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Volumn 53, Issue 3, 2012, Pages 429-436

CaMKII effects on inotropic but not lusitropic force frequency responses require phospholamban

Author keywords

CaM kinase II; Force frequency relation; Frequency dependent acceleration of relaxation; Phospholamban

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; PHOSPHOLAMBAN;

EID: 84864794549     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2012.06.019     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 78649742900 scopus 로고    scopus 로고
    • Myocardial contraction-relaxation coupling
    • Janssen P.M. Myocardial contraction-relaxation coupling. Am J Physiol Heart Circ Physiol 2010, 299:H1741-H1749.
    • (2010) Am J Physiol Heart Circ Physiol , vol.299
    • Janssen, P.M.1
  • 2
    • 4644287428 scopus 로고    scopus 로고
    • Force-frequency relationship in intact mammalian ventricular myocardium: physiological and pathophysiological relevance
    • Endoh M. Force-frequency relationship in intact mammalian ventricular myocardium: physiological and pathophysiological relevance. Eur J Pharmacol 2004, 500:73-86.
    • (2004) Eur J Pharmacol , vol.500 , pp. 73-86
    • Endoh, M.1
  • 3
    • 35348995458 scopus 로고    scopus 로고
    • Determinants of frequency-dependent contraction and relaxation of mammalian myocardium
    • Janssen P.M., Periasamy M. Determinants of frequency-dependent contraction and relaxation of mammalian myocardium. J Mol Cell Cardiol 2007, 43:523-531.
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 523-531
    • Janssen, P.M.1    Periasamy, M.2
  • 4
    • 34250809531 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation involves decreased myofilament calcium sensitivity
    • Varian K.D., Janssen P.M. Frequency-dependent acceleration of relaxation involves decreased myofilament calcium sensitivity. Am J Physiol Heart Circ Physiol 2007, 292:H2212-H2219.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Varian, K.D.1    Janssen, P.M.2
  • 5
    • 77953418093 scopus 로고    scopus 로고
    • Role of CaMKIIdelta phosphorylation of the cardiac ryanodine receptor in the force frequency relationship and heart failure
    • Kushnir A., Shan J., Betzenhauser M.J., Reiken S., Marks A.R. Role of CaMKIIdelta phosphorylation of the cardiac ryanodine receptor in the force frequency relationship and heart failure. Proc Natl Acad Sci U S A 2010, 107:10274-10279.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10274-10279
    • Kushnir, A.1    Shan, J.2    Betzenhauser, M.J.3    Reiken, S.4    Marks, A.R.5
  • 7
    • 15244345086 scopus 로고    scopus 로고
    • Calmodulin kinase signaling in heart: an intriguing candidate target for therapy of myocardial dysfunction and arrhythmias
    • Anderson M.E. Calmodulin kinase signaling in heart: an intriguing candidate target for therapy of myocardial dysfunction and arrhythmias. Pharmacol Ther 2005, 106:39-55.
    • (2005) Pharmacol Ther , vol.106 , pp. 39-55
    • Anderson, M.E.1
  • 8
    • 49049108214 scopus 로고    scopus 로고
    • The role of calmodulin kinase II in myocardial physiology and disease
    • Couchonnal L.F., Anderson M.E. The role of calmodulin kinase II in myocardial physiology and disease. Physiology (Bethesda) 2008, 23:151-159.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 151-159
    • Couchonnal, L.F.1    Anderson, M.E.2
  • 9
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • MacLennan D.H., Kranias E.G. Phospholamban: a crucial regulator of cardiac contractility. Nat Rev Mol Cell Biol 2003, 4:566-577.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 10
    • 63849184245 scopus 로고    scopus 로고
    • Role of CaMKII for signaling and regulation in the heart
    • Maier L.S. Role of CaMKII for signaling and regulation in the heart. Front Biosci 2009, 14:486-496.
    • (2009) Front Biosci , vol.14 , pp. 486-496
    • Maier, L.S.1
  • 11
    • 33846858884 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase (CaMK) in excitation-contraction coupling in the heart
    • 2+/calmodulin-dependent protein kinase (CaMK) in excitation-contraction coupling in the heart. Cardiovasc Res 2007, 73:631-640.
    • (2007) Cardiovasc Res , vol.73 , pp. 631-640
    • Maier, L.S.1    Bers, D.M.2
  • 12
    • 0032953974 scopus 로고    scopus 로고
    • Phospholamban-to-SERCA2 ratio controls the force-frequency relationship
    • Meyer M., Bluhm W.F., He H., Post S.R., Giordano F.J., Lew W.Y., et al. Phospholamban-to-SERCA2 ratio controls the force-frequency relationship. Am J Physiol 1999, 276:H779-H785.
    • (1999) Am J Physiol , vol.276
    • Meyer, M.1    Bluhm, W.F.2    He, H.3    Post, S.R.4    Giordano, F.J.5    Lew, W.Y.6
  • 14
    • 0034697901 scopus 로고    scopus 로고
    • Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes
    • Hagemann D., Kuschel M., Kuramochi T., Zhu W., Cheng H., Xiao R.P. Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes. J Biol Chem 2000, 275:22532-22536.
    • (2000) J Biol Chem , vol.275 , pp. 22532-22536
    • Hagemann, D.1    Kuschel, M.2    Kuramochi, T.3    Zhu, W.4    Cheng, H.5    Xiao, R.P.6
  • 15
    • 27644551362 scopus 로고    scopus 로고
    • Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
    • Mattiazzi A., Mundina-Weilenmann C., Guoxiang C., Vittone L., Kranias E. Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions. Cardiovasc Res 2005, 68:366-375.
    • (2005) Cardiovasc Res , vol.68 , pp. 366-375
    • Mattiazzi, A.1    Mundina-Weilenmann, C.2    Guoxiang, C.3    Vittone, L.4    Kranias, E.5
  • 16
    • 0037106310 scopus 로고    scopus 로고
    • Mechanisms underlying the frequency dependence of contraction and [Ca(2+)](i) transients in mouse ventricular myocytes
    • Antoons G., Mubagwa K., Nevelsteen I., Sipido K.R. Mechanisms underlying the frequency dependence of contraction and [Ca(2+)](i) transients in mouse ventricular myocytes. J Physiol 2002, 543:889-898.
    • (2002) J Physiol , vol.543 , pp. 889-898
    • Antoons, G.1    Mubagwa, K.2    Nevelsteen, I.3    Sipido, K.R.4
  • 17
    • 26244457597 scopus 로고    scopus 로고
    • Myocardial contractility in the echo lab: molecular, cellular and pathophysiological basis
    • Bombardini T. Myocardial contractility in the echo lab: molecular, cellular and pathophysiological basis. Cardiovasc Ultrasound 2005, 3:27.
    • (2005) Cardiovasc Ultrasound , vol.3 , pp. 27
    • Bombardini, T.1
  • 19
    • 0036702654 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban
    • DeSantiago J., Maier L.S., Bers D.M. Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban. J Mol Cell Cardiol 2002, 34:975-984.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 975-984
    • DeSantiago, J.1    Maier, L.S.2    Bers, D.M.3
  • 20
    • 13844271328 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation
    • Valverde C.A., Mundina-Weilenmann C., Said M., Ferrero P., Vittone L., Salas M., et al. Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation. J Physiol 2005, 562:801-813.
    • (2005) J Physiol , vol.562 , pp. 801-813
    • Valverde, C.A.1    Mundina-Weilenmann, C.2    Said, M.3    Ferrero, P.4    Vittone, L.5    Salas, M.6
  • 21
    • 79551583334 scopus 로고    scopus 로고
    • Enhanced myofilament responsiveness upon beta-adrenergic stimulation in post-infarct remodeled myocardium
    • Boontje N.M., Merkus D., Zaremba R., Versteilen A., de Waard M.C., Mearini G., et al. Enhanced myofilament responsiveness upon beta-adrenergic stimulation in post-infarct remodeled myocardium. J Mol Cell Cardiol 2011, 50:487-499.
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 487-499
    • Boontje, N.M.1    Merkus, D.2    Zaremba, R.3    Versteilen, A.4    de Waard, M.C.5    Mearini, G.6
  • 23
    • 20244362095 scopus 로고    scopus 로고
    • Calmodulin kinase II inhibition protects against structural heart disease
    • Zhang R., Khoo M.S., Wu Y., Yang Y., Grueter C.E., Ni G., et al. Calmodulin kinase II inhibition protects against structural heart disease. Nat Med 2005, 11:409-417.
    • (2005) Nat Med , vol.11 , pp. 409-417
    • Zhang, R.1    Khoo, M.S.2    Wu, Y.3    Yang, Y.4    Grueter, C.E.5    Ni, G.6
  • 24
    • 0033039754 scopus 로고    scopus 로고
    • Modulation of force-frequency relation by phospholamban in genetically engineered mice
    • Kadambi V.J., Ball N., Kranias E.G., Walsh R.A., Hoit B.D. Modulation of force-frequency relation by phospholamban in genetically engineered mice. Am J Physiol 1999, 276:H2245-H2250.
    • (1999) Am J Physiol , vol.276
    • Kadambi, V.J.1    Ball, N.2    Kranias, E.G.3    Walsh, R.A.4    Hoit, B.D.5
  • 25
    • 31444441035 scopus 로고    scopus 로고
    • Suppression of dynamic Ca(2+) transient responses to pacing in ventricular myocytes from mice with genetic calmodulin kinase II inhibition
    • Wu Y., Shintani A., Grueter C., Zhang R., Hou Y., Yang J., et al. Suppression of dynamic Ca(2+) transient responses to pacing in ventricular myocytes from mice with genetic calmodulin kinase II inhibition. J Mol Cell Cardiol 2006, 40:213-223.
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 213-223
    • Wu, Y.1    Shintani, A.2    Grueter, C.3    Zhang, R.4    Hou, Y.5    Yang, J.6
  • 27
    • 77955277122 scopus 로고    scopus 로고
    • Calcium sensitivity and the Frank-Starling mechanism of the heart are increased in titin N2B region-deficient mice
    • Lee E.J., Peng J., Radke M., Gotthardt M., Granzier H.L. Calcium sensitivity and the Frank-Starling mechanism of the heart are increased in titin N2B region-deficient mice. J Mol Cell Cardiol 2010, 49:449-458.
    • (2010) J Mol Cell Cardiol , vol.49 , pp. 449-458
    • Lee, E.J.1    Peng, J.2    Radke, M.3    Gotthardt, M.4    Granzier, H.L.5
  • 28
    • 42949085382 scopus 로고    scopus 로고
    • A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
    • Erickson J.R., Joiner M.L., Guan X., Kutschke W., Yang J., Oddis C.V., et al. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 2008, 133:462-474.
    • (2008) Cell , vol.133 , pp. 462-474
    • Erickson, J.R.1    Joiner, M.L.2    Guan, X.3    Kutschke, W.4    Yang, J.5    Oddis, C.V.6
  • 29
    • 3142616782 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of systolic and diastolic dysfunction in an avian model of dilated cardiomyopathy
    • Wu Y., Tobias A.H., Bell K., Barry W., Helmes M., Trombitas K., et al. Cellular and molecular mechanisms of systolic and diastolic dysfunction in an avian model of dilated cardiomyopathy. J Mol Cell Cardiol 2004, 37:111-119.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 111-119
    • Wu, Y.1    Tobias, A.H.2    Bell, K.3    Barry, W.4    Helmes, M.5    Trombitas, K.6
  • 30
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla O., Wu Y., Irving T.C., Granzier H. Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ Res 2001, 88:1028-1035.
    • (2001) Circ Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 31
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol Paris 1979, 75:463-505.
    • (1979) J Physiol Paris , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 33
    • 4444368240 scopus 로고    scopus 로고
    • Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics
    • Tong C.W., Gaffin R.D., Zawieja D.C., Muthuchamy M. Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics. J Physiol 2004, 558:927-941.
    • (2004) J Physiol , vol.558 , pp. 927-941
    • Tong, C.W.1    Gaffin, R.D.2    Zawieja, D.C.3    Muthuchamy, M.4
  • 34
    • 0024778855 scopus 로고
    • Frequency-dependent inhibition of the intracellular calcium transients by calmodulin antagonists in the aequorin-injected rabbit papillary muscle
    • Endoh M. Frequency-dependent inhibition of the intracellular calcium transients by calmodulin antagonists in the aequorin-injected rabbit papillary muscle. Adv Exp Med Biol 1989, 255:461-470.
    • (1989) Adv Exp Med Biol , vol.255 , pp. 461-470
    • Endoh, M.1
  • 35
    • 0032520057 scopus 로고    scopus 로고
    • Calcium cycling and contractile activation in intact mouse cardiac muscle
    • Gao W.D., Perez N.G., Marban E. Calcium cycling and contractile activation in intact mouse cardiac muscle. J Physiol 1998, 507(Pt 1):175-184.
    • (1998) J Physiol , vol.507 , Issue.PART 1 , pp. 175-184
    • Gao, W.D.1    Perez, N.G.2    Marban, E.3
  • 36
    • 0036850754 scopus 로고    scopus 로고
    • Effect of stimulation rate, sarcomere length and Ca(2+) on force generation by mouse cardiac muscle
    • Stuyvers B.D., McCulloch A.D., Guo J., Duff H.J., ter Keurs H.E. Effect of stimulation rate, sarcomere length and Ca(2+) on force generation by mouse cardiac muscle. J Physiol 2002, 544:817-830.
    • (2002) J Physiol , vol.544 , pp. 817-830
    • Stuyvers, B.D.1    McCulloch, A.D.2    Guo, J.3    Duff, H.J.4    ter Keurs, H.E.5
  • 37
    • 3042763171 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ Res 2004, 94:e61-e70.
    • (2004) Circ Res , vol.94
    • Wehrens, X.H.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 38
    • 3242679707 scopus 로고    scopus 로고
    • Threonine-17 phosphorylation of phospholamban: a key determinant of frequency-dependent increase of cardiac contractility
    • Zhao W., Uehara Y., Chu G., Song Q., Qian J., Young K., et al. Threonine-17 phosphorylation of phospholamban: a key determinant of frequency-dependent increase of cardiac contractility. J Mol Cell Cardiol 2004, 37:607-612.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 607-612
    • Zhao, W.1    Uehara, Y.2    Chu, G.3    Song, Q.4    Qian, J.5    Young, K.6
  • 39
    • 2842612680 scopus 로고    scopus 로고
    • Ser16-, but not Thr17-phosphorylation of phospholamban influences frequency-dependent force generation in human myocardium
    • Brixius K., Wollmer A., Bolck B., Mehlhorn U., Schwinger R.H. Ser16-, but not Thr17-phosphorylation of phospholamban influences frequency-dependent force generation in human myocardium. Pflugers Arch 2003, 447:150-157.
    • (2003) Pflugers Arch , vol.447 , pp. 150-157
    • Brixius, K.1    Wollmer, A.2    Bolck, B.3    Mehlhorn, U.4    Schwinger, R.H.5
  • 40
    • 77958063805 scopus 로고    scopus 로고
    • Kinetics of cardiac muscle contraction and relaxation are linked and determined by properties of the cardiac sarcomere
    • Janssen P.M. Kinetics of cardiac muscle contraction and relaxation are linked and determined by properties of the cardiac sarcomere. Am J Physiol Heart Circ Physiol 2010, 299:H1092-H1099.
    • (2010) Am J Physiol Heart Circ Physiol , vol.299
    • Janssen, P.M.1
  • 41
    • 70349756663 scopus 로고    scopus 로고
    • Threonine-5 at the N-terminus can modulate sarcolipin function in cardiac myocytes
    • Bhupathy P., Babu G.J., Ito M., Periasamy M. Threonine-5 at the N-terminus can modulate sarcolipin function in cardiac myocytes. J Mol Cell Cardiol 2009, 47:723-729.
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 723-729
    • Bhupathy, P.1    Babu, G.J.2    Ito, M.3    Periasamy, M.4
  • 42
    • 0028930629 scopus 로고
    • CaMKII is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes
    • Bassani R.A., Mattiazzi A., Bers D.M. CaMKII is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes. Am J Physiol 1995, 268:H703-H712.
    • (1995) Am J Physiol , vol.268
    • Bassani, R.A.1    Mattiazzi, A.2    Bers, D.M.3
  • 43
    • 0031922664 scopus 로고    scopus 로고
    • Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects
    • Li L., Chu G., Kranias E.G., Bers D.M. Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects. Am J Physiol 1998, 274:H1335-H1347.
    • (1998) Am J Physiol , vol.274
    • Li, L.1    Chu, G.2    Kranias, E.G.3    Bers, D.M.4
  • 44
    • 52049115619 scopus 로고    scopus 로고
    • Phospholamban phosphorylation by CaMKII under pathophysiological conditions
    • Vittone L., Mundina-Weilenmann C., Mattiazzi A. Phospholamban phosphorylation by CaMKII under pathophysiological conditions. Front Biosci 2008, 13:5988-6005.
    • (2008) Front Biosci , vol.13 , pp. 5988-6005
    • Vittone, L.1    Mundina-Weilenmann, C.2    Mattiazzi, A.3
  • 46
    • 33646398865 scopus 로고    scopus 로고
    • The importance of the Thr17 residue of phospholamban as a phosphorylation site under physiological and pathological conditions
    • Mattiazzi A., Mundina-Weilenmann C., Vittone L., Said M., Kranias E.G. The importance of the Thr17 residue of phospholamban as a phosphorylation site under physiological and pathological conditions. Braz J Med Biol Res 2006, 39:563-572.
    • (2006) Braz J Med Biol Res , vol.39 , pp. 563-572
    • Mattiazzi, A.1    Mundina-Weilenmann, C.2    Vittone, L.3    Said, M.4    Kranias, E.G.5


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