002;171-182.
    • (2002) J. Physiol. , vol.544 , pp. 171-182
    • Layland, J.1    Kentish, J.C.2
  • 21
    • 0033667759 scopus 로고    scopus 로고
    • Altered hemodynamics in transgenic mice harboring mutant tropomyosin linked to hypertrophic cardiomyopathy
    • Evans C.C., Pena J.R., Phillips R.M., Muthuchamy M., Wieczorek D.F., Solaro R.J., et al. Altered hemodynamics in transgenic mice harboring mutant tropomyosin linked to hypertrophic cardiomyopathy. Am. J. Physiol. 279:2000;H2414-H2423.
    • (2000) Am. J. Physiol. , vol.279 , pp. 2414-H2423
    • Evans, C.C.1    Pena, J.R.2    Phillips, R.M.3    Muthuchamy, M.4    Wieczorek, D.F.5    Solaro, R.J.6
  • 22
    • 0030951068 scopus 로고    scopus 로고
    • Measurement of intraventricular pressure and cardiac performance in the intact closed-chest anesthetized mouse
    • Lorenz J.N., Robbins J. Measurement of intraventricular pressure and cardiac performance in the intact closed-chest anesthetized mouse. Am. J. Physiol. 41:1997;H1137-H1146.
    • (1997) Am. J. Physiol. , vol.41 , pp. 1137-H1146
    • Lorenz, J.N.1    Robbins, J.2
  • 23
    • 0025052108 scopus 로고
    • Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts
    • Karczewski P., Bartel S., Krause E.G. Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts. Biochem. J. 266:1990;115-122.
    • (1990) Biochem. J. , vol.266 , pp. 115-122
    • Karczewski, P.1    Bartel, S.2    Krause, E.G.3
  • 24
    • 10544246896 scopus 로고    scopus 로고
    • Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts
    • Chu G., Luo W., Slack J.P., Tilgmann C., Sweet W.E., Spindler M., et al. Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts. Circ. Res. 79:1996;1064-1076.
    • (1996) Circ. Res. , vol.79 , pp. 1064-1076
    • Chu, G.1    Luo, W.2    Slack, J.P.3    Tilgmann, C.4    Sweet, W.E.5    Spindler, M.6
  • 26
    • 0029154871 scopus 로고
    • In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency
    • Hoit B.D., Houry S.F., Kranias E.G., Ball N., Walsh R.A. In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency. Circ. Res. 77:1995;632-637.
    • (1995) Circ. Res. , vol.77 , pp. 632-637
    • Hoit, B.D.1    Houry, S.F.2    Kranias, E.G.3    Ball, N.4    Walsh, R.A.5
  • 27
    • 33750702216 scopus 로고    scopus 로고
    • Regulatory effects of phospholamban on cardiac function in intact mice
    • Lorenz J.N., Kranias E.G. Regulatory effects of phospholamban on cardiac function in intact mice. Am. J. Physiol. 273:1997;H2826-H2831.
    • (1997) Am. J. Physiol. , vol.273 , pp. 2826-H2831
    • Lorenz, J.N.1    Kranias, E.G.2
  • 28
    • 0037023633 scopus 로고    scopus 로고
    • Phosphorylation of troponin I controls cardiac twitch dynamics: Evidence from phosphorylation site mutants expressed on a troponin I-null background in mice
    • Pi Y., Kemnitz K.R., Zhang D., Kranias E.G., Walker J.W. Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice. Circ. Res. 90:2002;649-656.
    • (2002) Circ. Res. , vol.90 , pp. 649-656
    • Pi, Y.1    Kemnitz, K.R.2    Zhang, D.3    Kranias, E.G.4    Walker, J.W.5
  • 29
    • 0029884605 scopus 로고    scopus 로고
    • Temperature and relative contributions of Ca transport systems in cardiac myocyte relaxation
    • Puglisi J.L., Bassani R., Bassani J.W.M., Amin J.N., Bers D.M. Temperature and relative contributions of Ca transport systems in cardiac myocyte relaxation. Am. J. Physiol. 39:1996;H1772-H1778.
    • (1996) Am. J. Physiol. , vol.39 , pp. 1772-H1778
    • Puglisi, J.L.1    Bassani, R.2    Bassani, J.W.M.3    Amin, J.N.4    Bers, D.M.5
  • 30
    • 0036088280 scopus 로고    scopus 로고
    • Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat
    • Janssen P.M., Stull L.B., Marban E. Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat. Am. J. Physiol. 282:2002;H499-H507.
    • (2002) Am. J. Physiol. , vol.282 , pp. 499-H507
    • Janssen, P.M.1    Stull, L.B.2    Marban, E.3
  • 31
    • 17944378311 scopus 로고    scopus 로고
    • Expression of slow skeletal troponin I in adult transgenic mouse heart muscle reduces the force decline observed during acidic conditions
    • Wolska B.M., Vijayan K., Arteaga G.M., Konhilas J.P., Phillips R.M., Kim R., et al. Expression of slow skeletal troponin I in adult transgenic mouse heart muscle reduces the force decline observed during acidic conditions. J. Physiol. 536:2001;863-870.
    • (2001) J. Physiol. , vol.536 , pp. 863-870
    • Wolska, B.M.1    Vijayan, K.2    Arteaga, G.M.3    Konhilas, J.P.4    Phillips, R.M.5    Kim, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.