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Volumn 276, Issue 5 45-5, 1999, Pages

Ser16 prevails over Thr17 phospholamban phosphorylation in the β- adrenergic regulation of ardiac relaxation

Author keywords

Adenosine 3',5' cyclic monophosphate dependent protein kinase; Calcium calmodulin dependent protein kinase; Cross signaling adenosine 3',5' cyclic monophosphate calcium; Intact rat heart; Relaxation

Indexed keywords

CALCIUM CHANNEL; ISOPRENALINE; NIFEDIPINE; PHOSPHOLAMBAN; RYANODINE; VERAPAMIL; ADENOSINE TRIPHOSPHATASE (CALCIUM); BETA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CALCIMYCIN; CALCIUM; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL L TYPE; CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN-DEPENDENT PROTEIN KINASE II; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; IONOPHORE; PROTEIN KINASE (CALCIUM,CALMODULIN); SERINE; THREONINE;

EID: 0033125604     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1999.276.5.h1625     Document Type: Article
Times cited : (68)

References (45)
  • 2
    • 0029085160 scopus 로고
    • The cardiac sarcoplasmic reticulum phospholamban kinase is a distinct δ-CaM kinase isozyme
    • Baltas, L., P. Karczewski, and E.-G. Krause. The cardiac sarcoplasmic reticulum phospholamban kinase is a distinct δ-CaM kinase isozyme. FEBS Lett. 373: 71-75, 1995.
    • (1995) FEBS Lett. , vol.373 , pp. 71-75
    • Baltas, L.1    Karczewski, P.2    Krause, E.-G.3
  • 3
    • 0028930629 scopus 로고
    • CaM kinase II is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes
    • Heart Circ. Physiol. 37
    • Bassani, R. A., A. Mattiazzi, and D. M. Bers. CaM kinase II is responsible for activity-dependent acceleration of relaxation in rat ventricular myocytes. Am. J. Physiol. 268 (Heart Circ. Physiol. 37): H703-H712, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Bassani, R.A.1    Mattiazzi, A.2    Bers, D.M.3
  • 4
    • 0019860734 scopus 로고
    • Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase
    • Bilezikjian, L. M., E. G. Kranias, J. D. Potter, and A. Schwartz. Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase. Circ. Res. 49: 1356-1362, 1981.
    • (1981) Circ. Res. , vol.49 , pp. 1356-1362
    • Bilezikjian, L.M.1    Kranias, E.G.2    Potter, J.D.3    Schwartz, A.4
  • 6
    • 0027967507 scopus 로고
    • Phosphorylation site-specific antibodies to cardiac phospholamban
    • Drago, G. A., and J. Colyer. Phosphorylation site-specific antibodies to cardiac phospholamban. J. Biol. Chem. 269: 25073-25077, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25073-25077
    • Drago, G.A.1    Colyer, J.2
  • 8
    • 0014854395 scopus 로고
    • A protein binding assay for adenosine 3′,5′-cyclic monophosphate
    • Gilman, A. G. A protein binding assay for adenosine 3′,5′-cyclic monophosphate. Proc. Natl. Acad. Sci. USA 67: 305-312, 1970.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 305-312
    • Gilman, A.G.1
  • 11
    • 33751260357 scopus 로고    scopus 로고
    • 2+ transient in rat hearts is independent of phospholamban phosphorylation
    • Heart Circ. Physiol. 42
    • 2+ transient in rat hearts is independent of phospholamban phosphorylation. Am. J. Physiol. 273 (Heart Circ. Physiol. 42): H695-H706, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Hussain, M.1    Drago, G.A.2    Colyer, J.3    Orchard, C.H.4
  • 13
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi, V. J., S. Ponniah, J. M. Harrer, B. D. Hoit, G. W. Dorn, R. A. Walsh, and E. G. Kranias. Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J. Clin. Invest. 97: 533-539, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 533-539
    • Kadambi, V.J.1    Ponniah, S.2    Harrer, J.M.3    Hoit, B.D.4    Dorn, G.W.5    Walsh, R.A.6    Kranias, E.G.7
  • 14
    • 0025052108 scopus 로고
    • Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts
    • Karczewski, P., S. Bartel, and E.-G. Krause. Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts. Biochem. J. 266: 115-122, 1990.
    • (1990) Biochem. J. , vol.266 , pp. 115-122
    • Karczewski, P.1    Bartel, S.2    Krause, E.-G.3
  • 16
    • 0030220713 scopus 로고    scopus 로고
    • Calcium channel diversity in the cardiovascular system
    • Katz, A. M. Calcium channel diversity in the cardiovascular system. J. Am. Coll. Cardiol. 8: 522-529, 1996.
    • (1996) J. Am. Coll. Cardiol. , vol.8 , pp. 522-529
    • Katz, A.M.1
  • 17
    • 0345282310 scopus 로고
    • Neural control of the heart: Sympathetic-vagal interactions
    • edited by J. Baan, A. Noodergraaf, and J. Raines. Cambridge, MA: MIT Press
    • Levy, M. N. Neural control of the heart: sympathetic-vagal interactions. In: Cardiovascular System Dynamics, edited by J. Baan, A. Noodergraaf, and J. Raines. Cambridge, MA: MIT Press, 1978, p. 365-370.
    • (1978) Cardiovascular System Dynamics , pp. 365-370
    • Levy, M.N.1
  • 18
    • 0031922664 scopus 로고    scopus 로고
    • Cardiac myocyte calcium transport in phospholamban knockout mouse: Relaxation and endogenous CaMK II effects
    • Heart Circ. Physiol. 43
    • Li, L., G. Chu, E. G. Kranias, and D. M. Bers. Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMK II effects. Am. J. Physiol. 274 (Heart Circ. Physiol. 43): H1335-H1347, 1998.
    • (1998) Am. J. Physiol. , vol.274
    • Li, L.1    Chu, G.2    Kranias, E.G.3    Bers, D.M.4
  • 21
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo, W., I. L. Grupp, J. M. Harrer, S. Ponniah, G. Grupp, J. J. Duffy, T. Doetschman, and E. G. Kranias. 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.M.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 22
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo, W., C. Guoxiang, Y. Sato, Z. Zhou, V. J. Kadambi, and E. G. Kranias. 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    Guoxiang, C.2    Sato, Y.3    Zhou, Z.4    Kadambi, V.J.5    Kranias, E.G.6
  • 23
    • 0344689769 scopus 로고    scopus 로고
    • Reintroduction of wild-type and mutant phospholamban into phospholamban-deficient hearts reverses enhanced contractility
    • Luo, W., Y. Sato, V. J. Kadambi, and E. G. Kranias. Reintroduction of wild-type and mutant phospholamban into phospholamban-deficient hearts reverses enhanced contractility (Abstract). Circulation 94, Suppl. I: 1087, 1996.
    • (1996) Circulation , vol.94 , Issue.SUPPL. I , pp. 1087
    • Luo, W.1    Sato, Y.2    Kadambi, V.J.3    Kranias, E.G.4
  • 24
    • 0016220001 scopus 로고
    • Simultaneous isolation of adenosine 3′,5′-cyclic monophosphate (cAMP) and guanosine 3′,5′-cyclic monophosphate (cGMP) in small tissue samples
    • Mao, C., and A. Guidotti. Simultaneous isolation of adenosine 3′,5′-cyclic monophosphate (cAMP) and guanosine 3′,5′-cyclic monophosphate (cGMP) in small tissue samples. Anal. Biochem. 59: 63-68, 1974.
    • (1974) Anal. Biochem. , vol.59 , pp. 63-68
    • Mao, C.1    Guidotti, A.2
  • 25
    • 0031001358 scopus 로고    scopus 로고
    • Phospholamban deficiency alters inactivation kinetics of L-type Ca channels in mouse ventricular myocytes
    • Heart Circ. Physiol. 41
    • Masaki, H., Y. Sato, W. Luo, E. G. Kranias, and A. Yatani. Phospholamban deficiency alters inactivation kinetics of L-type Ca channels in mouse ventricular myocytes. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H606-H612, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Masaki, H.1    Sato, Y.2    Luo, W.3    Kranias, E.G.4    Yatani, A.5
  • 26
  • 27
    • 0030479505 scopus 로고    scopus 로고
    • Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart
    • Mundiña, C., L. Vittone, M. Ortales, G. Chiappe de Cingolani, and A. Mattiazzi. Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart. J. Biol. Chem. 271: 33561-33567, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33561-33567
    • Mundiña, C.1    Vittone, L.2    Ortales, M.3    Chiappe De Cingolani, G.4    Mattiazzi, A.5
  • 28
    • 0343779934 scopus 로고
    • Protein kinase measurement of cAMP-dependent protein kinase ratio in hearts by use of a synthetic peptide
    • Murray, K. J., P. J. England, J. A. Lynham, D. Mills, and M. Reeves. Protein kinase measurement of cAMP-dependent protein kinase ratio in hearts by use of a synthetic peptide. Biochem. Soc. Trans. 16: 355-361, 1988.
    • (1988) Biochem. Soc. Trans. , vol.16 , pp. 355-361
    • Murray, K.J.1    England, P.J.2    Lynham, J.A.3    Mills, D.4    Reeves, M.5
  • 29
    • 0025791964 scopus 로고
    • Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart
    • Neumann, J., R. C. Gupta, W. Schmitz, H. Scholz, A. C. Nairn, and A. M. Watanabe. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circ. Res. 69: 1450-1457, 1991.
    • (1991) Circ. Res. , vol.69 , pp. 1450-1457
    • Neumann, J.1    Gupta, R.C.2    Schmitz, W.3    Scholz, H.4    Nairn, A.C.5    Watanabe, A.M.6
  • 30
    • 0024492885 scopus 로고
    • Inotropic responses to isoproterenol and phosphodiesterase inhibitors in intact guinea pig hearts: Comparison of cyclic AMP levels and phosphorylation of sarcoplasmic reticulum and myofibrillar proteins
    • Rapundalo, S. T., R. J. Solaro, and E. G. Kranias. Inotropic responses to isoproterenol and phosphodiesterase inhibitors in intact guinea pig hearts: comparison of cyclic AMP levels and phosphorylation of sarcoplasmic reticulum and myofibrillar proteins. Circ. Res. 64: 104-111, 1989.
    • (1989) Circ. Res. , vol.64 , pp. 104-111
    • Rapundalo, S.T.1    Solaro, R.J.2    Kranias, E.G.3
  • 33
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban: Identification of phosphorylation sites and two major structural domains
    • Simmerman, H. K. B., J. H. Collins, J. L. Theiber, A. D. Wegener, and L. R. Jones. Sequence analysis of phospholamban: identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261: 13333-13341, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13333-13341
    • Simmerman, H.K.B.1    Collins, J.H.2    Theiber, J.L.3    Wegener, A.D.4    Jones, L.R.5
  • 34
    • 0028789065 scopus 로고
    • Regulation of phospholamban and troponin-I phosphorylation in the intact rat cardiomyocytes by adrenergic and cholinergic stimuli: Roles of cyclic nucleotides, calcium, protein kinases and phosphatases and depolarization
    • Sulakhe, P. V., and T. X. Vo. Regulation of phospholamban and troponin-I phosphorylation in the intact rat cardiomyocytes by adrenergic and cholinergic stimuli: roles of cyclic nucleotides, calcium, protein kinases and phosphatases and depolarization. Mol. Cell. Biochem. 149-150: 103-126, 1995.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 103-126
    • Sulakhe, P.V.1    Vo, T.X.2
  • 35
    • 0018866614 scopus 로고
    • Ryanodine alterations of the contractile state of rat ventricular myocardium: Comparison with dog, cat, and rabbit ventricular tissues
    • Sutko, J. L., and J. T. Willerson. Ryanodine alterations of the contractile state of rat ventricular myocardium: comparison with dog, cat, and rabbit ventricular tissues. Circ. Res. 46: 332-343, 1980.
    • (1980) Circ. Res. , vol.46 , pp. 332-343
    • Sutko, J.L.1    Willerson, J.T.2
  • 36
    • 0015017308 scopus 로고
    • Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulphate
    • Swank, R. T., and K. D. Munkres. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulphate. Anal. Biochem. 39: 462-477, 1971
    • (1971) Anal. Biochem. , vol.39 , pp. 462-477
    • Swank, R.T.1    Munkres, K.D.2
  • 37
    • 0027480875 scopus 로고
    • Intracellular mechanisms mediating reversal of β-adrenergic stimulation in intact beating hearts
    • Heart Circ. Physiol. 33
    • Talosi, L., I. Edes, and E. G. Kranias. Intracellular mechanisms mediating reversal of β-adrenergic stimulation in intact beating hearts. Am. J. Physiol. 264 (Heart Circ. Physiol. 33): H791-H797, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Talosi, L.1    Edes, I.2    Kranias, E.G.3
  • 38
    • 0024840048 scopus 로고
    • Effect of ryanodine on neonatal and adult rat heart: Developmental increase in sarcoplasmic reticulum function
    • Tanaka, H., and K. Shigenobu. Effect of ryanodine on neonatal and adult rat heart: developmental increase in sarcoplasmic reticulum function. J. Mol. Cell. Cardiol. 21: 1305-1313, 1989.
    • (1989) J. Mol. Cell. Cardiol. , vol.21 , pp. 1305-1313
    • Tanaka, H.1    Shigenobu, K.2
  • 39
    • 0025273128 scopus 로고
    • Regulation of cardiac L-type calcium current by phosphorylation and G proteins
    • Trautwein, W., and J. Hescheler. Regulation of cardiac L-type calcium current by phosphorylation and G proteins. Annu. Rev. Physiol. 52: 257-274, 1990.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 257-274
    • Trautwein, W.1    Hescheler, J.2
  • 40
    • 0025348147 scopus 로고
    • cAMP and calcium-dependent mechanisms of phospholamban phosphorylation in intact hearts
    • Heart Circ. Physiol. 27
    • Vittone, L., C. Mundiña, G. Chiappe de Cingolani, and A. Mattiazzi. cAMP and calcium-dependent mechanisms of phospholamban phosphorylation in intact hearts. Am. J. Physiol. 258 (Heart Circ. Physiol. 27): H318-H325, 1990.
    • (1990) Am. J. Physiol. , vol.258
    • Vittone, L.1    Mundiña, C.2    Chiappe De Cingolani, G.3    Mattiazzi, A.4
  • 41
    • 0027320436 scopus 로고
    • Role of phospholamban phosphorylation on the relaxant effect of β-adrenergic agonists
    • Vittone, L. C., G. Mundiña, G. Chiappe de Cingolani, and A. Mattiazzi. Role of phospholamban phosphorylation on the relaxant effect of β-adrenergic agonists. Mol. Cell. Biochem. 124: 33-42, 1993.
    • (1993) Mol. Cell. Biochem. , vol.124 , pp. 33-42
    • Vittone, L.C.1    Mundiña, G.2    Chiappe De Cingolani, G.3    Mattiazzi, A.4
  • 42
    • 2642614533 scopus 로고    scopus 로고
    • Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart
    • Vittone, L. C., G. Mundiña-Weilenmann, M. Said, and A. Mattiazzi. Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart. J. Biol. Chem. 273: 9804-9811, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9804-9811
    • Vittone, L.C.1    Mundiña-Weilenmann, G.2    Said, M.3    Mattiazzi, A.4
  • 43
    • 0024360671 scopus 로고
    • Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation
    • Wegener, A. D., H. K. B. Simmermann, J. P. Lindemann, and L. R. Jones. Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation. J. Biol. Chem. 264: 11469-11474, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11469-11474
    • Wegener, A.D.1    Simmermann, H.K.B.2    Lindemann, J.P.3    Jones, L.R.4


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