메뉴 건너뛰기




Volumn 157, Issue 1-2, 1996, Pages 171-179

Protein phosphorylation in isolated trabeculae from nonfailing and failing human hearts

Author keywords

Force of contraction; Human heart; Phospholamban; Protein phosphorylation

Indexed keywords

BETA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; BUCLADESINE; CYCLIC AMP; ISOPRENALINE; PHOSPHODIESTERASE INHIBITOR; PHOSPHOLAMBAN; PHOSPHOPROTEIN; PIMOBENDAN; PROTEIN C; TROPONIN I;

EID: 0029968801     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00227896     Document Type: Article
Times cited : (65)

References (37)
  • 2
    • 85047677300 scopus 로고
    • Reduced positive inotropic effects in diseased human ventricularmyocardium
    • Brown L, Lorenz B, Erdmann E: Reduced positive inotropic effects in diseased human ventricularmyocardium. Cardiovasc Res 20: 516-520, 1986
    • (1986) Cardiovasc Res , vol.20 , pp. 516-520
    • Brown, L.1    Lorenz, B.2    Erdmann, E.3
  • 3
    • 0001618979 scopus 로고
    • Effect of α- and β-adrenergic agonists, phosphodiesterase inhibitors and adenosine on isolated human muscle preparations
    • Schmitz W, Scholz H, Erdmann E: Effect of α- and β-adrenergic agonists, phosphodiesterase inhibitors and adenosine on isolated human muscle preparations. Trend Pharmacol Sci 8: 447-450, 1987
    • (1987) Trend Pharmacol Sci , vol.8 , pp. 447-450
    • Schmitz, W.1    Scholz, H.2    Erdmann, E.3
  • 4
    • 0023130366 scopus 로고
    • Deficient production of cyclic AMP: Pharmacological evidence of an important cause of contractile dysfunction in patients with end-stage heart failure
    • Feldman MD, Capelas L, Gwathmey JK: Deficient production of cyclic AMP: pharmacological evidence of an important cause of contractile dysfunction in patients with end-stage heart failure. Circulation 75: 331-339, 1987
    • (1987) Circulation , vol.75 , pp. 331-339
    • Feldman, M.D.1    Capelas, L.2    Gwathmey, J.K.3
  • 6
    • 0025799802 scopus 로고
    • Mechanism underlying the reduced positive inotropic effects of the phosphodiesterase III inhibitors pimobendan, adibendan and saterinone in failing as compared to nonfailing human cardiac muscle preparations
    • von der Leyen H, Neumann J, Nose M, Schmitz W, Scholz H, Starbatty J, Stein B, Wenzlaff H, Doring V, Kalmar P, Haverich A: Mechanism underlying the reduced positive inotropic effects of the phosphodiesterase III inhibitors pimobendan, adibendan and saterinone in failing as compared to nonfailing human cardiac muscle preparations. Naunyn Schmiedeberg's Arch Pharmacol 344: 90-100, 1991
    • (1991) Naunyn Schmiedeberg's Arch Pharmacol , vol.344 , pp. 90-100
    • Von Der Leyen, H.1    Neumann, J.2    Nose, M.3    Schmitz, W.4    Scholz, H.5    Starbatty, J.6    Stein, B.7    Wenzlaff, H.8    Doring, V.9    Kalmar, P.10    Haverich, A.11
  • 8
    • 0025122012 scopus 로고
    • Abnormalities of diastolic function as a pontential cause of exercise intolerance in chronic heart failure
    • Packer M: Abnormalities of diastolic function as a pontential cause of exercise intolerance in chronic heart failure. Circulation 81 (Suppl III): 78-86, 1990
    • (1990) Circulation , vol.81 , Issue.3 SUPPL. , pp. 78-86
    • Packer, M.1
  • 10
    • 0024327222 scopus 로고
    • Altered expression of α-subunit of G proteins in failing human hearts
    • Feldman AM, Cates AE, Bristow MR, van Dop C: Altered expression of α-subunit of G proteins in failing human hearts. J Mol Cell Cardiol 21: 359-365, 1989
    • (1989) J Mol Cell Cardiol , vol.21 , pp. 359-365
    • Feldman, A.M.1    Cates, A.E.2    Bristow, M.R.3    Van Dop, C.4
  • 11
    • 0024389550 scopus 로고
    • Distribution of β-adrenergic receptors in failing human myocardium. Implications for mechanisms of down-regulation
    • Murphree SS, Jeffrey E, Saffitz MD: Distribution of β-adrenergic receptors in failing human myocardium. Implications for mechanisms of down-regulation. Circulation 79: 1214-1225, 1989
    • (1989) Circulation , vol.79 , pp. 1214-1225
    • Murphree, S.S.1    Jeffrey, E.2    Saffitz, M.D.3
  • 13
    • 0020015867 scopus 로고
    • Phosphorylation of the sarcoplasmic reticulum and sarcolemma
    • Tada M, Katz AM: Phosphorylation of the sarcoplasmic reticulum and sarcolemma. Annu Rev Physiol 44: 401-423, 1982
    • (1982) Annu Rev Physiol , vol.44 , pp. 401-423
    • Tada, M.1    Katz, A.M.2
  • 14
    • 27044447732 scopus 로고
    • Phosphorylation of cardiac muscle contractile proteins
    • A.J. Drake-Holland and M.I.M Noble (eds). John Wiley & Sons, New York, 1983
    • England PJ: Phosphorylation of cardiac muscle contractile proteins. In: A.J. Drake-Holland and M.I.M Noble (eds). Cardiac Metabolism. John Wiley & Sons, New York, 1983, pp 365-389, 1983
    • (1983) Cardiac Metabolism , pp. 365-389
    • England, P.J.1
  • 15
    • 0002060693 scopus 로고
    • Modulation of activation of cardiac myofilaments by beta-adrenergic agonists
    • J.A. Lee, D.G. Allen (eds). Oxford University Press
    • Solaro RJ: Modulation of activation of cardiac myofilaments by beta-adrenergic agonists. In: J.A. Lee, D.G. Allen (eds). Modulation of Cardiac Calcium. Oxford University Press, 1993, pp 160-177
    • (1993) Modulation of Cardiac Calcium , pp. 160-177
    • Solaro, R.J.1
  • 16
    • 0026542534 scopus 로고
    • Intracellular calcium handling in isolated venticular myocytes from patients with terminal heart failure
    • Beuckelmann DJ, Nabauer M, Erdmann E: Intracellular calcium handling in isolated venticular myocytes from patients with terminal heart failure. Circulation 85: 1045-10559, 1992
    • (1992) Circulation , vol.85 , pp. 1045-10559
    • Beuckelmann, D.J.1    Nabauer, M.2    Erdmann, E.3
  • 17
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang R, Zhao J, Mandveno A, Potter J D: Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ Res 76: 1028-1035, 1995
    • (1995) Circ Res , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 18
    • 0025052108 scopus 로고
    • Differential sensitivity to isoproterenol of phospholamban and troponin I phosphorlyation in isolated rat hearts
    • Karozewski P, Bartel S, Krause EG: Differential sensitivity to isoproterenol of phospholamban and troponin I phosphorlyation in isolated rat hearts. Biochem J 266: 115-122, 1990
    • (1990) Biochem J , vol.266 , pp. 115-122
    • Karozewski, P.1    Bartel, S.2    Krause, E.G.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685, 1970
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0027372328 scopus 로고
    • Phosphorylation of the L-type calcium channel β-subunit is involved in β-adrenergic signal transduction in canine myocardium
    • Haase H, Karczewski P, Beckert R, Krause EG: Phosphorylation of the L-type calcium channel β-subunit is involved in β-adrenergic signal transduction in canine myocardium. FEBS lett 335: 217-222, 1993
    • (1993) FEBS Lett , vol.335 , pp. 217-222
    • Haase, H.1    Karczewski, P.2    Beckert, R.3    Krause, E.G.4
  • 23
    • 0028940325 scopus 로고
    • Identification of soluble protein phosphatases that dephosphorylate voltage-sensitive sodium channels in rat brain
    • Chen TC, Law B, Kondratyuk T, Rossie S: Identification of soluble protein phosphatases that dephosphorylate voltage-sensitive sodium channels in rat brain. J Biol Chem 270(13): 7750-7756, 1995
    • (1995) J Biol Chem , vol.270 , Issue.13 , pp. 7750-7756
    • Chen, T.C.1    Law, B.2    Kondratyuk, T.3    Rossie, S.4
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon I: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci 76: 4350-4354, 1979
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, I.3
  • 26
    • 0028100606 scopus 로고
    • 2+-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium
    • 2+-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium. Circulation 90: 653-657, 1994
    • (1994) Circulation , vol.90 , pp. 653-657
    • Movsesian, M.A.1    Karimi, M.2    Green, K.3    Jones, L.R.4
  • 29
  • 32
    • 85047679474 scopus 로고
    • cAMP concentrations, cAMP-dependent protein kinase activity, and phospholamban in non-failing and failing myocardium
    • Bohm M, Reiger B, Schwinger RHG, Erdmann E: cAMP concentrations, cAMP-dependent protein kinase activity, and phospholamban in non-failing and failing myocardium. Cardiovasc Res 28: 1713-1719, 1994
    • (1994) Cardiovasc Res , vol.28 , pp. 1713-1719
    • Bohm, M.1    Reiger, B.2    Schwinger, R.H.G.3    Erdmann, E.4
  • 34
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo W, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG: Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ Res 75: 401-409, 1994
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 35
    • 0026360178 scopus 로고
    • 2+-sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers
    • 2+-sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers. J Gen Physiol 97: 1141-1163, 1991
    • (1991) J Gen Physiol , vol.97 , pp. 1141-1163
    • Hofmann, P.A.1    Hartzell, H.C.2    Moss, R.L.3
  • 36
    • 0025848016 scopus 로고
    • Purification and complete sequence determination of the major plasma membrane substrate for cAMP-dependent protein kinase and protein kinase C in myocardium
    • Palmer CJ, Scott BT, Jones LR: Purification and complete sequence determination of the major plasma membrane substrate for cAMP-dependent protein kinase and protein kinase C in myocardium. J Biol Chem 266: 11126-11130, 1991
    • (1991) J Biol Chem , vol.266 , pp. 11126-11130
    • Palmer, C.J.1    Scott, B.T.2    Jones, L.R.3
  • 37
    • 0026583919 scopus 로고
    • Phosphorylation of ryanodine receptors in rat myocytes during beta-adrenergic stimulation
    • Tokyo
    • Yoshida A, Takahasi M, Imagawa T, Shigekawa M, Takisawa H, Nakamura T: Phosphorylation of ryanodine receptors in rat myocytes during beta-adrenergic stimulation J Biochem (Tokyo) 111: 186-190, 1992
    • (1992) J Biochem , vol.111 , pp. 186-190
    • Yoshida, A.1    Takahasi, M.2    Imagawa, T.3    Shigekawa, M.4    Takisawa, H.5    Nakamura, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.