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Volumn 301, Issue 1, 2011, Pages

Protein kinase A changes calcium sensitivity but not crossbridge kinetics in human cardiac myofibrils

Author keywords

Heart; Muscle contraction; Phosphatase; Relaxation

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; MYOSIN BINDING PROTEIN C; PHOSPHORUS 32; TROPONIN I;

EID: 79959907357     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00838.2010     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 55149084783 scopus 로고    scopus 로고
    • Myosin binding protein C positioned to play a key role in regulation of muscle contraction: Structure and interactions of domain C1
    • Ababou A, Rostkova E, Mistry S, Le Masurier C, Gautel M, Pfuhl M. Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1. J Mol Biol 384: 615-630, 2008.
    • (2008) J Mol Biol , vol.384 , pp. 615-630
    • Ababou, A.1    Rostkova, E.2    Mistry, S.3    le Masurier, C.4    Gautel, M.5    Pfuhl, M.6
  • 2
    • 62549106588 scopus 로고    scopus 로고
    • Glass microneedles for force measurements: A finite-element analysis model
    • Ayittey PN, Walker JS, Rice JJ, de Tombe PP. Glass microneedles for force measurements: a finite-element analysis model. Pflügers Arch 457: 1415-1422, 2009.
    • (2009) Pflügers Arch , vol.457 , pp. 1415-1422
    • Ayittey, P.N.1    Walker, J.S.2    Rice, J.J.3    de Tombe, P.P.4
  • 4
    • 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: 3265-3629, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3265-3629
    • Brenner, B.1
  • 7
    • 0030948459 scopus 로고    scopus 로고
    • Active and passive forces of isolated myofibrils from cardiac and fast skeletal muscle of the frog
    • Colomo F, Piroddi N, Poggesi C, te Kronnie G, Tesi C. Active and passive forces of isolated myofibrils from cardiac and fast skeletal muscle of the frog. J Physiol 500: 535-548, 1997.
    • (1997) J Physiol , vol.500 , pp. 535-548
    • Colomo, F.1    Piroddi, N.2    Poggesi, C.3    te Kronnie, G.4    Tesi, C.5
  • 9
    • 0028955956 scopus 로고
    • Protein kinase A does not alter economy of force maintenance in skinned rat cardiac trabeculae
    • de Tombe PP, Stienen GJ. Protein kinase A does not alter economy of force maintenance in skinned rat cardiac trabeculae. Circ Res 76: 734-741, 1995.
    • (1995) Circ Res , vol.76 , pp. 734-741
    • de Tombe, P.P.1    Stienen, G.J.2
  • 10
    • 0026093402 scopus 로고
    • Lack of effect of isoproterenol on unloaded velocity of sarcomere shortening in rat cardiac trabeculae
    • de Tombe PP, ter Keurs HE. Lack of effect of isoproterenol on unloaded velocity of sarcomere shortening in rat cardiac trabeculae. Circ Res 68: 382-391, 1991.
    • (1991) Circ Res , vol.68 , pp. 382-391
    • de Tombe, P.P.1    ter Keurs, H.E.2
  • 13
    • 0028271419 scopus 로고
    • Effects of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats
    • Hofmann PA, Lange JH. Effects of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats. Circ Res 74: 718-726, 1994.
    • (1994) Circ Res , vol.74 , pp. 718-726
    • Hofmann, P.A.1    Lange, J.H.2
  • 16
    • 0030305457 scopus 로고    scopus 로고
    • R: A language for data analysis and graphics
    • Ihaka R, Gentleman R. R: a language for data analysis and graphics. J Comp Graph Stat 5: 299-314, 1996.
    • (1996) J Comp Graph Stat , vol.5 , pp. 299-314
    • Ihaka, R.1    Gentleman, R.2
  • 17
    • 33751280974 scopus 로고    scopus 로고
    • Protein kinase A does not alter unloaded velocity of sarcomere shortening in skinned rat cardiac trabeculae
    • Janssen PM, de Tombe PP. Protein kinase A does not alter unloaded velocity of sarcomere shortening in skinned rat cardiac trabeculae. Am J Physiol Heart Circ Physiol 273: H2415-H2422, 1997.
    • (1997) Am J Physiol Heart Circ Physiol , vol.273
    • Janssen, P.M.1    de Tombe, P.P.2
  • 18
    • 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. Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae. Pflügers Arch 433: 842-844, 1997.
    • (1997) Pflügers Arch , vol.433 , pp. 842-844
    • Johns, E.C.1    Simnett, S.J.2    Mulligan, I.P.3    Ashley, C.C.4
  • 19
    • 0019308296 scopus 로고
    • Sinusoidal analysis: A high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish
    • Kawai M, Brandt PW. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J Muscle Res Cell Motil 1: 279-303, 1980.
    • (1980) J Muscle Res Cell Motil , vol.1 , pp. 279-303
    • Kawai, M.1    Brandt, P.W.2
  • 20
    • 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. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ Res 88: 1059-1065, 2001.
    • (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
  • 21
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • Layland J, Solaro RJ, Shah AM. Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc Res 66: 12-21, 2005.
    • (2005) Cardiovasc Res , vol.66 , pp. 12-21
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 25
    • 17444431193 scopus 로고    scopus 로고
    • Sarcomeric determinants of striated muscle relaxation kinetics
    • Poggesi C, Tesi C, Stehle R. Sarcomeric determinants of striated muscle relaxation kinetics. Pflügers Arch 449: 505-517, 2005.
    • (2005) Pflügers Arch , vol.449 , pp. 505-517
    • Poggesi, C.1    Tesi, C.2    Stehle, R.3
  • 26
    • 0017176627 scopus 로고
    • Phosphorylation of the inhibitory subunit of troponin and its effect on the calcium dependence of cardiac myofibril adenosine triphosphatase
    • Ray KP, England PJ. Phosphorylation of the inhibitory subunit of troponin and its effect on the calcium dependence of cardiac myofibril adenosine triphosphatase. FEBS Lett 70: 11-16, 1976.
    • (1976) FEBS Lett , vol.70 , pp. 11-16
    • Ray, K.P.1    England, P.J.2
  • 27
    • 59449108572 scopus 로고    scopus 로고
    • Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae
    • Razumova MV, Bezold KL, Tu AY, Regnier M, Harris SP. Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae. J Gen Physiol 132: 575-585, 2008.
    • (2008) J Gen Physiol , vol.132 , pp. 575-585
    • Razumova, M.V.1    Bezold, K.L.2    Tu, A.Y.3    Regnier, M.4    Harris, S.P.5
  • 28
    • 33846021648 scopus 로고    scopus 로고
    • Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: Evidence for long-lived cross-bridges
    • Razumova MV, Shaffer JF, Tu AY, Flint GV, Regnier M, Harris SP. Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: Evidence for long-lived cross-bridges. J Biol Chem 281: 35846-35854, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 35846-35854
    • Razumova, M.V.1    Shaffer, J.F.2    Tu, A.Y.3    Flint, G.V.4    Regnier, M.5    Harris, S.P.6
  • 29
    • 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: 453-460, 1990.
    • (1990) J Mol Cell Cardiol , vol.22 , pp. 453-460
    • Saeki, Y.1    Shiozawa, K.2    Yanagisawa, K.3    Shibata, T.4
  • 30
    • 0017143827 scopus 로고
    • Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart
    • Solaro RJ, Moir AJ, Perry SV. Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart. Nature 262: 615-617, 1976.
    • (1976) Nature , vol.262 , pp. 615-617
    • Solaro, R.J.1    Moir, A.J.2    Perry, S.V.3
  • 31
    • 0006886180 scopus 로고
    • Troponin-I phosphorylation: A unique regulator of the amounts of caclium required to activate cardiac myofibrils. Cold Spring Harbor Conference
    • Solaro RJ, Robertson S, Johnson J, Holroyde M, Potter J. Troponin-I phosphorylation: a unique regulator of the amounts of caclium required to activate cardiac myofibrils. Cold Spring Harbor Conference. Cell Proliferation 8: 901-911, 1981.
    • (1981) Cell Proliferation , vol.8 , pp. 901-911
    • Solaro, R.J.1    Robertson, S.2    Johnson, J.3    Holroyde, M.4    Potter, J.5
  • 33
    • 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. 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.
    • (2007) Circ Res , vol.101 , pp. 503-511
    • Stelzer, J.E.1    Patel, J.R.2    Walker, J.W.3    Moss, R.L.4
  • 34
    • 0028174245 scopus 로고
    • Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats
    • Strang KT, Sweitzer NK, Greaser ML, Moss RL. Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats. Circ Res 74: 542-549, 1994.
    • (1994) Circ Res , vol.74 , pp. 542-549
    • Strang, K.T.1    Sweitzer, N.K.2    Greaser, M.L.3    Moss, R.L.4
  • 35
    • 0036687680 scopus 로고    scopus 로고
    • phosphorylation enhances crossbridge kinetics during beta-adrenergic stimulation in rat cardiac tissue
    • Turnbull L, Hoh JF, Ludowyke RI, Rossmanith GH. Troponin I phosphorylation enhances crossbridge kinetics during beta-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.2    Ludowyke, R.I.3    Rossmanith, G.H.4    Troponin, I.5
  • 37
    • 0034633299 scopus 로고    scopus 로고
    • A dilution immunoassay to measure myosin light chain phosphorylation
    • Walker JS, Walker LA, Etter EF, Murphy RA. A dilution immunoassay to measure myosin light chain phosphorylation. Anal Biochem 284: 173-182, 2000.
    • (2000) Anal Biochem , vol.284 , pp. 173-182
    • Walker, J.S.1    Walker, L.A.2    Etter, E.F.3    Murphy, R.A.4
  • 38
    • 0022618718 scopus 로고
    • Adrenergic regulation of myosin adenosine triphosphatase activity
    • Winegrad S, Weisberg A, Lin LE, McClellan G. Adrenergic regulation of myosin adenosine triphosphatase activity. Circ Res 58: 83-95, 1986.
    • (1986) Circ Res , vol.58 , pp. 83-95
    • Winegrad, S.1    Weisberg, A.2    Lin, L.E.3    McClellan, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.