Review: Regulation of Cardiac Sarcoplasmic Reticulum Function by Phospholamban

References

• Berman M. C., Aderem A. A. A calcium stat method for measurement of calcium transport in isolated sarcoplasmic reticulum vesicles. Anal. Biochem. 1981; 115: 297–301
   PubMedGoogle Scholar
• Bidlack J. M., Ambudkar I. S., Shamoo A. E. Purification of phospholamban, a 22,000-dalton protein from cardiac sarcoplasmic reticulum that is specifically phosphorylated by cyclic AMP-dependent protein kinase. J. Biol. Chem. 1982; 257: 4501–4506
   PubMedGoogle Scholar
• Bilezikjian L. M., Kranias E. G., Potter J. D., Schwartz A. Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase. Circ. Res. 1981; 49: 1356–1361
   PubMedGoogle Scholar
• Brandl C. J., Green N. M., Korczak B., MacLennan D. H. Two ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences. Cell 1986; 44: 597–607
   PubMedGoogle Scholar
• Brandl C. J., Deleon S., Martin D. R., MacLennan D. H. Adult forms of the Ca2+ ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle. J. Biol. Chem. 1987; 262: 3768–3774
   PubMed Web of Science ®Google Scholar
• Brum G, Osterreider W., Trautwein W. β-Adrenergic increase in the calcium conductance of cardiac myocytes studied with the patch clamp. Pflugers Arch. 1984; 401: 111–118
   PubMed Web of Science ®Google Scholar
• Carafoli E. M., Niggli V., Malmstrom K., Caroni P. Calmodulin in natural and reconstituted calcium transporting systems. Ann. N.Y. Acad. Sci. 1980; 356: 258–266
   PubMedGoogle Scholar
• Chamberlain B. K., Levitsky D. O., Fleischer S. Isolation and characterization of canine cardiac sarcoplasmic reticulum with improved Ca2+ transport properties. J. Biol. Chem. 1983; 258: 6602–6609
   PubMedGoogle Scholar
• Collins J. H., Kranias E. G., Reeves A. S., Bilezikjian L. M., Schwartz A. Isolation of phospholamban and a second proteolipid component from canine cardiac sarcoplasmic reticulum. Biochem. Biophys. Res. Commun. 1981; 99: 796–803
   PubMedGoogle Scholar
• Davis B. A., Schwartz A., Samaha F. J., Kranias E. G. Regulation of cardiac sarcoplasmic reticulum calcium transport by calcium-calmodulin-dependent phosphorylation. J. Biol. Chem. 1983; 258: 13, 587–13; 591
   Google Scholar
• Deadman J. R., Jackson R. L., Schreiber W. E., Means A. R. Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins. J. Biol. Chem. 1978; 253: 343–346
   PubMedGoogle Scholar
• Ferguson D. G., Young E. F., Kranias E. G. Immunogold localization of phospholamban-like polypeptide in canine vascular and visceral smooth muscle homogenates. Biophys. J. 1987; 51: 350a
   Google Scholar
• Fujii J, Ueno A., Kitano K., Tanaka S., Kadoma M., Tada M. Complete complementery DNA-derived amino acid sequence of canine cardiac phospholamban. J. Clin. Invest 1987; 79: 301–304
   PubMedGoogle Scholar
• Gupta R. C., Davis B. A., Kranias E. G. Mechanism of the stimulation of cardiac sarcoplasmic reticulum calcium pump by calmodulin. Membrane Biochem. 1988; 7: 73–86
   Google Scholar
• Harigaya S, Schwartz A. Rate of calcium binding and uptake in normal animal and failing human cardiac muscle. Circ. Res. 1969; 25: 781–794
   PubMed Web of Science ®Google Scholar
• Hasselbach W, Oetliker H. Energetics and electrogenicity of the sarcoplasmic reticulum calcium pump. Annu. Rev. Physiol. 1983; 45: 325–339
   PubMed Web of Science ®Google Scholar
• Hicks M. J., Shigekawa M., Katz A. M. Mechanism by which cyclic adenosine 3′:5′-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum. Circ. Res. 1979; 44: 384–391
   PubMedGoogle Scholar
• Inui M, Kadoma M., Tada M. Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum. J. Biol. Chem. 1985; 260: 3708–3715
   PubMedGoogle Scholar
• Inui M, Chamberlain B. K., Saito A., Fleischer S. The nature of the modulation of Ca2+ transport as studied by reconstitution of cardiac sarcoplasmic reticulum. J. Biol. Chem. 1986; 261: 1794–1800
   PubMedGoogle Scholar
• Jakab G, Kranias E. G. Phosphorylation and dephosphorylation of purified phospholamban and associated phosphatidylinositides. Biochemistry 1988; 27: 3799–3806
   PubMedGoogle Scholar
• Jones L. R., Besh H. R., Jr., Fleming J. W., McConnaughy M. M., Watanabe A. M. Separation of vesicles of cardiac sarcoplasmic reticulum. J. Biol. Chem. 1979; 254: 530–539
   PubMed Web of Science ®Google Scholar
• Jones L. R., Cala S. R. Biochemical evidence for functional heterogeneity of cardiac sarcoplasmic reticulum vesicles. J. Biol. Chem. 1981; 256: 11, 809–11; 818
   Google Scholar
• Jones L. R., Simmerman H. K.B., Wilson W. W., Gurd F. R.N., Wegener A. D. Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum. J. Biol. Chem. 1985; 260: 7721–7730
   PubMed Web of Science ®Google Scholar
• Katz A. M., Tada M., Kirchberger M. A. Control of calcium transport on the myocardium by cAMP-protein kinase system. Advances in Cyclic Nucleotide Research, G. I. Drummond. Raven Press, New York 1975; 5: 453–472
   Google Scholar
• Katz A. M. Role of the contractile proteins and sarcoplasmic reticulum in the response of the heart to catecholamines: An historical review. Advances in Cyclic Nucleotide Research, P. Greengard, G. A. Robison. Raven Press, New York. 1979; 11: 303–343
   Google Scholar
• Katz S, Remtulla M. A. Phosphodiesterase protein activator stimulates calcium transport in cardiac microsomal preparations enriched in sarcoplasmic reticulum. Biochem. Biophys. Res. Commun. 1978; 83: 1373–1379
   PubMedGoogle Scholar
• Kim H. W., Kim D. H., Ikemoto N., Kranias E. G. Lack of effects of calcium-calmodulin-dependent phosphorylation on Ca2+ release from cardiac sarcoplasmic reticulum. Biochim. Biophys. Acta 1987; 903: 333–340
   PubMedGoogle Scholar
• Kirchberger M. A., Tada M., Repke D. L., Katz A. Cyclic adenosine 3′,5′-monophosphate dependent protein kinase stimulation of the calcium uptake by canine cardiac microsomes. J. Mol. Cell. Cardiol. 1972; 4: 673–680
   PubMedGoogle Scholar
• Kirchberger M. A., Tada M., Katz A. Adenosine 3′:5′-monophosphate dependent protein kinase catalyzed phosphorylation reaction and its relationship to calcium transport in cardiac sarcoplasmic reticulum. J. Biol. Chem. 1974; 249: 6166–6173
   PubMed Web of Science ®Google Scholar
• Kirchberger M. A., Raffo A. Decrease in calcium transport associated with phosphoprotein phosphatase-catalyzed dephosphorylation of cardiac sarcoplasmic reticulum. J. Cyclic Nucl. Res. 1977; 3: 45–53
   PubMedGoogle Scholar
• Kirchberger M. A., Wong D. Calcium efflux from isolated cardiac sarcoplasmic reticulum. J. Biol. Chem. 1978; 253: 6941–6945
   PubMedGoogle Scholar
• Kirchberger M. A., Antonetz T. Calmodulin-mediated regulation of calcium transport and (Ca2+ + Mg2+)activated ATPase activity of isolated cardiac sarcoplasmic reticulum. J. Biol. Chem. 1982; 257: 15, 685–15; 691
   Google Scholar
• Kranias E. G., Bilezikjian L. M., Potter J. D., Piascik M. T., Schwartz A. Role of calmodulin in regulation of cardiac sarcoplasmic reticulum phosphorylation. Ann. N.Y. Acad. Sci. 1980; 356: 279–291
   PubMedGoogle Scholar
• Kranias E. G., Mandel F., Wang T., Schwartz A. Mechanism of the stimulation of calcium ion dependent adenosine triphosphatase of cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate dependent protein kinase. Biochemistry 1980; 19: 5434–5439
   PubMed Web of Science ®Google Scholar
• Kranias E. G., Schwartz A., Jungman R. A. Characterization of cyclic 3′:5′-AMP-dependent protein kinase in sarcoplasmic reticulum and cytosol of canine myocardium. Biochim. Biophys. Acta 1982; 709: 28–37
   PubMedGoogle Scholar
• Kranias E. G., Solaro R. J. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature 1982; 298: 182–184
   PubMed Web of Science ®Google Scholar
• Kranias E. G., Solaro R. J. Coordination of cardiac sarcoplasmic reticulum and myofibrillar function by protein phosphorylation. Fed. Proc. 1983; 42: 33–38
   PubMedGoogle Scholar
• Kranias E. G. Regulation of Ca2+ transport by cyclic 3′:5′-AMP-dependent and calcium-calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Biochim. Biophys. Acta 1985; 844: 193–199
   PubMedGoogle Scholar
• Kranias E. G. Regulation of calcium transport by protein phosphatase activity associated with cardiac sarcoplasmic reticulum. J. Biol. Chem. 1985; 260: 11, 006–11; 010
   Google Scholar
• Kranias E. G., Garvey J. L., Srivastava R. D., Solaro R. J. Phosphorylation and functional modifications of sarcoplasmic reticulum and myofibrils in isolated rabbit hearts stimulated with isoprenaline. Biochem. J. 1985; 226: 113–121
   PubMed Web of Science ®Google Scholar
• Kranias E. G., DiSalvo J. A phospholamban protein phosphatase activity associated with cardiac sarcoplasmic reticulum. J. Biol. Chem. 1986; 261: 10, 029–10; 032
   Google Scholar
• Kuo J. F., Anderson R. G.G., Wise R. C., Mackerlova K., Salomonsson I., Brackett N. L., Katoh N., Shoji M., Wrenn R. W. Calcium-dependent protein kinase: Widespread occurence in various tissues and phyla of the animal kingdom and comparison of the effects of phospholipid, calmodulin and trifluoperazine. Proc. Natl. Acad. Sci. USA 1980; 77: 7039–7043
   PubMedGoogle Scholar
• LaRaia P. J., Morkin E. Adenosine 3′,5′-monophosphate dependent membrane phosphorylation, a possible mechanism for the control of microsomal calcium transport in heart muscle. Circ. Res. 1974; 35: 298–306
   Google Scholar
• LePeuch C. J., Haiech J., Demaille J. G. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations. Biochemistry 1979; 18: 5150–5157
   PubMed Web of Science ®Google Scholar
• LePeuch C. J., LePeuch D. A.M., Demaille J. G. Phospholamban, activator of the cardiac sarcoplasmic reticulum pump. Physical properties and diagonal purification. Biochemistry 1980; 19: 3368–3373
   PubMedGoogle Scholar
• LePeuch C. J., Guilleux J. C., Demaille J. G. Phospholamban phosphorylation in the perfused rat heart is not solely dependent on β-adrenergic stimulation. FEBS Lett. 1980; 114: 165–168
   PubMedGoogle Scholar
• Levitsky D. O., Aliev M. K., Kuzmin A. V., Leuchenko T. S., Smirnov V. N., Chazov E. I. Isolation of calcium pump system and purification of calcium ion-dependent ATPase from heart muscle. Biochim. Biophys. Acta 1976; 443: 468–484
   PubMedGoogle Scholar
• Levitsky D. O., Benevolensky D. S., Levichenko T. S., Smirnov V. N., Chazov E. I. Calcium binding rate and capacity of cardiac sarcoplasmic reticulum. J. Mol. Cell. Cardiol. 1981; 13: 785–796
   PubMedGoogle Scholar
• Lighty G. W., Bertrand H. A. Cardiac sarcoplasmic reticulum isolation from slaughterhouse beef heart. Anal. Biochem. 1979; 99: 41–52
   PubMedGoogle Scholar
• Limas C. J. Phosphorylation of cardiac sarcoplasmic reticulum by a calcium-activated, phospholipid-dependent protein kinase. Biochem. Biophys. Res. Commun. 1980; 96: 1378–1383
   PubMedGoogle Scholar
• Lindemann J. P., Jones L. R., Hathaway D. R., Henry B. G., Watanabe A. M. β-Adrenergic stimulation of phospholamban phosphorylation and Ca2+-ATPase activity in guinea pig ventricles. J. Biol. Chem. 1983; 258: 464–471
   PubMed Web of Science ®Google Scholar
• Lindemann J. P., Watanabe A. M. Phosphorylation of phospholamban in intact myocardium. Role of Ca2+-calmodulin dependent mechanisms. J. Biol. Chem. 1985; 260: 4516–4525
   PubMedGoogle Scholar
• Lindemann J. P., Watanabe A. M. Muscarinic cholinergic inhibition of β-adrenergic stimulation of phospholamban phosphorylation and Ca2+ transport in guinea pig ventricles. J. Biol. Chem. 1985; 260: 13, 122–13; 129
   Google Scholar
• Lindemann J. P., Jones L. R. Sequential phospholamban (PLB) phosphorylation in intact hearts. Biophys. J. 1987; 51: 402a
   Google Scholar
• Lopaschuk G, Richter B., Katz S. Characterization of calmodulin effects on calcium transport in cardiac microsomes enriched in sarcoplasmic reticulum. Biochemistry 1980; 19: 5603–5607
   PubMedGoogle Scholar
• MacLennan D. H., Brandl C. J., Korczak B., Green N. M. Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 1985; 316: 696–700
   PubMed Web of Science ®Google Scholar
• Martonosi A, Feretos R. Sarcoplasmic reticulum III. Correlation between adenosine triphosphatase activity and Ca2+ uptake. J. Biol. Chem. 1964; 239: 659–668
   PubMedGoogle Scholar
• Miyakoda G, Yoshida A., Takisawa H., Nakamura T. β-Adrenergic regulation of contractility and protein phosphorylation in spontaneously beating isolated rat myocardial cells. J. Biochem. 1987; 102: 211–224
   PubMedGoogle Scholar
• Movsesian M. A., Nishikawa M., Adelstein R. S. Phosphorylation of phospholamban by calcium-activated, phospholipid-dependent protein kinase. J. Biol. Chem. 1984; 259: 8029–8032
   PubMedGoogle Scholar
• Osterreider W, Brum G., Heschler J., Trautwein W., Flockerzi V., Hofman F. Injection of subunits of cyclic AMP-dependent protein kinase into cardiac myocytes modulates Ca2+ current. Nature 1982; 298: 576–578
   PubMedGoogle Scholar
• Plank B, Wyskovsky W., Hellmann G., Suko J. Calmodulin-dependent elevation of calcium transport associated with calmodulin-dependent phosphorylation in cardiac sarcoplasmic reticulum. Biochim. Biophys. Acta 1983; 732: 99–109
   PubMedGoogle Scholar
• Plank B, Pifl C., Hellmann G., Wyskovsky W., Hoffman R., Suko J. Correlation between calmodulin-dependent increase in the rate of calcium transport and calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Eur. J. Biochem. 1983; 136: 215–221
   PubMedGoogle Scholar
• Rapundalo S. T., Solaro R. J., Kranias E. G. circ. Res., (In Press).
   Google Scholar
• Schwartz A, Entman M. L., Kanike K., Lane L. K., Van Winkle W. B., Bornet E. P. The rate of calcium uptake into sarcoplasmic reticulum of cardiac muscle and skeletal muscle. Effects of cyclic AMP-dependent protein kinase and phosphorylase b kinase. Biochim. Biophys. Acta 1976; 426: 57–72
   PubMed Web of Science ®Google Scholar
• Seiler S, Wegener A. D., Whang D. D., Hathaway D. R., Jones L. R. High molecular weight proteins in cardiac and skeletal junctional sarcoplasmic reticulum vesicles bind calmodulin, are phosphorylated, and are degraded by Ca2+-activated protease. J. Biol. Chem. 1984; 259: 8550–8557
   PubMed Web of Science ®Google Scholar
• Shamoo A. E., Ambudkar I. S. Regulation of calcium transport in cardiac cells. Can. J. Physiol. Pharmacol. 1983; 62: 9–22
   Google Scholar
• Shigekawa M, Finegan J. A.M., Katz A. M. Calcium transport ATPase of canine-cardiac sarcoplasmic reticulum: a comparison with that of rabbit fast skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 1976; 251: 6894–6900
   PubMedGoogle Scholar
• Simmerman H. K.B., Collins J. H., Theibert J. L., Wegener A. D., Jones L. R. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 1986; 261: 13, 333–13; 341
   PubMedGoogle Scholar
• Louis P.J. St., Sulakhe P. V. Phosphorylation of cardiac sarcolemma by endogenous and exogenous protein kinases. Arch. Biochem. Biophys. 1979; 198: 227–240
   PubMedGoogle Scholar
• Suko J, Hasselbach W. Characterization of cardiac sarcoplasmic reticulum ATP-ADP phosphate exchange and phosphorylation of the calcium transport adenosine triphosphatase. Eur. J. Biochem. 1976; 64: 123–130
   PubMedGoogle Scholar
• Sumida M, Wang T., Mandel F., Froehlich J. P., Schwartz A. Transient state kinetics of Ca2+-transport of sarcoplasmic reticulum. J. Biol. Chem. 1978; 253: 8772–8777
   PubMedGoogle Scholar
• Suzuki T, Wang J. H. Stimulation of bovine cardiac sarcoplasmic reticulum Ca2+ pump and blocking of phospholamban phosphorylation and dephosphorylation by a phospholamban monoclonal antibody. J. Biol. Chem. 1986; 261: 7018–7023
   PubMed Web of Science ®Google Scholar
• Suzuki T, Lui P., Wang J. H. The use of monoclonal antibodies for the species and tissue distribution of phospholamban. Cell Calcium 1986; 7: 41–47
   PubMedGoogle Scholar
• Suzuki T, Lui P., Wang J. H. Rapid purification of phospholamban by monoclonal antibody immunoaffinity chromatography. Biochem. Cell. Biol. 1987; 65: 302–309
   PubMedGoogle Scholar
• Tada M, Kirchberger M. A., Repke D. I., Katz A. M. The stimulation of calcium transport in cardiac sarcoplasmic reticulum by adenosine 3′,5′-monophosphate-dependent protein kinase. J. Biol. Chem. 1974; 249: 6194–6180
   Google Scholar
• Tada M, Kirchberger M. A., Katz A. M. Phosphorylation of a 22,000-dalton component of the sarcoplasmic reticulum by adenosine 3′,5′-monophosphate-dependent protein kinase. J. Biol. Chem. 1975; 250: 2640–2647
   PubMed Web of Science ®Google Scholar
• Tada M, Yamamoto T., Tonomura Y. Molecular mechanism of active calcium transport by sarcoplasmic reticulum. Physiol. Rev. 1978; 58: 1–79
   PubMed Web of Science ®Google Scholar
• Tada M, Yamada M., Ohmori F., Kuzuya T., Inui M., Abe H. Transient state kinetic studies of Ca2+-dependent ATPase and calcium transport by sarcoplasmic reticulum. J. Biol. Chem. 1980; 255: 1985–1992
   PubMedGoogle Scholar
• Tada M, Yamada M., Kadoma M., Inui M., Ohmori F. Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban. Mol. Cell Biochem. 1982; 46: 73–95
   PubMed Web of Science ®Google Scholar
• Tada M, Inui M., Yamada M., Kodoma M., Kuzuya T., Abe H., Kakiuchi S. Effects of phospholamban phosphorylation catalyzed by adenosine 3′:5′ monophosphate and calmodulin dependent protein kinases on calcium transport ATPase of cardiac sarcoplasmic reticulum. J. Mol. Cell. Cardiol. 1983; 15: 335–346
   PubMed Web of Science ®Google Scholar
• Takai Y, Kishimoto A., Iwasa Y., Kawahara Y., Mori T., Nishizuka Y. Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids. J. Biol. Chem. 1979; 254: 3692–3695
   PubMed Web of Science ®Google Scholar
• Watterson D. M., Sharief F., Vanaman T. C. The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J. Biol. Chem. 1980; 255: 962–975
   PubMed Web of Science ®Google Scholar
• Wegener A. D., Jones L. R. Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorytable subunits. J. Biol. Chem. 1984; 259: 1834–1841
   PubMedGoogle Scholar
• Wegener A. D., Simmerman H. K.B., Liepnieks J., Jones L. R. Proteolytic cleavage of phospholamban purified from canine cardiac sarcoplasmic reticulum vesicles. Generation of a low resolution model of phospholamban structure. J. Biol. Chem. 1986; 261: 5154–5159
   PubMedGoogle Scholar
• Wendt-Gallitelli M. F., Wolburg H., Schlote W., Schwegler M., Holnbarsch C., Jacob R. Prospect of x-ray microanalysis of myocardial contraction. Basic Res. Cardiol. 1980; 75: 66–72
   PubMedGoogle Scholar
• Will H, Blanck J., Smettan G., Wollenberger A. A quench-flow kinetic investigation of calcium ion accumulation by isolated cardiac sarcoplasmic reticulum. Dependence of initial velocity on free calcium concentration and influence of preincubation with a protein kinase, MgATP and cyclic AMP. Biochim. Biophys. Acta 1976; 449: 295–303
   PubMedGoogle Scholar
• Will H, Levchenko T. S., Levitsky D. O., Smirnov V. N., Wollenberger A. Partial characterization of protein kinase-catalyzed phosphorylation of low molecular weight proteins in purified preparations of pigeon heart sarcolemmea and sarcoplasmic reticulum. Biochim. Biophys. Acta 1978; 543: 175–193
   PubMedGoogle Scholar
• Wollenberger A. Cyclic nucleotides and the regulation of heart beat. Abstr. Fifth Int. Congr. Pharmacol. 1972; 231
   Google Scholar
• Wray H. L., Gray R. R., Olsson R. A. Cyclic adenosine 3′,5′-monophosphate-stimulated protein kinase and a substrate associated with sarcoplasmic reticulum. J. Biol. Chem. 1973; 248: 1496–1498
   PubMedGoogle Scholar
• Young E. F., Ferguson D. G., Kranias E. G. Immunogold localization of phospholamban in canine cardiac homogenates and microsomes. Biophys. J. 1987; 51: 350a
   Google Scholar