메뉴 건너뛰기




Volumn 60, Issue 3, 2003, Pages 580-588

Myosin light chain isoforms modify force-generating ability of cardiac myosin by changing the kinetics of actin-myosin interaction

Author keywords

Actin translocating velocity; ATPase activity; Cardiac myosin; In vitro motility assay; Laser trap; Myosin light chain; Unitary displacement; Unitary force

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; CARDIAC MYOSIN; ISOPROTEIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN;

EID: 0345059065     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2003.09.011     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0023120631 scopus 로고
    • Myosin heavy chain messenger RNA and protein isoform transitions during cardiac hypertrophy. Interaction between hemodynamic and thyroid hormone-induced signals
    • Izumo S., Lompre A.M., Matsuoka R.et al. Myosin heavy chain messenger RNA and protein isoform transitions during cardiac hypertrophy. Interaction between hemodynamic and thyroid hormone-induced signals. J. Clin. Invest. 79:1987;970-977.
    • (1987) J. Clin. Invest. , vol.79 , pp. 970-977
    • Izumo, S.1    Lompre, A.M.2    Matsuoka, R.3
  • 2
    • 0018093539 scopus 로고
    • Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacement
    • Hoh J.F., McGrath P.A., Hale P.T. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J. Mol. Cell. Cardiol. 10:1978;1053-1076.
    • (1978) J. Mol. Cell. Cardiol. , vol.10 , pp. 1053-1076
    • Hoh, J.F.1    McGrath, P.A.2    Hale, P.T.3
  • 4
    • 0020064214 scopus 로고
    • Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. A characterization of heat liberation in normal and hypertrophied right ventricular papillary muscles
    • Alpert N.R., Mulieri L.A. Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. A characterization of heat liberation in normal and hypertrophied right ventricular papillary muscles. Circ. Res. 50:1982;491-500.
    • (1982) Circ. Res. , vol.50 , pp. 491-500
    • Alpert, N.R.1    Mulieri, L.A.2
  • 5
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: Molecular basis for cardiac adaptation
    • Sugiura S., Kobayakawa N., Fujita H.et al. Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: molecular basis for cardiac adaptation. Circ. Res. 82:1998;1029-1034.
    • (1998) Circ. Res. , vol.82 , pp. 1029-1034
    • Sugiura, S.1    Kobayakawa, N.2    Fujita, H.3
  • 6
    • 0033198519 scopus 로고    scopus 로고
    • Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
    • Palmiter K.A., Tyska M.J., Dupuis D.E., Alpert N.R., Warshaw D.M. Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms. J. Physiol. 519:1999;669-678.
    • (1999) J. Physiol. , vol.519 , pp. 669-678
    • Palmiter, K.A.1    Tyska, M.J.2    Dupuis, D.E.3    Alpert, N.R.4    Warshaw, D.M.5
  • 7
    • 0030685743 scopus 로고    scopus 로고
    • Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium
    • Lowes B.D., Minobe W., Abraham W.T.et al. Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium. J. Clin. Invest. 100:1997;2315-2324.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2315-2324
    • Lowes, B.D.1    Minobe, W.2    Abraham, W.T.3
  • 8
    • 0034599128 scopus 로고    scopus 로고
    • Myosin heavy chain isoform expression in the failing and nonfailing human heart
    • Miyata S., Minobe W., Bristow M.R., Leinwand L.A. Myosin heavy chain isoform expression in the failing and nonfailing human heart. Circ. Res. 86:2000;386-390.
    • (2000) Circ. Res. , vol.86 , pp. 386-390
    • Miyata, S.1    Minobe, W.2    Bristow, M.R.3    Leinwand, L.A.4
  • 10
    • 0000266364 scopus 로고    scopus 로고
    • Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms
    • Schaub M.C., Hefti M.A., Zuellig R.A., Morano I. Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. Cardiovasc. Res. 37:1998;381-404.
    • (1998) Cardiovasc. Res. , vol.37 , pp. 381-404
    • Schaub, M.C.1    Hefti, M.A.2    Zuellig, R.A.3    Morano, I.4
  • 11
    • 0022400802 scopus 로고
    • Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy
    • Hirzel H.O., Tuchschmid C.R., Schneider J., Krayenbuehl H.P., Schaub M.C. Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circ. Res. 57:1985;729-740.
    • (1985) Circ. Res. , vol.57 , pp. 729-740
    • Hirzel, H.O.1    Tuchschmid, C.R.2    Schneider, J.3    Krayenbuehl, H.P.4    Schaub, M.C.5
  • 13
    • 0032853632 scopus 로고    scopus 로고
    • Tuning the human heart molecular motors by myosin light chains
    • Morano I. Tuning the human heart molecular motors by myosin light chains. J. Mol. Med. 77:1999;544-555.
    • (1999) J. Mol. Med. , vol.77 , pp. 544-555
    • Morano, I.1
  • 14
    • 0021231105 scopus 로고
    • Enzymatic comparisons between light chain isozymes of human cardiac myosin subfragment-1
    • Tobacman L.S., Adelstein R.S. Enzymatic comparisons between light chain isozymes of human cardiac myosin subfragment-1. J. Biol. Chem. 259:1984;11226-11230.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11226-11230
    • Tobacman, L.S.1    Adelstein, R.S.2
  • 15
    • 0026608619 scopus 로고
    • Hemodynamic performance and myosin light chain-1 expression of the hypertrophied left ventricle in aortic valve disease before and after valve replacement
    • Sutsch G., Brunner U.T., von Schulthess C.et al. Hemodynamic performance and myosin light chain-1 expression of the hypertrophied left ventricle in aortic valve disease before and after valve replacement. Circ. Res. 70:1992;1035-1043.
    • (1992) Circ. Res. , vol.70 , pp. 1035-1043
    • Sutsch, G.1    Brunner, U.T.2    Von Schulthess, C.3
  • 16
    • 0030038230 scopus 로고    scopus 로고
    • Regulation of human heart contractility by essential myosin light chain isoforms
    • Morano M., Zacharzowski U., Maier M.et al. Regulation of human heart contractility by essential myosin light chain isoforms. J. Clin. Invest. 98:1996;467-473.
    • (1996) J. Clin. Invest. , vol.98 , pp. 467-473
    • Morano, M.1    Zacharzowski, U.2    Maier, M.3
  • 17
    • 0028229723 scopus 로고
    • ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins
    • Yamashita H., Sata M., Sugiura S., Momomura S., Serizawa T., Iizuka M. ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins. Circ. Res. 74:1994;1027-1033.
    • (1994) Circ. Res. , vol.74 , pp. 1027-1033
    • Yamashita, H.1    Sata, M.2    Sugiura, S.3    Momomura, S.4    Serizawa, T.5    Iizuka, M.6
  • 18
    • 0034623233 scopus 로고    scopus 로고
    • Functional consequences of mutations in the smooth muscle myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy
    • Yamashita H., Tyska M.J., Warshaw D.M., Lowey S., Trybus K.M. Functional consequences of mutations in the smooth muscle myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy. J. Biol. Chem. 275:2000;28045-28052.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28045-28052
    • Yamashita, H.1    Tyska, M.J.2    Warshaw, D.M.3    Lowey, S.4    Trybus, K.M.5
  • 19
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction: I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction: I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 21
    • 0031893185 scopus 로고    scopus 로고
    • Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species
    • Reiser P.J., Kline W.O. Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species. Am. J. Physiol. 274:1998;H1048-H1053.
    • (1998) Am. J. Physiol. , vol.274 , pp. 1048-H1053
    • Reiser, P.J.1    Kline, W.O.2
  • 22
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie W.T., Perry S.V. An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119:1970;31-38.
    • (1970) Biochem. J. , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 23
    • 0019332945 scopus 로고
    • The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPase
    • Pemrick S.M. The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPase. J. Biol. Chem. 255:1980;8836-8841.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8836-8841
    • Pemrick, S.M.1
  • 24
    • 0018427133 scopus 로고
    • N-Ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions
    • Meeusen R.L., Cande W.Z. N-Ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions. J. Cell Biol. 82:1979;57-65.
    • (1979) J. Cell Biol. , vol.82 , pp. 57-65
    • Meeusen, R.L.1    Cande, W.Z.2
  • 25
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron S.J., Spudich J.A. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. U. S. A. 83:1986;6272-6276.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 29
    • 0029165327 scopus 로고
    • Maximum speed of shortening and ATPase activity in atrial and ventricular myocardia of hyperthyroid rats
    • Bottinelli R., Canepari M., Cappelli V., Reggiani C. Maximum speed of shortening and ATPase activity in atrial and ventricular myocardia of hyperthyroid rats. Am. J. Physiol. 269:1995;C785-C790.
    • (1995) Am. J. Physiol. , vol.269 , pp. 785-C790
    • Bottinelli, R.1    Canepari, M.2    Cappelli, V.3    Reggiani, C.4
  • 30
    • 0019798668 scopus 로고
    • Formation and characterization of myosin hybrids containing essential light chains and heavy chains from different muscle myosins
    • Wagner P.D. Formation and characterization of myosin hybrids containing essential light chains and heavy chains from different muscle myosins. J. Biol. Chem. 256:1981;2493-2498.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2493-2498
    • Wagner, P.D.1
  • 31
    • 0028983138 scopus 로고
    • Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro
    • VanBuren P., Harris D.E., Alpert N.R., Warshaw D.M. Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circ. Res. 77:1995;439-444.
    • (1995) Circ. Res. , vol.77 , pp. 439-444
    • Vanburen, P.1    Harris, D.E.2    Alpert, N.R.3    Warshaw, D.M.4
  • 32
    • 0032526249 scopus 로고    scopus 로고
    • Functional significance of cardiac myosin essential light chain isoform switching in transgenic mice
    • Fewell J.G., Hewett T.E., Sanbe A.et al. Functional significance of cardiac myosin essential light chain isoform switching in transgenic mice. J. Clin. Invest. 101:1998;2630-2639.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2630-2639
    • Fewell, J.G.1    Hewett, T.E.2    Sanbe, A.3
  • 34
    • 0021368686 scopus 로고
    • Kinetics of the interaction between actin, ADP, and cardiac myosin-S1
    • Siemankowski R.F., White H.D. Kinetics of the interaction between actin, ADP, and cardiac myosin-S1. J. Biol. Chem. 259:1984;5045-5053.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5045-5053
    • Siemankowski, R.F.1    White, H.D.2
  • 35
    • 0030683682 scopus 로고    scopus 로고
    • Interaction of the heavy and light chains of cardiac myosin subfragment-1 with F-actin
    • Andreev O.A., Borejdo J. Interaction of the heavy and light chains of cardiac myosin subfragment-1 with F-actin. Circ. Res. 81:1997;688-693.
    • (1997) Circ. Res. , vol.81 , pp. 688-693
    • Andreev, O.A.1    Borejdo, J.2
  • 36
    • 0033603493 scopus 로고    scopus 로고
    • Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains
    • Timson D.J., Trayer H.R., Smith K.J., Trayer I.P. Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains. J. Biol. Chem. 274:1999;18271-18277.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18271-18277
    • Timson, D.J.1    Trayer, H.R.2    Smith, K.J.3    Trayer, I.P.4
  • 37
    • 0030976482 scopus 로고    scopus 로고
    • Different actin affinities of human cardiac essential myosin light chain isoforms
    • Morano I., Haase H. Different actin affinities of human cardiac essential myosin light chain isoforms. FEBS Lett. 408:1997;71-74.
    • (1997) FEBS Lett. , vol.408 , pp. 71-74
    • Morano, I.1    Haase, H.2
  • 38
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A.F. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:1957;255-318.
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 39
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment I., Rypniewski W.R., Schmidt-Base K.et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 261:1993;50-58.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1    Rypniewski, W.R.2    Schmidt-Base, K.3
  • 40
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda T.Q., Abramson P.D., Spudich J.A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. U. S. A. 93:1996;4459-4464.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 41
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey S., Waller G.S., Trybus K.M. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature. 365:1993;454-456.
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 42
    • 0020324269 scopus 로고
    • Transitions in human atrial and ventricular myosin light-chain isoenzymes in response to cardiac-pressure-overload-induced hypertrophy
    • Cummins P. Transitions in human atrial and ventricular myosin light-chain isoenzymes in response to cardiac-pressure-overload-induced hypertrophy. Biochem. J. 205:1982;195-204.
    • (1982) Biochem. J. , vol.205 , pp. 195-204
    • Cummins, P.1
  • 43
    • 0027183397 scopus 로고
    • Myosin light chain gene expression associated with disease states of the human heart
    • Trahair T., Yeoh T., Cartmill T.et al. Myosin light chain gene expression associated with disease states of the human heart. J. Mol. Cell. Cardiol. 25:1993;577-585.
    • (1993) J. Mol. Cell. Cardiol. , vol.25 , pp. 577-585
    • Trahair, T.1    Yeoh, T.2    Cartmill, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.