메뉴 건너뛰기




Volumn 57, Issue 2, 2003, Pages 505-514

The effect of myosin light chain 2 dephosphorylation on Ca2+-sensitivity of force is enhanced in failing human hearts

Author keywords

Cardiomyopathy; Contractile apparatus; Contractile function; Myocytes; Signal transduction

Indexed keywords

CALCIUM ION; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 2; PHOSPHOPROTEIN PHOSPHATASE 1; UNCLASSIFIED DRUG;

EID: 12244249137     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(02)00662-4     Document Type: Article
Times cited : (122)

References (36)
  • 1
    • 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
  • 2
    • 0024399052 scopus 로고
    • Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites
    • Noland T.A., Raynor R.L., Kuo J.F. Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J Biol Chem. 264:1989;20778-20785.
    • (1989) J Biol Chem , vol.264 , pp. 20778-20785
    • Noland, T.A.1    Raynor, R.L.2    Kuo, J.F.3
  • 3
    • 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
  • 4
    • 0024359705 scopus 로고
    • Myosin P-light chain isoenzymes in the human heart: Evidence for diphosphorylation of the atrial P-light chain isoform
    • Morano I., Wankerl M., Böhm M., Erdman E., Rüegg J.C. Myosin P-light chain isoenzymes in the human heart: evidence for diphosphorylation of the atrial P-light chain isoform. Basic Res Cardiol. 84:1989;298-305.
    • (1989) Basic Res Cardiol , vol.84 , pp. 298-305
    • Morano, I.1    Wankerl, M.2    Böhm, M.3    Erdman, E.4    Rüegg, J.C.5
  • 5
    • 0016743032 scopus 로고
    • Phosphorylation of the light-chain components of myosin from cardiac and red skeletal muscles
    • Frearson N., Perry S.V. Phosphorylation of the light-chain components of myosin from cardiac and red skeletal muscles. Biochem J. 151:1975;99-107.
    • (1975) Biochem J , vol.151 , pp. 99-107
    • Frearson, N.1    Perry, S.V.2
  • 6
    • 0027248968 scopus 로고
    • Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2
    • Venema R.C., Raynor R.L., Noland T.A., Kuo J.F. Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2. Biochem J. 294:1993;401-406.
    • (1993) Biochem J , vol.294 , pp. 401-406
    • Venema, R.C.1    Raynor, R.L.2    Noland, T.A.3    Kuo, J.F.4
  • 7
    • 0026632809 scopus 로고
    • Effects of different expression and posttranslational modifications of myosin light chains on contractility of skinned human cardiac fibers
    • Morano I. Effects of different expression and posttranslational modifications of myosin light chains on contractility of skinned human cardiac fibers. Basic Res Cardiol. 87:1992;129-141.
    • (1992) Basic Res Cardiol , vol.87 , pp. 129-141
    • Morano, I.1
  • 8
    • 0032917447 scopus 로고    scopus 로고
    • 2+-sensitive isoforms in the failing human heart
    • 2+-sensitive isoforms in the failing human heart. Circulation. 99:1999;384-391.
    • (1999) Circulation , vol.99 , pp. 384-391
    • Bowling, N.1    Walsh, R.A.2    Song, G.3
  • 10
    • 0030888810 scopus 로고    scopus 로고
    • Increased expression of cardiac phosphatases in patients with end-stage heart failure
    • Neumann J., Eschenhagen T., Jones L.R., et al. Increased expression of cardiac phosphatases in patients with end-stage heart failure. J Mol Cell Cardiol. 29:1997;265-272.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 265-272
    • Neumann, J.1    Eschenhagen, T.2    Jones, L.R.3
  • 11
    • 0035806920 scopus 로고    scopus 로고
    • Effects of calcium, inorganic phosphate and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts
    • Van der Velden J., Klein L.J., Zaremba R., et al. Effects of calcium, inorganic phosphate and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts. Circulation. 104:2001;1140-1146.
    • (2001) Circulation , vol.104 , pp. 1140-1146
    • Van der Velden, J.1    Klein, L.J.2    Zaremba, R.3
  • 12
    • 12244268941 scopus 로고    scopus 로고
    • 2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins
    • in press
    • 2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins. Cardiovasc Res (in press).
    • Cardiovasc Res
    • Van Der Velden, J.1    Papp, Z.2    Zaremba, R.3
  • 13
    • 0023037423 scopus 로고
    • Further studies on the effects of myosin P-light chain phosphorylation on contractile properties of skinned cardiac fibers
    • Morano I., Arndt H., Bächle-Stolz C., Rüegg J.C. Further studies on the effects of myosin P-light chain phosphorylation on contractile properties of skinned cardiac fibers. Basic Res Cardiol. 81:1986;611-619.
    • (1986) Basic Res Cardiol , vol.81 , pp. 611-619
    • Morano, I.1    Arndt, H.2    Bächle-Stolz, C.3    Rüegg, J.C.4
  • 15
    • 12244304470 scopus 로고    scopus 로고
    • 2+-sensitivity of tension in rat myocardium
    • 2+-sensitivity of tension in rat myocardium. Biophys J. 76:1999;A311.
    • (1999) Biophys J , vol.76 , pp. 311
    • Hollander, M.S.1    Moss, R.L.2
  • 16
    • 12244278593 scopus 로고    scopus 로고
    • Modulation of mechanical properties due to regulatory light chain phosphorylation in myocardium
    • Huiting-Hollander M.S., Chen J., Chu P., Moss R.L. Modulation of mechanical properties due to regulatory light chain phosphorylation in myocardium. Biophys J. 80:2001;91a.
    • (2001) Biophys J , vol.80
    • Huiting-Hollander, M.S.1    Chen, J.2    Chu, P.3    Moss, R.L.4
  • 17
    • 17744416349 scopus 로고    scopus 로고
    • Changes in essential myosin light chain isoform expression provide a molecular basis for isometric tension regulation in the failing human heart
    • Morano I., Hädicke K., Haase H., Böhm M., Erdmann E., Schaub M.C. Changes in essential myosin light chain isoform expression provide a molecular basis for isometric tension regulation in the failing human heart. J Mol Cell Cardiol. 29:1997;1177-1187.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1177-1187
    • Morano, I.1    Hädicke, K.2    Haase, H.3    Böhm, M.4    Erdmann, E.5    Schaub, M.C.6
  • 18
    • 0030015928 scopus 로고    scopus 로고
    • Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies
    • Wolff M.R., Buck S.H., Stoker S.W., Greaser M.L., Mentzer R.M. Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies. J Clin Invest. 98:1996;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
  • 19
    • 0033034564 scopus 로고    scopus 로고
    • Isometric tension development and its calcium sensitivity in skinned myocyte-sized preparations from different regions of the human heart
    • Van der Velden J., Klein L.J., van der Bijl M., et al. Isometric tension development and its calcium sensitivity in skinned myocyte-sized preparations from different regions of the human heart. Cardiovasc Res. 42:1999;706-719.
    • (1999) Cardiovasc Res , vol.42 , pp. 706-719
    • Van der Velden, J.1    Klein, L.J.2    Van der Bijl, M.3
  • 20
    • 17444437951 scopus 로고    scopus 로고
    • Force production in mechanically isolated cardiac myocytes from human ventricular muscle tissue
    • Van der Velden J., Klein L.J., van der Bijl M., et al. Force production in mechanically isolated cardiac myocytes from human ventricular muscle tissue. Cardiovasc Res. 38:1998;414-423.
    • (1998) Cardiovasc Res , vol.38 , pp. 414-423
    • Van der Velden, J.1    Klein, L.J.2    Van der Bijl, M.3
  • 21
    • 0019769492 scopus 로고
    • Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle
    • Fabiato A. Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle. J Gen Physiol. 78:1981;457-497.
    • (1981) J Gen Physiol , vol.78 , pp. 457-497
    • Fabiato, A.1
  • 22
    • 0033962648 scopus 로고    scopus 로고
    • Calpain-1 induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart
    • Papp Z., van der Velden J., Stienen G.J.M. Calpain-1 induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart. Cardiovasc Res. 45:2000;981-993.
    • (2000) Cardiovasc Res , vol.45 , pp. 981-993
    • Papp, Z.1    Van der Velden, J.2    Stienen, G.J.M.3
  • 23
    • 0034027364 scopus 로고    scopus 로고
    • Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes
    • Van der Velden J., de Jong J.W., Owen V.J., Burton P.B.J., Stienen G.J.M. Effect of protein kinase A on calcium sensitivity of force and its sarcomere length dependence in human cardiomyocytes. Cardiovasc Res. 46:2000;487-495.
    • (2000) Cardiovasc Res , vol.46 , pp. 487-495
    • Van der Velden, J.1    De Jong, J.W.2    Owen, V.J.3    Burton, P.B.J.4    Stienen, G.J.M.5
  • 24
    • 0025606303 scopus 로고
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle. J Gen Physiol. 96:1990;1221-1245.
    • (1990) J Gen Physiol , vol.96 , pp. 1221-1245
    • Sweitzer, N.K.1    Moss, R.L.2
  • 25
    • 0030246902 scopus 로고    scopus 로고
    • 2+-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats
    • 2+-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats. Cardiovasc Res. 32:1996;580-586.
    • (1996) Cardiovasc Res , vol.32 , pp. 580-586
    • Vannier, C.1    Chevassus, H.2    Vassort, G.3
  • 26
    • 0035002723 scopus 로고    scopus 로고
    • Cooperative mechanisms in the activation dependence of the rate of force redevelopment in rabbit skinned skeletal muscle fibers
    • Fitzsimons D.P., Patel J.R., Campbell K.S., Moss R.L. Cooperative mechanisms in the activation dependence of the rate of force redevelopment in rabbit skinned skeletal muscle fibers. J Gen Physiol. 117:2001;133-148.
    • (2001) J Gen Physiol , vol.117 , pp. 133-148
    • Fitzsimons, D.P.1    Patel, J.R.2    Campbell, K.S.3    Moss, R.L.4
  • 27
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff M.R., McDonald K.S., Moss R.L. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ Res. 76:1995;154-160.
    • (1995) Circ Res , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.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. 83:1998;179-186.
    • (1998) Circ Res , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 29
    • 0029011407 scopus 로고
    • Rate of active tension development from rigor in skinned atrial and ventricular cardiac fibers from swine following photolytic release of ATP from caged ATP
    • Morano I., Österman A., Arner A. Rate of active tension development from rigor in skinned atrial and ventricular cardiac fibers from swine following photolytic release of ATP from caged ATP. Acta Physiol Scand. 154:1995;343-353.
    • (1995) Acta Physiol Scand , vol.154 , pp. 343-353
    • Morano, I.1    Österman, A.2    Arner, A.3
  • 30
    • 0023968180 scopus 로고
    • Pressure overload changes cardiac skinned-fiber mechanics in rats, not in guinea-pigs
    • Ventura-Clapier R., Mekhfi H., Oliviero P., Swynghedauw B. Pressure overload changes cardiac skinned-fiber mechanics in rats, not in guinea-pigs. Am J Physiol. 254:1988;H517-H524.
    • (1988) Am J Physiol , vol.254 , pp. 517-H524
    • Ventura-Clapier, R.1    Mekhfi, H.2    Oliviero, P.3    Swynghedauw, B.4
  • 31
    • 0023849569 scopus 로고    scopus 로고
    • Skinned fibers of human atrium and ventricle: Myosin isoenzymes and contractility
    • Morano I., Arndt H., Gärtner C., Rüegg J.C. Skinned fibers of human atrium and ventricle: myosin isoenzymes and contractility. Circ Res. 62:1998;632-639.
    • (1998) Circ Res , vol.62 , pp. 632-639
    • Morano, I.1    Arndt, H.2    Gärtner, C.3    Rüegg, J.C.4
  • 32
    • 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. 85:1988;3265-3269.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0025727168 scopus 로고
    • Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II
    • Schlender K.K., Bean L.J. Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II. J Biol Chem. 266:1991;2811-2817.
    • (1991) J Biol Chem , vol.266 , pp. 2811-2817
    • Schlender, K.K.1    Bean, L.J.2
  • 36
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments
    • Levine R.J., Kensler R.W., Yang Z., Stull J.T., Sweeney H.L. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys J. 71:1996;898-907.
    • (1996) Biophys J , vol.71 , pp. 898-907
    • Levine, R.J.1    Kensler, R.W.2    Yang, Z.3    Stull, J.T.4    Sweeney, H.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.