메뉴 건너뛰기




Volumn 34, Issue 9, 2002, Pages 1135-1139

Relaxation... It's not getting any easier

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; CALMODULIN; HELIX LOOP HELIX PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN SERINE THREONINE KINASE;

EID: 0036749968     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2828(02)92055-9     Document Type: Editorial
Times cited : (1)

References (35)
  • 1
    • 0022558520 scopus 로고
    • Intracellular calcium transients underlyng the short-term force-interval relationship in ferret ventricular myocardium
    • Wier WG, Yue DT. Intracellular calcium transients underlyng the short-term force-interval relationship in ferret ventricular myocardium. J Physiol (Lond) 1986; 376: 507-530.
    • (1986) J Physiol (Lond) , vol.376 , pp. 507-530
    • Wier, W.G.1    Yue, D.T.2
  • 2
    • 0021957372 scopus 로고
    • Postextrasystolic potentiation of the isolated canine left ventricle: Relationship to mechanical restitution
    • Yue DT, Burkhoff D, Franz M et al. Postextrasystolic potentiation of the isolated canine left ventricle: relationship to mechanical restitution. Circ Res 1985; 56: 340-350.
    • (1985) Circ Res , vol.56 , pp. 340-350
    • Yue, D.T.1    Burkhoff, D.2    Franz, M.3
  • 3
    • 0017045434 scopus 로고
    • Evaluation of the force-frequency relationship as a descriptor of the inotropic state of canine left ventricular myocardium
    • Anderson P, Rankins J, Arentzen C et al. Evaluation of the force-frequency relationship as a descriptor of the inotropic state of canine left ventricular myocardium. Circ Res 1976; 39: 832-839.
    • (1976) Circ Res , vol.39 , pp. 832-839
    • Anderson, P.1    Rankins, J.2    Arentzen, C.3
  • 4
    • 0033039754 scopus 로고    scopus 로고
    • Modulation of the force frequency relation by phospholamban in genetically engineered mice
    • Kadambi VJ, Ball N, Kranias EG et al. Modulation of the 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
  • 5
    • 0012681048 scopus 로고
    • The cardiovascular system I
    • Berne RM (ed.). Bethesda, MD: American Physiology Society
    • Johnson EA. The cardiovascular system I. In: Berne RM (ed.) Handbook of Physiology. 1979: Bethesda, MD: American Physiology Society, 475-496.
    • (1979) Handbook of Physiology , pp. 475-496
    • Johnson, E.A.1
  • 6
    • 0030833435 scopus 로고    scopus 로고
    • Force-frequency effect is a powerful determinant of myocardial contractility in the mouse
    • Palakodeti V, Oh S, Oh BH et al. Force-frequency effect is a powerful determinant of myocardial contractility in the mouse. Am J Physiol 1997; 273: H1283-H1290.
    • (1997) Am J Physiol , vol.273
    • Palakodeti, V.1    Oh, S.2    Oh, B.H.3
  • 7
    • 0028850826 scopus 로고
    • Effect of tachycardiac heart failure on the restitution of left ventricular function in closed-chest dogs
    • Prabhu SD, Freeman GL. Effect of tachycardiac heart failure on the restitution of left ventricular function in closed-chest dogs. Circulation 1995; 91: 176-185.
    • (1995) Circulation , vol.91 , pp. 176-185
    • Prabhu, S.D.1    Freeman, G.L.2
  • 8
    • 0029797234 scopus 로고    scopus 로고
    • Effects of thyroid hormone on left ventricular performance and regulation of contractile and Ca(2+)-cycling proteins in the baboon. Implications for the force-frequency and relaxation-frequency relationships
    • Khoury SF, Hoit BD, Dave V et al. Effects of thyroid hormone on left ventricular performance and regulation of contractile and Ca(2+)-cycling proteins in the baboon. Implications for the force-frequency and relaxation-frequency relationships. Circ Res 1996: 79: 727-735.
    • (1996) Circ Res , vol.79 , pp. 727-735
    • Khoury, S.F.1    Hoit, B.D.2    Dave, V.3
  • 9
    • 0036545583 scopus 로고    scopus 로고
    • Cardiac Na/Ca exchange function in rabbit, mouse and man: What's the difference?
    • Bers DM. Cardiac Na/Ca exchange fucntion in rabbit, mouse and man: what's the difference? J Mol Cell Cardiol 2002.
    • (2002) J Mol Cell Cardiol
    • Bers, D.M.1
  • 10
    • 0033538344 scopus 로고    scopus 로고
    • Ca2+ handling and sarcoplasmic reticulum Ca2+ content in isolated failing and nonfailing human myocardium
    • Pieske B, Maier LS, Bers DM et al. Ca2+ handling and sarcoplasmic reticulum Ca2+ content in isolated failing and nonfailing human myocardium. Circ Res 1999; 85: 38-46.
    • (1999) Circ Res , vol.85 , pp. 38-46
    • Pieske, B.1    Maier, L.S.2    Bers, D.M.3
  • 11
    • 0034502322 scopus 로고    scopus 로고
    • Differences in Ca(2+)-handling and sarcoplasmic reticulum Ca(2+)-content in isolated rat and rabbit myocardium
    • Maier LS, Bers DM, Pieske B. Differences in Ca(2+)-handling and sarcoplasmic reticulum Ca(2+)-content in isolated rat and rabbit myocardium. J Mol Cell Cardiol 2000; 32: 2249-2258.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2249-2258
    • Maier, L.S.1    Bers, D.M.2    Pieske, B.3
  • 12
    • 0032403984 scopus 로고    scopus 로고
    • Ryanodine the left ventricular force-interval and relaxation-interval relations in closed-chest dogs: Insights on calcium handling
    • Prabhu SD. Ryanodine and the left ventricular force-interval and relaxation-interval relations in closed-chest dogs: insights on calcium handling. Cardiovasc Res 1998; 40: 483-491.
    • (1998) Cardiovasc Res , vol.40 , pp. 483-491
    • Prabhu, S.D.1
  • 13
    • 0027994674 scopus 로고
    • Calmodulin and the regulation of smooth muscle contraction
    • Walsh MP. Calmodulin and the regulation of smooth muscle contraction. Mol Cell Biochem 1994; 135: 21-41.
    • (1994) Mol Cell Biochem , vol.135 , pp. 21-41
    • Walsh, M.P.1
  • 14
    • 0035028435 scopus 로고    scopus 로고
    • Ca(2+)/CaM-dependent kinases: From activation to function
    • Hook SS, Means AR. Ca(2+)/CaM-dependent kinases: from activation to function. Annu Rev Pharmacol Toxicol 2001; 41: 471-505.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 471-505
    • Hook, S.S.1    Means, A.R.2
  • 15
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: From form to function
    • Braun AP, Schulman H. The multifunctional calcium/calmodulin-dependent protein kinase: from form to function. Annu Rev Physiol 1995; 57: 417-445.
    • (1995) Annu Rev Physiol , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 16
    • 0037059791 scopus 로고    scopus 로고
    • The cardiac-specific nuclear delta(B) isoform of Ca2+/calmodulin-dependent protein kinase II induces hypertrophy and dilated cardiomyopathy associated with increased protein phosphatase 2A activity
    • Zhang T, Johnson EN, Gu Y et al. The cardiac-specific nuclear delta(B) isoform of Ca2+/calmodulin-dependent protein kinase II induces hypertrophy and dilated cardiomyopathy associated with increased protein phosphatase 2A activity. J Biol Chem 2002; 277: 1261-1267.
    • (2002) J Biol Chem , vol.277 , pp. 1261-1267
    • Zhang, T.1    Johnson, E.N.2    Gu, Y.3
  • 18
    • 0029882295 scopus 로고    scopus 로고
    • Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications binding IQ-motifs
    • Swindells MB, Ikura M. Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications binding IQ-motifs. Nat Struct Biol 1996; 3: 501-504.
    • (1996) Nat Struct Biol , vol.3 , pp. 501-504
    • Swindells, M.B.1    Ikura, M.2
  • 19
    • 0033125604 scopus 로고    scopus 로고
    • Ser16 prevails over Thr17 phospholamban phosphorylation in the beta-adrenergic regulation of cardiac relaxation
    • Kuschel M, Karczewski P, Hempel P et al. Ser16 prevails over Thr17 phospholamban phosphorylation in the beta-adrenergic regulation of cardiac relaxation. Am J Physiol 1999; 276: H1625-H1633.
    • (1999) Am J Physiol , vol.276
    • Kuschel, M.1    Karczewski, P.2    Hempel, P.3
  • 20
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo W, Chu G, Sato Y et al. Transgenic approaches to define the functional role of dual site phospholamban phosphorylation. J Biol Chem 1998; 273: 4734-4739.
    • (1998) J Biol Chem , vol.273 , pp. 4734-4739
    • Luo, W.1    Chu, G.2    Sato, Y.3
  • 21
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi VJ, Ponniah S, Harrer JM et al. Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J Clin Invest 1996; 97: 533-539.
    • (1996) J Clin Invest , vol.97 , pp. 533-539
    • Kadambi, V.J.1    Ponniah, S.2    Harrer, J.M.3
  • 22
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo W, Grupp IL, Harrer J et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res 1994; 75: 401-409.
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3
  • 23
    • 0035852663 scopus 로고    scopus 로고
    • Interactions between phospholamban and beta-adrenergic drive may lead to cardiomyopathy and early mortality
    • Dash R, Kadambi V, Schmidt AG et al. Interactions between phospholamban and beta-adrenergic drive may lead to cardiomyopathy and early mortality. Circulation 2001; 103: 889-896.
    • (2001) Circulation , vol.103 , pp. 889-896
    • Dash, R.1    Kadambi, V.2    Schmidt, A.G.3
  • 24
    • 0033969489 scopus 로고    scopus 로고
    • Phospholamban: A major determinant of the cardiac force-frequency relationship
    • Bluhm WF, Kranias EG, Dillmann WH et al. Phospholamban: a major determinant of the cardiac force-frequency relationship. Am J Physiol Heart Circ Physiol 2000; 278: H249-H255.
    • (2000) Am J Physiol Heart Circ Physiol , vol.278
    • Bluhm, W.F.1    Kranias, E.G.2    Dillmann, W.H.3
  • 25
    • 0011058685 scopus 로고    scopus 로고
    • Genetically altered phospholamban levels modulate the rate of mechanical restitution in vivo
    • Kadambi VJ, Ball N, Bannerjee A et al. Genetically altered phospholamban levels modulate the rate of mechanical restitution in vivo. Circulation 1998; 98: I-142.
    • (1998) Circulation , vol.98
    • Kadambi, V.J.1    Ball, N.2    Bannerjee, A.3
  • 26
    • 0034623718 scopus 로고    scopus 로고
    • A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to beta-agonists
    • Chu G, Lester JW, Young KB et al. A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to beta-agonists. J Biol Chem 2000; 275: 38938-38943.
    • (2000) J Biol Chem , vol.275 , pp. 38938-38943
    • Chu, G.1    Lester, J.W.2    Young, K.B.3
  • 27
    • 0034697901 scopus 로고    scopus 로고
    • Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes
    • Hagemann D, Kuschel M, Kuramochi T et al. 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
  • 28
    • 33751260357 scopus 로고    scopus 로고
    • Rate-dependent abbreviation of Ca2+ transient in rat heart is independent of phospholamban phosphorylation
    • Hussain M, Drago GA, Colyer J et al. Rate-dependent abbreviation of Ca2+ transient in rat heart is independent of phospholamban phosphorylation. Am J Physiol 1997; 273: H695-H706.
    • (1997) Am J Physiol , vol.273
    • Hussain, M.1    Drago, G.A.2    Colyer, J.3
  • 29
    • 0031922664 scopus 로고    scopus 로고
    • Cardiac myocyte calcium transport in phospholamban knockout mouse: Relaxation and endogenous CaMKII effects
    • Li L, Chu G, Kranias EG et al. 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
  • 30
    • 0034799606 scopus 로고    scopus 로고
    • Cardiac hypertrophy and failure: Lessons learned from genetically engineered mice
    • Takeishi Y, Walsh RA. Cardiac hypertrophy and failure: lessons learned from genetically engineered mice. Acta Physiol Scand 2001; 173: 103-111.
    • (2001) Acta Physiol Scand , vol.173 , pp. 103-111
    • Takeishi, Y.1    Walsh, R.A.2
  • 31
    • 0028172951 scopus 로고
    • Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase
    • Toyofuku T, Curotto Kurzydlowski K, Narayanan N et al. Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase. J Biol Chem 1994; 269: 26492-26496.
    • (1994) J Biol Chem , vol.269 , pp. 26492-26496
    • Toyofuku, T.1    Curotto Kurzydlowski, K.2    Narayanan, N.3
  • 32
    • 0030994868 scopus 로고    scopus 로고
    • Phosphorylation regulation of the Ca(2+)-pumping ATPase in cardiac sarcoplasmic reticulum by calcium/calmodulin-dependent protein kinase
    • Narayanan N, Xu A. Phosphorylation and regulation of the Ca(2+)-pumping ATPase in cardiac sarcoplasmic reticulum by calcium/calmodulin-dependent protein kinase. Basic Res Cardiol 1997; 92: 25-35.
    • (1997) Basic Res Cardiol , vol.92 , pp. 25-35
    • Narayanan, N.1    Xu, A.2
  • 33
    • 0034635438 scopus 로고    scopus 로고
    • Reversible inhibition of the calcium-pumping ATPase in native cardiac sarcoplasmic reticulum by a calmodulin-binding peptide. Evidence for calmodulin-dependent regulation of the V(max) of calcium transport
    • Xu A, Narayanan N. Reversible inhibition of the calcium-pumping ATPase in native cardiac sarcoplasmic reticulum by a calmodulin-binding peptide. Evidence for calmodulin-dependent regulation of the V(max) of calcium transport. J Biol Chem 2000; 275: 4407-4416.
    • (2000) J Biol Chem , vol.275 , pp. 4407-4416
    • Xu, A.1    Narayanan, N.2
  • 34
    • 0029666260 scopus 로고    scopus 로고
    • The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban
    • Odermatt A, Kurzydlowski K, Maclennan DH. The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban. J Biol Chem 1996; 271: 14206-14213.
    • (1996) J Biol Chem , vol.271 , pp. 14206-14213
    • Odermatt, A.1    Kurzydlowski, K.2    Maclennan, D.H.3
  • 35
    • 0034177180 scopus 로고    scopus 로고
    • Rate-dependent changes of twitch force duration in rat cardiac trabeculae: A property of the contractile system
    • Kassiri Z, Myers R, Kaprielian R et al. Rate-dependent changes of twitch force duration in rat cardiac trabeculae: a property of the contractile system. J Physiol 2000; 524: 221-231.
    • (2000) J Physiol , vol.524 , pp. 221-231
    • Kassiri, Z.1    Myers, R.2    Kaprielian, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.