메뉴 건너뛰기




Volumn 287, Issue 6 56-6, 2004, Pages

Basal myosin light chain phosphorylation is a determinant of Ca 2+ sensitivity of force and activation dependence of the kinetics of myocardial force development

Author keywords

Kinetics of force development; Skinned myocardium

Indexed keywords

CALCIUM ION; CALMODULIN; DIACETYL OXIME; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN KINASE;

EID: 9344244157     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.01067.2003     Document Type: Article
Times cited : (106)

References (49)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actinomyosin-ATP interaction
    • Adelstein RS and Eisenberg E. Regulation and kinetics of the actinomyosin-ATP interaction. Annu Rev Biochem 49: 921-956, 1980.
    • (1980) Annu Rev Biochem , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 4
    • 0029658668 scopus 로고    scopus 로고
    • 2+ sensitizer EMD 53998 antagonizes the effect of 2,3-butanedione monoxime on skinned cardiac muscle fibres
    • 2+ sensitizer EMD 53998 antagonizes the effect of 2,3-butanedione monoxime on skinned cardiac muscle fibres. Eur J Pharmacol 296: 285-289, 1996.
    • (1996) Eur J Pharmacol , vol.296 , pp. 285-289
    • Barth, Z.1    Strauss, J.D.2    Dohet, C.3    Rüegg, J.C.4
  • 5
    • 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
  • 6
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomysoin ATPase activity in solution
    • Brenner B and Eisenberg E. Rate of force generation in muscle: correlation with actomysoin ATPase activity in solution. Proc Natl Acad Sci USA 83: 3542-3546, 1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 8
    • 0026766553 scopus 로고
    • Protein kinase C enhances myosin light-chain kinase effects on force development and ATPase activity in rat single skinned cardiac cells
    • Clement O, Puceat M, Walsh MP, and Vassort G. Protein kinase C enhances myosin light-chain kinase effects on force development and ATPase activity in rat single skinned cardiac cells. Biochem J 285: 311-317, 1992.
    • (1992) Biochem J , vol.285 , pp. 311-317
    • Clement, O.1    Puceat, M.2    Walsh, M.P.3    Vassort, G.4
  • 9
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres
    • Dantzig JA, Hibberd MG, Trentham DR, and Goldman YE. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J Physiol 432: 639-680, 1991.
    • (1991) J Physiol , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Trentham, D.R.3    Goldman, Y.E.4
  • 10
    • 0035977144 scopus 로고    scopus 로고
    • The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation
    • Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, and Epstein ND. The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell 107: 631-641, 2001.
    • (2001) Cell , vol.107 , pp. 631-641
    • Davis, J.S.1    Hassanzadeh, S.2    Winitsky, S.3    Lin, H.4    Satorius, C.5    Vemuri, R.6    Aletras, A.H.7    Wen, H.8    Epstein, N.D.9
  • 11
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato A. Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol 157: 378-417, 1988.
    • (1988) Methods Enzymol , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 12
    • 0024799085 scopus 로고
    • Phosphorlyation of rodent cardiac myosin light chain 2: Effects of exercise
    • Fitzsimons DP, Bodell PW, and Baldwin KM. Phosphorlyation of rodent cardiac myosin light chain 2: effects of exercise. J Appl Physiol 67: 2447-2453, 1989.
    • (1989) J Appl Physiol , vol.67 , pp. 2447-2453
    • Fitzsimons, D.P.1    Bodell, P.W.2    Baldwin, K.M.3
  • 13
    • 0035862210 scopus 로고    scopus 로고
    • Cross-bridge interaction kinetics in rat myocardium are accelerated by stron binding of myosin to the thin filament
    • Fitzsimons DP, Patel JR, and Moss RL. Cross-bridge interaction kinetics in rat myocardium are accelerated by stron binding of myosin to the thin filament. J Physiol 530: 263-272, 2001.
    • (2001) J Physiol , vol.530 , pp. 263-272
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 14
    • 0019974315 scopus 로고
    • Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog
    • Godt RE and Lindley BD. Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J Gen Physiol 80: 279-297, 1982.
    • (1982) J Gen Physiol , vol.80 , pp. 279-297
    • Godt, R.E.1    Lindley, B.D.2
  • 15
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF. Muscle structure and theories of contraction. Prog Biophys Biophys Chem 7: 257-318, 1957.
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 257-318
    • Huxley, A.F.1
  • 16
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm KE and Stull JT. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu Rev Pharmacol Toxicol 25: 593-620, 1985.
    • (1985) Annu Rev Pharmacol Toxicol , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 17
    • 0027216259 scopus 로고
    • Cross-bridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret
    • Kawai M, Saeki Y, and Zhao Y. Cross-bridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ Res 73: 35-50, 1993.
    • (1993) Circ Res , vol.73 , pp. 35-50
    • Kawai, M.1    Saeki, Y.2    Zhao, Y.3
  • 18
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal thick filaments
    • Levine RJC, Kensler RW, Yang Z, Stull JT, and Sweeney HL. Myosin light chain phosphorylation affects the structure of rabbit skeletal thick filaments. Biophys J 71: 898-907, 1996.
    • (1996) Biophys J , vol.71 , pp. 898-907
    • Levine, R.J.C.1    Kensler, R.W.2    Yang, Z.3    Stull, J.T.4    Sweeney, H.L.5
  • 19
    • 0032940756 scopus 로고    scopus 로고
    • A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibres: Effects of pH, MgADP, and inorganic phosphate
    • Lipscomb S, Palmer RE, Li Q, Allhouse LD, Miller T, Potter JD, and Ashley CC. A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibres: effects of pH, MgADP, and inorganic phosphate. Pflügers Arch 437: 204-212, 1999.
    • (1999) Pflügers Arch , vol.437 , pp. 204-212
    • Lipscomb, S.1    Palmer, R.E.2    Li, Q.3    Allhouse, L.D.4    Miller, T.5    Potter, J.D.6    Ashley, C.C.7
  • 20
    • 0027315793 scopus 로고
    • Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers
    • Lu Z, Moss RL, and Walker JW. Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers. J Gen Physiol 101: 867-888, 1993.
    • (1993) J Gen Physiol , vol.101 , pp. 867-888
    • Lu, Z.1    Moss, R.L.2    Walker, J.W.3
  • 21
    • 0034961156 scopus 로고    scopus 로고
    • Regulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers
    • Lu Z, Swartz DR, Metzger JM, Moss RL, and Walker JW. Regulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers. Biophys 781: 334-344, 2001.
    • (2001) Biophys , vol.781 , pp. 334-344
    • Lu, Z.1    Swartz, D.R.2    Metzger, J.M.3    Moss, R.L.4    Walker, J.W.5
  • 22
    • 0028294216 scopus 로고
    • Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP
    • Martin H and Barsotti RJ. Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP. Biophys J 66: 1115-1128, 1994.
    • (1994) Biophys J , vol.66 , pp. 1115-1128
    • Martin, H.1    Barsotti, R.J.2
  • 23
    • 0030069624 scopus 로고    scopus 로고
    • Effect of phosphate and ADP on shortening velocity during maximal and submaximal calcium activation of thin filament in skeletal muscle
    • Metzger JM. Effect of phosphate and ADP on shortening velocity during maximal and submaximal calcium activation of thin filament in skeletal muscle. Biophys J 70: 409-417, 1996.
    • (1996) Biophys J , vol.70 , pp. 409-417
    • Metzger, J.M.1
  • 24
    • 0024312136 scopus 로고
    • Variation in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • Metzger JM, Greaser ML, and Moss RL. Variation in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. J Gen Physiol 93: 855-883, 1989.
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 25
    • 0025311949 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins: Relationships based on amino acid sequences
    • Moncrief ND, Kretsinger RH, and Goodman M. Evolution of EF-hand calcium-modulated proteins: relationships based on amino acid sequences. J Mol Evol 30: 522-562, 1990.
    • (1990) J Mol Evol , vol.30 , pp. 522-562
    • Moncrief, N.D.1    Kretsinger, R.H.2    Goodman, M.3
  • 26
    • 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: 129-141, 1992.
    • (1992) Basic Res Cardiol , vol.87 , pp. 129-141
    • Morano, I.1
  • 27
    • 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: 544-555, 1999.
    • (1999) J Mol Med , vol.77 , pp. 544-555
    • Morano, I.1
  • 28
    • 0026560943 scopus 로고
    • Expression of myosin heavy and light chains and phosphorylation of the phosphorylatable myosin light chain in the heart ventricle of the European hamster during hibernation and in summer
    • Morano I, Adler K, Agostini B, and Hasselbach W. Expression of myosin heavy and light chains and phosphorylation of the phosphorylatable myosin light chain in the heart ventricle of the European hamster during hibernation and in summer. J Muscle Res Cell Motil 13: 64-70, 1992.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 64-70
    • Morano, I.1    Adler, K.2    Agostini, B.3    Hasselbach, W.4
  • 29
    • 0023762259 scopus 로고
    • Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase
    • Morano I, Bachle-Stolz C, Katus A, and Rüegg JC. Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase. Basic Res Cardiol 83: 350-359, 1988.
    • (1988) Basic Res Cardiol , vol.83 , pp. 350-359
    • Morano, I.1    Bachle-Stolz, C.2    Katus, A.3    Rüegg, J.C.4
  • 30
    • 0021930144 scopus 로고
    • The influence of P-light chain phosphorylation by myosin light chain kinase on the calcium sensitivity of chemically skinned heart fibres
    • Morano I, Hofmann F, Zimmer M, and R̈egg JC. The influence of P-light chain phosphorylation by myosin light chain kinase on the calcium sensitivity of chemically skinned heart fibres. FEBS Lett 189: 221-224, 1985.
    • (1985) FEBS Lett , vol.189 , pp. 221-224
    • Morano, I.1    Hofmann, F.2    Zimmer, M.3    R̈egg, J.C.4
  • 31
    • 0024212357 scopus 로고
    • Chronic hypertension changes myosin isoenzyme pattern and decreases myosin phosphorylation in the rat heart
    • Morano I, Lengsfeld M, Ganten U, Ganten D, and R̈egg JC. Chronic hypertension changes myosin isoenzyme pattern and decreases myosin phosphorylation in the rat heart. J Mol Cell Cardiol 20: 875-886, 1988.
    • (1988) J Mol Cell Cardiol , vol.20 , pp. 875-886
    • Morano, I.1    Lengsfeld, M.2    Ganten, U.3    Ganten, D.4    R̈egg, J.C.5
  • 32
    • 0029011407 scopus 로고
    • Rate of active tension development from rigor in skinned atrial and ventricular cardiac fibres from swine following photolytic release of ATP from caged ATP
    • Morano I, Osterman A, and Arner A. Rate of active tension development from rigor in skinned atrial and ventricular cardiac fibres from swine following photolytic release of ATP from caged ATP. Acta Physiol Scand 154: 343-353, 1995.
    • (1995) Acta Physiol Scand , vol.154 , pp. 343-353
    • Morano, I.1    Osterman, A.2    Arner, A.3
  • 33
    • 0026611165 scopus 로고
    • 2+ regulation of mechanical properties of striated muscle: Mechanistic studies using extraction and replacement of regulatory proteins
    • 2+ regulation of mechanical properties of striated muscle: Mechanistic studies using extraction and replacement of regulatory proteins. Circ Res 70: 865-884, 1992.
    • (1992) Circ Res , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 34
    • 0020644495 scopus 로고
    • 2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths
    • 2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths. Biophys J 43: 115-119, 1983.
    • (1983) Biophys J , vol.43 , pp. 115-119
    • Moss, R.L.1    Swinford, A.E.2    Greaser, M.L.3
  • 35
    • 0021355101 scopus 로고
    • Properties of myosin light chain kinase prepared from rabbit skeletal muscle myosin by an improved method
    • Nagamoto H and Yagi K. Properties of myosin light chain kinase prepared from rabbit skeletal muscle myosin by an improved method. J Biochem (Tokyo) 95: 1119-1130, 1984.
    • (1984) J Biochem (Tokyo) , vol.95 , pp. 1119-1130
    • Nagamoto, H.1    Yagi, K.2
  • 36
    • 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
  • 37
    • 0031972823 scopus 로고    scopus 로고
    • Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle
    • Patel JR, Diffee GM, Huang XP, and Moss RL. Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle. Biophys J 74: 360-368, 1998.
    • (1998) Biophys J , vol.74 , pp. 360-368
    • Patel, J.R.1    Diffee, G.M.2    Huang, X.P.3    Moss, R.L.4
  • 39
    • 0030734153 scopus 로고    scopus 로고
    • Mechanism of action of endothelin in rat cardiac muscle: Cross-bridge kinetics and myosin light chain phosphorylation
    • Rossmanith GH, Hoh JFY, Turnbull L, and Ludowyke RI. Mechanism of action of endothelin in rat cardiac muscle: cross-bridge kinetics and myosin light chain phosphorylation. J Physiol 505: 217-227, 1997.
    • (1997) J Physiol , vol.505 , pp. 217-227
    • Rossmanith, G.H.1    Hoh, J.F.Y.2    Turnbull, L.3    Ludowyke, R.I.4
  • 40
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo AP and Somlyo AV. Signal transduction and regulation in smooth muscle. Nature 372: 231-236, 1994.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 41
    • 0022458216 scopus 로고
    • Phosphorylation of myosin in permeabilized mammalian cardiac and skeletal muscle cells
    • Sweeney HL and Stull JT. Phosphorylation of myosin in permeabilized mammalian cardiac and skeletal muscle cells. Am J Physiol Cell Physiol 250: C657-C660, 1986.
    • (1986) Am J Physiol Cell Physiol , vol.250
    • Sweeney, H.L.1    Stull, J.T.2
  • 42
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL and Stull JT. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc Natl Acad Sci USA 87: 414-418, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 43
    • 0027494274 scopus 로고
    • Determinants of loaded shortening velocity in single cardiac myocytes permeabilized with α-hemolysin
    • Sweitzer NK and Moss RL. Determinants of loaded shortening velocity in single cardiac myocytes permeabilized with α-hemolysin. Circ Res 73: 1150-1162, 1993.
    • (1993) Circ Res , vol.73 , pp. 1150-1162
    • Sweitzer, N.K.1    Moss, R.L.2
  • 45
    • 0036687680 scopus 로고    scopus 로고
    • Troponin I phosphorylation enhances crossbridge kinetics during β-adrenergic stimulation in rat cardiac tissue
    • Turnbull L, Hoh JFY, Ludowyke RI, and Rossmanith GH. Troponin I phosphorylation enhances crossbridge kinetics during β-adrenergic stimulation in rat cardiac tissue. J Physiol 542: 911-920, 2002.
    • (2002) J Physiol , vol.542 , pp. 911-920
    • Turnbull, L.1    Hoh, J.F.Y.2    Ludowyke, R.I.3    Rossmanith, G.H.4
  • 46
    • 0027248968 scopus 로고
    • Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2
    • Venema RC, Raynor RL, Noland TAJ, and Kuo JF. Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2. Biochem J 294: 401-406, 1993.
    • (1993) Biochem J , vol.294 , pp. 401-406
    • Venema, R.C.1    Raynor, R.L.2    Noland, T.A.J.3    Kuo, J.F.4
  • 48
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff MR, McDonald KS, and 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
  • 49
    • 0031692828 scopus 로고    scopus 로고
    • Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers
    • Yang Z, Stull JT, Levine RJC, and Sweeney HL. Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers. J Struct Biol 122: 139-148, 1998.
    • (1998) J Struct Biol , vol.122 , pp. 139-148
    • Yang, Z.1    Stull, J.T.2    Levine, R.J.C.3    Sweeney, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.