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Volumn 290, Issue 2, 2006, Pages

Targeted inhibition of sarcoplasmic reticulum CaMKII activity results in alterations of Ca2+ homeostasis and cardiac contractility

Author keywords

adrenergic stimulation; Calcium calmodulin dependent protein kinase II; Cardiac contractility; Phospholamban; Ryanodine receptor; Transgenic mice

Indexed keywords

BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CAFFEINE; ISOPRENALINE; PHOSPHOLAMBAN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; RYANODINE RECEPTOR; CALCIUM; CALCIUM BINDING PROTEIN; CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN-DEPENDENT PROTEIN KINASE II; CAMKII INHIBITOR AIP; CARDIOTONIC AGENT; PEPTIDE; PROTEIN KINASE (CALCIUM,CALMODULIN);

EID: 33644855766     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00214.2005     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0028930629 scopus 로고
    • CaMKII is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes
    • Bassani RA, Mattiazzi A, and Bers DM. CaMKII is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes. Am J Physiol Heart Circ Physiol 268: H703-H712, 1995.
    • (1995) Am J Physiol Heart Circ Physiol , vol.268
    • Bassani, R.A.1    Mattiazzi, A.2    Bers, D.M.3
  • 3
    • 0029098909 scopus 로고
    • Sarcoplasmic reticulum in cardiac length-dependent activation in rabbits
    • Bluhm WF and Lew WYW. Sarcoplasmic reticulum in cardiac length-dependent activation in rabbits. Am J Physiol Heart Circ Physiol 269: H965-H972, 1995.
    • (1995) Am J Physiol Heart Circ Physiol , vol.269
    • Bluhm, W.F.1    Lew, W.Y.W.2
  • 4
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: Form to function
    • Braun AP and Schulman H. The multifunctional calcium/calmodulin-dependent protein kinase: form to function. Annu Rev Physiol 57: 417-445, 1995.
    • (1995) Annu Rev Physiol , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 5
    • 0034697029 scopus 로고    scopus 로고
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban. J Biol Chem 275: 12129-12135, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12129-12135
    • Brittsan, A.G.1    Carr, A.N.2    Schmidt, A.G.3    Kranias, E.G.4
  • 6
    • 0034623718 scopus 로고    scopus 로고
    • 16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac response of β-agonist
    • 16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac response of β-agonist. J Biol Chem 275: 38938-38943, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 38938-38943
    • Chu, G.1    Lester, J.W.2    Young, K.B.3    Luo, W.4    Zhai, J.5    Kranias, E.G.6
  • 7
    • 0942290432 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IIδ associates with the ryanodine receptor complex and regulates channel function in rabbit heart
    • Currie S, Loughrey CM, Craig MA, and Smith GL. Calcium/calmodulin- dependent protein kinase IIδ associates with the ryanodine receptor complex and regulates channel function in rabbit heart. Biochem J 377: 357-366, 2004.
    • (2004) Biochem J , vol.377 , pp. 357-366
    • Currie, S.1    Loughrey, C.M.2    Craig, M.A.3    Smith, G.L.4
  • 8
    • 0036702654 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban
    • DeSantiago J, Maier LS, and Bers DM. Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban. J Mol Cell Cardiol 34: 975-984, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 975-984
    • DeSantiago, J.1    Maier, L.S.2    Bers, D.M.3
  • 9
    • 0016842083 scopus 로고
    • Dependence of the contractile activation of skinned cardiac cells on the sarcomere length
    • Fabiato A and Fabiato F. Dependence of the contractile activation of skinned cardiac cells on the sarcomere length. Nature 256: 54-56, 1975.
    • (1975) Nature , vol.256 , pp. 54-56
    • Fabiato, A.1    Fabiato, F.2
  • 10
    • 0344661975 scopus 로고    scopus 로고
    • The isolated work-performing mouse heart preparation. Comparison and quantification of cardiac performance in transgenic and wild-type mice
    • edited by Walsh RA and Hoid BD. Boston, MA: Kluwer
    • Grupp IL, Grupp G, and Syfris G. The isolated work-performing mouse heart preparation. Comparison and quantification of cardiac performance in transgenic and wild-type mice. In: Cardiovascular Physiology in the Genetically Engineered Mouse, edited by Walsh RA and Hoid BD. Boston, MA: Kluwer, 1998, p. 77-95.
    • (1998) Cardiovascular Physiology in the Genetically Engineered Mouse , pp. 77-95
    • Grupp, I.L.1    Grupp, G.2    Syfris, G.3
  • 11
    • 0029670185 scopus 로고    scopus 로고
    • 2+ current in isolated rat ventricular myocytes following an increase in cell length
    • 2+ current in isolated rat ventricular myocytes following an increase in cell length. J Physiol 491: 609-619, 1996.
    • (1996) J Physiol , vol.491 , pp. 609-619
    • Hongo, K.1    White, E.2    Le Guennec, J.Y.3    Orchard, C.H.4
  • 12
    • 0042591401 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II in cardiac longitudinal sarcoplasmic reticulum results in decreased phospholamban phosphorylation at threonine 17
    • 2+/calmodulin-dependent protein kinase II in cardiac longitudinal sarcoplasmic reticulum results in decreased phospholamban phosphorylation at threonine 17. J Biol Chem 278: 25063-25071, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 25063-25071
    • Ji, Y.1    Li, B.2    Reed, T.D.3    Lorenz, J.N.4    Kaetzel, M.A.5    Dedman, J.R.6
  • 13
    • 0345643419 scopus 로고    scopus 로고
    • 2+ ATPase enzymatic properties using mouse cardiac tissue homogenates
    • 2+ ATPase enzymatic properties using mouse cardiac tissue homogenates. Anal Biochem 269: 236-244, 1999.
    • (1999) Anal Biochem , vol.269 , pp. 236-244
    • Ji, Y.1    Loukianov, E.2    Periasamy, M.3
  • 14
    • 0024366890 scopus 로고
    • Differential tissue expression of three 35-kDa annexin calcium-dependent phospholipids-binding proteins
    • Kaetzel MA, Hazarika P, and Dedman JR. Differential tissue expression of three 35-kDa annexin calcium-dependent phospholipids-binding proteins. J Biol Chem 264: 14463-14470, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 14463-14470
    • Kaetzel, M.A.1    Hazarika, P.2    Dedman, J.R.3
  • 15
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura Y, Kurzydlowski K, Tada M, and MacLennan DH. Phospholamban inhibitory function is activated by depolymerization. J Biol Chem 272: 15061-15064, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 16
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filament, and the integrative biology of cardiac contractility
    • Kobayashi T and Solaro RJ. Calcium, thin filament, and the integrative biology of cardiac contractility. Annu Rev Physiol 67: 39-67, 2005.
    • (2005) Annu Rev Physiol , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 17
    • 0022429894 scopus 로고
    • 2+ transport by cyclic 3′,5′-AMP- dependent and calcium-calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum
    • 2+ transport by cyclic 3′,5′-AMP-dependent and calcium-calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Biochim Biophys Acta 844: 193-199, 1985.
    • (1985) Biochim Biophys Acta , vol.844 , pp. 193-199
    • Kranias, E.G.1
  • 19
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo W, Chu G, Sato Y, Zhou Z, Kadambi VJ, and Kranias EG. Transgenic approaches to define the functional role of dual site phospholamban phosphorylation. J Biol Chem 273: 4734-4739, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 4734-4739
    • Luo, W.1    Chu, G.2    Sato, Y.3    Zhou, Z.4    Kadambi, V.J.5    Kranias, E.G.6
  • 20
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan DH and Kranias EG. Phospholamban: a crucial regulator of cardiac contractility. Nat Rev Mol Cell Biol 4: 566-577, 2003.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 21
    • 0036702526 scopus 로고    scopus 로고
    • Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat to heartbeat and beyond
    • Maier LS and Bers DM. Calcium, calmodulin, and calcium-calmodulin kinase II: heartbeat to heartbeat and beyond. J Mol Cell Cardiol 34: 919-939, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 919-939
    • Maier, L.S.1    Bers, D.M.2
  • 23
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatus Y, Jayaraman T, Burkhoff D, Rosemblit N, and Marks AR. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 101: 365-376, 2000.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatus, Y.3    Jayaraman, T.4    Burkhoff, D.5    Rosemblit, N.6    Marks, A.R.7
  • 24
    • 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, and Winegrad S. Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C. Biophys J 81: 1083-1092, 2001.
    • (2001) Biophys J , vol.81 , pp. 1083-1092
    • McClellan, G.1    Kulikovskaya, I.2    Winegrad, S.3
  • 25
    • 0025773177 scopus 로고
    • Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction
    • Morgan JP. Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction. N Engl J Med 325: 625-632, 1991.
    • (1991) N Engl J Med , vol.325 , pp. 625-632
    • Morgan, J.P.1
  • 26
    • 33646404576 scopus 로고    scopus 로고
    • CaMKII inhibitor targeted to phospholamban inhibits frequency-dependent acceleration of relaxation and, surprisingly, Ca current facilitation
    • Picht E, DeSantiago J, Dedman JR, and Bers DM. CaMKII inhibitor targeted to phospholamban inhibits frequency-dependent acceleration of relaxation and, surprisingly, Ca current facilitation (Abstract). Circulation 131, Suppl III: 620, 2004.
    • (2004) Circulation , vol.131 , Issue.3 SUPPL. , pp. 620
    • Picht, E.1    DeSantiago, J.2    Dedman, J.R.3    Bers, D.M.4
  • 27
    • 0141532146 scopus 로고    scopus 로고
    • Stoichiometric phosphorylation of cardiac ryanodine receptor on serine 2809 by calmodulin-dependent kinase II and protein kinase A
    • Rodriguez P, Bhogal MS, and Coyler J. Stoichiometric phosphorylation of cardiac ryanodine receptor on serine 2809 by calmodulin-dependent kinase II and protein kinase A. J Biol Chem 278: 38593-38600, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 38593-38600
    • Rodriguez, P.1    Bhogal, M.S.2    Coyler, J.3
  • 28
    • 0036750178 scopus 로고    scopus 로고
    • The relative relevance of phosphorylation of the Thr(17) residue of phospholamban is different at different levels of β-adrenergic stimulation
    • Said M, Mundina-Weilenmann C, Vittone L, and Mattiazzi A. The relative relevance of phosphorylation of the Thr(17) residue of phospholamban is different at different levels of β-adrenergic stimulation. Pflügers Arch 444: 801-809, 2002.
    • (2002) Pflügers Arch , vol.444 , pp. 801-809
    • Said, M.1    Mundina-Weilenmann, C.2    Vittone, L.3    Mattiazzi, A.4
  • 29
    • 4444368240 scopus 로고    scopus 로고
    • Role of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics
    • Tong CW, Gaffin RD, Zawiejia DC, and Muthuchamy M. Role of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics. J Physiol 558: 927-941, 2004.
    • (2004) J Physiol , vol.558 , pp. 927-941
    • Tong, C.W.1    Gaffin, R.D.2    Zawiejia, D.C.3    Muthuchamy, M.4
  • 32
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher DR, Kovacs RJ, Schulman H, Cefali DC, and Jones LR. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 266: 11144-11152, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5
  • 34
    • 3242744450 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II in cardiac hypertrophy and heart failure
    • 2+/calmodulin-dependent protein kinase II in cardiac hypertrophy and heart failure. Cardiovasc Res 63: 476-486, 2004.
    • (2004) Cardiovasc Res , vol.63 , pp. 476-486
    • Zhang, T.1    Brown, J.H.2


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