© 1996 American Heart Association, Inc.
Articles |
Phospholamban: A Prominent Regulator of Myocardial Contractility
the Department of Pharmacology & Cell Biophysics, University of Cincinnati (Ohio) College of Medicine.
Correspondence to Dr Evangelia G. Kranias, Department of Pharmacology & Cell Biophysics, University of Cincinnati College of Medicine, 231 Bethesda Ave, Cincinnati, OH 45267-0576.
Key Words: phospholamban • sarcoplasmic reticulum • cardiac contractility
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Regulation of Cardiac Sarcoplasmic Reticulum Ca2+ Uptake by Phospholamban |
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In the early 1970s, a discovery was reported by Arnold Katz (Tada et al1 ), who demonstrated that phosphorylation of isolated cardiac sarcoplasmic reticulum membranes occurred mainly on a low molecular weight protein. This phosphoprotein was named phospholamban, from the Greek root words meaning "to receive phosphate."1 Phospholamban is a small protein, comprising 52 amino acid residues, and it is present in cardiac, smooth, and slow-twitch skeletal muscles. However, its regulatory effects have been mainly studied in cardiac muscle. In vitro studies indicated that phospholamban can be phosphorylated at three distinct sites by various protein kinases: serine 10, by protein kinase C; serine 16, by cAMP- or cGMP-dependent protein kinase; and threonine 17, by Ca2+-calmodulin–dependent protein kinase.2 3 Each phosphorylation is associated with stimulation of the initial rates of cardiac sarcoplasmic reticulum Ca2+ uptake, which is mainly pronounced at low [Ca2+], resulting in an overall increase in the affinity of the Ca2+ pump for Ca2+.4 5 On the basis of these observations, it was initially hypothesized that phosphorylated phospholamban functions as a stimulator of the cardiac sarcoplasmic reticulum Ca2+-ATPase (SERCA2) enzyme. However, in the late 1980s, a significant breakthrough occurred demonstrating that dephosphorylated phospholamban is actually an inhibitor of cardiac sarcoplasmic reticulum Ca2+ transport for Ca2+ and that phosphorylation relieves this inhibitory effect, giving the appearance of phosphorylation-induced stimulation.6 This finding, together with the identification of a cardiac sarcoplasmic reticulum–associated protein phosphatase that can dephosphorylate phospholamban,7 has led to our current understanding of phospholamban as a reversible inhibitor
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M. Kuschel, Y.-Y. Zhou, H. Cheng, S.-J. Zhang, Y. Chen, E. G. Lakatta, and R.-P. Xiao Gi Protein-mediated Functional Compartmentalization of Cardiac beta 2-Adrenergic Signaling J. Biol. Chem., July 30, 1999; 274(31): 22048 - 22052. [Abstract] [Full Text] [PDF]
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P. Boknik, C. Unkel, U. Kirchhefer, U. Kleideiter, O. Klein-Wiele, J. Knapp, B. Linck, H. Luss, F. Ulrich Muller, W. Schmitz, et al. Regional expression of phospholamban in the human heart Cardiovasc Res, July 1, 1999; 43(1): 67 - 76. [Abstract] [Full Text] [PDF]
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V. J. Kadambi, N. Ball, E. G. Kranias, R. A. Walsh, and B. D. Hoit Modulation of force-frequency relation by phospholamban in genetically engineered mice Am J Physiol Heart Circ Physiol, June 1, 1999; 276(6): H2245 - H2250. [Abstract] [Full Text] [PDF]
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M. Kuschel, Y.-Y. Zhou, H. A. Spurgeon, S. Bartel, P. Karczewski, S.-J. Zhang, E.-G. Krause, E. G. Lakatta, and R.-P. Xiao ß2-Adrenergic cAMP Signaling Is Uncoupled From Phosphorylation of Cytoplasmic Proteins in Canine Heart Circulation, May 11, 1999; 99(18): 2458 - 2465. [Abstract] [Full Text] [PDF]
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K. H. Desai, E. Schauble, W. Luo, E. Kranias, and D. Bernstein Phospholamban deficiency does not compromise exercise capacity Am J Physiol Heart Circ Physiol, April 1, 1999; 276(4): H1172 - H1177. [Abstract] [Full Text] [PDF]
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M. Meyer, W. F. Bluhm, H. He, S. R. Post, F. J. Giordano, W. Y. W. Lew, and W. H. Dillmann Phospholamban-to-SERCA2 ratio controls the force-frequency relationship Am J Physiol Heart Circ Physiol, March 1, 1999; 276(3): H779 - H785. [Abstract] [Full Text] [PDF]
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 U. Vahlensieck, P. Bokník, I. Gombosová, S. Huke, J. Knapp, B. Linck, J. Neumann, M. C. Deng, H. H. Scheld, H. Jankowski, et al. Inotropic Effects of Diadenosine Tetraphosphate (AP4A) in Human and Animal Cardiac Preparations J. Pharmacol. Exp. Ther., February 1, 1999; 288(2): 805 - 813. [Abstract] [Full Text]
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E. Mirit, A. Palmon, Y. Hasin, and M. Horowitz Heat acclimation induces changes in cardiac mechanical performance: the role of thyroid hormone Am J Physiol Regulatory Integrative Comp Physiol, February 1, 1999; 276(2): R550 - R558. [Abstract] [Full Text] [PDF]
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A. Kaumann, S. Bartel, P. Molenaar, L. Sanders, K. Burrell, D. Vetter, P. Hempel, P. Karczewski, and E.-G. Krause Activation of ß2-Adrenergic Receptors Hastens Relaxation and Mediates Phosphorylation of Phospholamban, Troponin I, and C-Protein in Ventricular Myocardium From Patients With Terminal Heart Failure Circulation, January 12, 1999; 99(1): 65 - 72. [Abstract] [Full Text] [PDF]
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 H. Shiels, E. Freund, A. Farrell, and B. Block The sarcoplasmic reticulum plays a major role in isometric contraction in atrial muscle of yellowfin tuna J. Exp. Biol., January 4, 1999; 202(7): 881 - 890. [Abstract] [PDF]
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Y. Ji, E. Loukianov, T. Loukianova, L. R. Jones, and M. Periasamy SERCA1a can functionally substitute for SERCA2a in the heart Am J Physiol Heart Circ Physiol, January 1, 1999; 276(1): H89 - H97. [Abstract] [Full Text] [PDF]
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G. Chu, L. Li, Y. Sato, J. M. Harrer, V. J. Kadambi, B. D. Hoit, D. M. Bers, and E. G. Kranias Pentameric Assembly of Phospholamban Facilitates Inhibition of Cardiac Function in Vivo J. Biol. Chem., December 11, 1998; 273(50): 33674 - 33680. [Abstract] [Full Text] [PDF]
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Y. Sato, D. G. Ferguson, H. Sako, G. W. Dorn II, V. J. Kadambi, A. Yatani, B. D. Hoit, R. A. Walsh, and E. G. Kranias Cardiac-specific Overexpression of Mouse Cardiac Calsequestrin Is Associated with Depressed Cardiovascular Function and Hypertrophy in Transgenic Mice J. Biol. Chem., October 23, 1998; 273(43): 28470 - 28477. [Abstract] [Full Text] [PDF]
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H. K. B. SIMMERMAN and L. R. JONES Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function Physiol Rev, October 1, 1998; 78(4): 921 - 947. [Abstract] [Full Text] [PDF]
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Y. Pi and J. W. Walker Role of intracellular Ca2+ and pH in positive inotropic response of cardiomyocytes to diacylglycerol Am J Physiol Heart Circ Physiol, October 1, 1998; 275(4): H1473 - H1481. [Abstract] [Full Text] [PDF]
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E. Kiss, A. G. Brittsan, I. Edes, I. L. Grupp, G. Grupp, and E. G. Kranias Thyroid Hormone–Induced Alterations in Phospholamban-Deficient Mouse Hearts Circ. Res., September 21, 1998; 83(6): 608 - 613. [Abstract] [Full Text] [PDF]
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I. Gombosova, P. Boknik, U. Kirchhefer, J. Knapp, H. Luss, F. U. Muller, T. Muller, U. Vahlensieck, W. Schmitz, G. S. Bodor, et al. Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases Am J Physiol Heart Circ Physiol, June 1, 1998; 274(6): H2123 - H2132. [Abstract] [Full Text] [PDF]
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S. T Rapundalo Cardiac protein phosphorylation: functional and pathophysiological correlates Cardiovasc Res, June 1, 1998; 38(3): 559 - 588. [Abstract] [Full Text] [PDF]
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J. Huser, D. M. Bers, and L. A. Blatter Subcellular properties of [Ca2+]i transients in phospholamban-deficient mouse ventricular cells Am J Physiol Heart Circ Physiol, May 1, 1998; 274(5): H1800 - H1811. [Abstract] [Full Text] [PDF]
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R. J. Hajjar, U. Schmidt, T. Matsui, J. L. Guerrero, K.-H. Lee, J. K. Gwathmey, G. W. Dec, M. J. Semigran, and A. Rosenzweig Modulation of ventricular function through gene transfer in vivo PNAS, April 28, 1998; 95(9): 5251 - 5256. [Abstract] [Full Text] [PDF]
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R. M Phillips, P. Narayan, A. M Gomez, K. Dilly, L. R Jones, W.J. Lederer, and R. A Altschuld Sarcoplasmic reticulum in heart failure: central player or bystander? Cardiovasc Res, February 1, 1998; 37(2): 346 - 351. [Full Text] [PDF]
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H. Sako, S. A. Green, E. G. Kranias, and A. Yatani Modulation of cardiac Ca2+ channels by isoproterenol studied in transgenic mice with altered SR Ca2+ content Am J Physiol Cell Physiol, November 1, 1997; 273(5): C1666 - C1672. [Abstract] [Full Text] [PDF]
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J. James and J. Robbins Molecular remodeling of cardiac contractile function Am J Physiol Heart Circ Physiol, November 1, 1997; 273(5): H2105 - H2118. [Abstract] [Full Text] [PDF]
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G. Chu, G. W. Dorn II, W. Luo, J. M. Harrer, V. J. Kadambi, R. A. Walsh, and E. G. Kranias Monomeric Phospholamban Overexpression in Transgenic Mouse Hearts Circ. Res., October 19, 1997; 81(4): 485 - 492. [Abstract] [Full Text]
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R. J. Hajjar, U. Schmidt, J. X. Kang, T. Matsui, and A. Rosenzweig Adenoviral Gene Transfer of Phospholamban in Isolated Rat Cardiomyocytes : Rescue Effects by Concomitant Gene Transfer of Sarcoplasmic Reticulum Ca2+-ATPase Circ. Res., August 19, 1997; 81(2): 145 - 153. [Abstract] [Full Text]
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D. Hagemann, M. Kuschel, T. Kuramochi, W. Zhu, H. Cheng, and R.-P. Xiao Frequency-encoding Thr17 Phospholamban Phosphorylation Is Independent of Ser16 Phosphorylation in Cardiac Myocytes J. Biol. Chem., July 14, 2000; 275(29): 22532 - 22536. [Abstract] [Full Text] [PDF]
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G. Chu, J. W. Lester, K. B. Young, W. Luo, J. Zhai, and E. G. Kranias A Single Site (Ser16) Phosphorylation in Phospholamban Is Sufficient in Mediating Its Maximal Cardiac Responses to beta -Agonists J. Biol. Chem., December 1, 2000; 275(49): 38938 - 38943. [Abstract] [Full Text] [PDF]
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Y. Ji, M. J. Lalli, G. J. Babu, Y. Xu, D. L. Kirkpatrick, L. H. Liu, N. Chiamvimonvat, R. A. Walsh, G. E. Shull, and M. Periasamy Disruption of a Single Copy of the SERCA2 Gene Results in Altered Ca2+ Homeostasis and Cardiomyocyte Function J. Biol. Chem., November 22, 2000; 275(48): 38073 - 38080. [Abstract] [Full Text] [PDF]
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