Cardiac protein phosphorylation: Functional and pathophysiological correlates

Cardiovascular Research

Volumn 38, Issue 3, 1998, Pages 559-588

  Rapundalo, Stephen T ^a  

^a PFIZER INC   (United States)

Author keywords

Dephosphorylation; Excitation contraction coupling; Phosphoproteins; Protein kinases; Protein phosphatases; Regulatory proteins

Indexed keywords

CALSEQUESTRIN; MUSCLE PROTEIN; MYOSIN LIGHT CHAIN; PHOSPHOLAMBAN; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PHOSPHORYLASE KINASE; POTASSIUM CHANNEL; PROTEIN C; PROTEIN KINASE C; RYANODINE RECEPTOR; TROPONIN I; TROPONIN T;

CARDIOMYOPATHY; EXCITATION CONTRACTION COUPLING; HEART CONTRACTION; HEART FAILURE; HEART HYPERTROPHY; HEART INFARCTION PREVENTION; HEART INNERVATION; HEART MUSCLE CONTRACTILITY; HEART MUSCLE FIBER MEMBRANE CONDUCTANCE; HEART MUSCLE ISCHEMIA; HEART MUSCLE METABOLISM; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; SODIUM CALCIUM EXCHANGE;

ANIMALS; CELLS, CULTURED; HEART DISEASES; HUMANS; MYOCARDIAL CONTRACTION; MYOCARDIUM; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN KINASES;

EID: 0032102779     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(98)00063-7     Document Type: Review

References (350)

1. [1] Kurosawa M. Phosphorylation and dephosphorylation of proteins in regulating cellular function. J Pharmacol Toxicol Methods 1994;31:135-139.
2. [2] Solaro RJ, editor. Protein Phosphorylation in Heart Muscle. Boca Raton, FL:CRC Press, 1986.
3. [3] Raju RVS, Kakkar R, Sharma RK. Biological significance of phosphorylation and myristoylation in the regulation of cardiac muscle proteins. Mol Cell Biochem 1997;176:135-143.
4. [4] Solaro RJ, Moir AJ, Perry SV. Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart. Nature 1976;262:615-617.
5. [5] Rapundalo ST, Solaro RJ, Kranias EG. 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 1989;64:104-111.
6. 2+-ATPaSe activity in guinea pig ventricles. J Biol Chem 1983;258:464-471.
7. [7] Kranias EG, Solaro RJ. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature 1982;298:182-184.
8. 2+-calmodulin-dependent mechanisms. J Biol Chem 1985;260:4516-4525.
9. 2+-calmodulin dependent phospholamban phosphorylation on the relaxant effect of beta-adrenergic agonists. Mol Cell Biochem 1993;124:33-42.
10. [10] Edes I, Talosi L, Kranias EG. The effect of alpha-adrenergic agents and protein kinase C activators on protein phosphorylation in isolated guinea pig hearts. Eur Heart J 1991;12:143-144.
11. [11] Talosi L, Kranias EG. Effect of alpha-adrenergic stimulation on activation of protein kinase C and phosphorylation of proteins in intact rabbit hearts. Circ Res 1992;70:670-678.
12. [12] Venema RC, Kuo JF. Protein kinase C-mediated phosphorylation of troponin I and C-protein in isolated myocardial cells is associated with inhibition of myofibrillar actomyosin MgATPase. J Biol Chem 1993;268:2705-2711.
13. [13] Huggins JP, Cook EA, Piggott JR, et al. Phospholamban is a good substrate for cyclic GMP-dependent protein kinase in vitro, but not in intact cardiac or smooth muscle. Biochem J 1989;260:829-835.
14. [14] Sabine B, Willenbrock R, Haase H, et al. Cyclic GMP-mediated phospholamban phosphorylation in intact cardiomyocytes. Biochem Biophys Res Commun 1995;214:75-80.
15. [15] Srivastava AK. Protein tyrosine phosphorylation in cardiovascular system. Mol Cell Biochem 1995;149/150:87-94.
16. [16] Foncea R, Andersson M, Ketterman A, et al. Insulin-like growth factor-I rapidly activates multiple signal transduction pathways in cultured rat cardiac myocytes. J Biol Chem 1997;272:19115-19124.
17. [17] Clerk A, Gillespie-Brown J, Fuller SJ, et al. Stimulation of phosphatidylinositol hydrolysis, protein kinase C translocation and mitogen-activated protein kinase activity by bradykinin in rat ventricular myocytes: dissociation from the hypertrophic response. Biochem J 1996;317:109-118.
18. [18] Clerk A, Sugden PH. Cell stress-induced phosphorylation of ATF2 and c-jun transcription factors in rat ventricular myocytes. Biochem J 1997;325:801-810.
19. [19] Hescheler J, Kameyama M, Trautwein W, et al. Regulation of the cardiac calcium channel by protein phosphatases. Eur J Biochem 1987;165:261-266.
20. [20] Ahmad Z, Green FJ, Subuhi HS, et al. Autonomic regulation of type 1 protein phosphatase in cardiac muscle. J Biol Chem 1989;264:3859-3863.
21. [21] Gupta RC, Neumann J, Watanabe AM. Comparison of adenosine and muscarinic receptor-mediated effects on protein phosphatase inhibitor-1 activity in the heart. J Pharmacol Exp Ther 1993;266:16-22.
22. [22] Barany K, Barany M, Giometti CS. Polyacrylamide gel electrophoretic methods in the separation of structural muscle proteins. J Chromatogr 1995;698:301-332.
23. [23] Presti CF, Scott BT, Jones LR. Identification of an endogeneous protein kinase C activity and its intrinsic 15-kilodalton substrate in purified canine cardiac sarcolemmal vesicles. J Biol Chem 1985;260:13879-13889.
24. [24] 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 1991;266:11126-11130.
25. [25] Lindemann JP. Alpha-adrenergic stimulation of sarcolemmal protein phosphorylation and slow responses in intact myocardium. J Biol Chem 1986;261:4860-4867.
26. [26] Presti CF, Jones LR, Lindemann JP. Isoproterenol-induced phosphorylation of a 15-kilodalton sarcolemmal protein in intact myocardium. J Biol Chem 1985;260:3860-3867.
27. [27] Sasaki Y, Yabana H, Nagao T, et al. Effect of denopamine on the phosphorylation of cardiac muscle proteins in the perfused guinea pig heart: comparison with isoproterenol. Biochem Pharmacol 1988;37:679-686.
28. [28] Talosi L, Edes I, Kranias EG. Intracellular mechanisms mediating reversal of beta-adrenergic stimulation in intact beating hearts. Am J Physiol 1993;264:H791-H797.
29. [29] Neumann J, Gupta RC, Jones LR, et al. Interaction of β-adrenoceptor and adenosine receptor agonists on phosphorylation: identification of target protein in mammalian ventricles. J Mol Cell Cardiol 1995;27:1655-1667.
30. [30] Hartmann M, Schrader J. Protein kinase C phosphorylates a 15 kDa protein but not phospholamban in intact rat cardiac myocytes. Eur J Pharmacol 1992;226:225-231.
31. [31] Edes I, Talosi L, Kranias EG. Effect of alpha adrenergic agents and phorbol esters on phosphorylation of sarcolemmal proteins in beating guinea pig hearts. Cardiovasc Res 1991;25:510-515.
32. [32] Moorman JR, Palmer CJ, John JEI, et al. Phospholemman expression induces a hyperpolarization-activated chloride current in Xenopus oocytes. J Biol Chem 1992;267:14551-14554.
33. - channels. Nature 1993;365:850-852.
34. [34] Condrescu M, Gardner JP, Chernaya G, et al. ATP-dependent regulation of sodium-calcium exchange in Chinese hamster ovary cells transfected with the bovine cardiac sodium-calcium exchanger. J Biol Chem 1995;270:9137-9146.
35. 2+ exchanger via protein kinase C. J Biol Chem 1996;271:13609-13615.
36. [36] Sperelakis N, Tohse N, Ohya Y. Regulation of calcium slow channels in cardiac muscle and vascular smooth muscle cells. Adv Exp Med Biol 1992;311:163-187.
37. [37] Sperelakis N, Xiong Z, Haddad G, et al. Regulation of slow calcium channels of myocardial cells and vascular smooth muscle cells by cyclic nucleotides and phosphorylation. Mol Cell Biochem 1994;140:103-117.
38. 2+ influx in myocardial cells by beta adrenergic receptors, cyclic nucleotides and phosphorylation. Mol Cell Biochem 1988;82:19-28.
39. [39] Trautwein W, Cavalie A, Flockerzi V, et al. Modulation of calcium channel function by phosphorylation in guinea pig ventricular cells and phospholipid bilayer membranes. Circ Res 1987;61:I17-23.
40. 2+ current. Nature 1982;298:576-578.
41. [41] Haddad G, Sperelakis N, Bkaily G. Regulation of calcium slow channels in myocardial cells by cyclic nucleotides and phosphorylation. Mol Cell Biochem 1995;148:89-94.
42. [42] Bkaily G, Sperelakis N. Injection of protein kinase inhibitor into cultured heart cells blocks calcium slow channels. Am J Physiol 1984;246:H630-H634.
43. [43] Reuter H. Calcium channel modulation by neurotransmitters, enzymes and drugs. Nature 1983;301:569-574.
44. [44] Haase H, Karczewski P, Beckert R, et al. Phosphorylation of the L-type calcium channel β subunit is involved in β-adrenergic signal transduction in canine myocardium. FEBS Lett 1993;335:217-222.
45. [45] Haase H, Bartel S, Karczewski P, et al. In-vivo phosphorylation of the cardiac L-type calcium channel beta-subunit in response to catecholamines. Mol Cell Biochem 1996; 163/164:99-106.
46. [46] Yoshida A, Takahashi M, Nishimura S, et al. Cyclic AMP-dependent phosphorylation and regulation of the cardiac dihydropyridine-sensitive Ca channel. FEBS Lett 1992;309:343-349.
47. 1 subunit. J Biochem 1996;120.
48. [48] Freer RJ, Pappano AJ, Peach MJ, et al. Mechanism of the positive inotropic effect of angiotensin II on isolated cardiac muscle. Circ Res 1976;39:178-183.
49. [49] Dosemeci A, Dhallan RS, Cohen NM, et al. Phorbol ester increases calcium current and simulates the effects of angiotensin II on cultured neonatal rat heart myocytes. Circ Res 1988;62:347-357.
50. [50] Tohse N, Kameyama M, Sekiguchi K, et al. Protein kinase C activation enhances the delayed rectifier potassium current in guinea pig heart cells. J Mol Cell Cardiol 1990;22:725-734.
51. [51] Bkaily G, Sperelakis N. Calmodulin is required for a full activation of the calcium slow channels in heart cells. J Cycl Nucleot Prot Phosph Res 1986;11:25-34.
52. [52] Tohse N, Sperelakis N. cGMP inhibits the activity of single calcium channels in embryonic chick heart cells. Circ Res 1991;69:325-331.
53. 2+ current in rat ventricular myocytes. Circ Res 1995;77:803-812.
54. [54] Cuppoletti J, Thakkar J, Sperelakis N, et al. Cardiac sarcolemmal substrate of the cGMP-dependent protein kinase. Membr Biochem 1987;7:135-142.
55. [55] Kameyama M, Hescheler J, Hofmann F, et al. Modulation of Ca current during the phosphorylation cycle in the guinea pig heart. Pflug Arch 1986;407:123-128.
56. [56] Hescheler J, Mieskes G, Ruegg JC, et al. Effects of a protein phosphatase inhibitor, okadaic acid, on membrane currents of isolated guinea pig cardiac myocytes. Pflug Arch 1988;412:248-252.
57. - currents in guinea pig ventricular myocytes. J Pharmacol Exp Ther 1997;52:725-734.
58. 2+ channels. Pflug Arch 1995;429:531-538.
59. [59] Huang XY, Morielli AD, Peralta EG. Molecular basis of cardiac potassium channel stimulation by protein kinase A. Proc Natl Acad Sci USA 1994;91:624-628.
60. [60] Hartzell HC, Simmons MA. Comparison of effects of acetylcholine on calcium and potassium currents in frog atria and ventricle. J Physiol (London) 1987;389:411-422.
61. [61] Koumi S, Backer CL, Arentzen CE, et al. β-Adrenergic modulation of the inwardly rectifying potassium channel in isolated human ventricular myocytes. J Clin Invest 1995;96:2870-2881.
62. + channel-opening drugs. Am J Physiol 1995;269:C525-C545.
63. [63] Light P. Regulation of ATP-sensitive potassium channels by phosphorylation. Biochim Biophys Acta 1996;1286:65-73.
64. + channels toward intracellular nucleoside diphosphates. Neuron 1994;12:1049-1058.
65. [65] Kwak YG, Park SK, Cho KP, et al. Reciprocal modulation of ATP-sensitive K+ channel activity in rat ventricular myocytes by phosphorylation of tyrosine and serine/threonine residues. Life Sci 1996;58:897-904.
66. [66] Light PE, Allen BG, Walsh MP, et al. Regulation of adenosine triphosphate-sensitive potassium channels from rabbit ventricular myocytes by protein kinase C and type 2A protein phosphatase. Biochemistry 1995;34:7252-7257.
67. + channels. A possible mechanistic link to ischemic preconditioning. Circ Res 1996;79:399-406.
68. [68] Bahinski A, Nairn AC, Greengard P, et al. Chloride conductance regulated by cyclic AMP-dependent protein kinase in cardiac myocytes. Nature 1989;340:718-721.
69. [69] Hwang TC, Horie M, Nairn AC, et al. Role of GTP-binding proteins in the regulation of mammalian cardiac chloride conductance. J Gen Physiol 1992;99:465-489.
70. - conductance in mammalian heart. J Gen Physiol 1993;101:629-650.
71. - currents in feline ventricular myocytes. Circ Res 1994;75:133-143.
72. [72] Kwak BR, Jongsma HJ. Regulation of cardiac gap junction channel permeability and conductance by several phosphorylating conditions. Mol Cell Biochem 1996;157:93-99.
73. [73] Takens-Kwak BR, Jongsma HJ. Cardiac gap junctions: three distinct single channel conductances and their modulation by phosphorylating treatments. Pflug Arch 1992;422:198-200.
74. [74] Moreno AP, Saez JC, Fishman GI, et al. Human connexin43 gap junction channels. Regulation of unitary conductances by phosphorylation. Circ Res 1994;74:1050-1057.
75. [75] Laing JG, Westphale EM, Engelmann GL, et al. Characterization of the gap junction protein, connexin45. J Membr Biol 1994;139:31-40.
76. [76] Darrow BJ, Fast VG, Kleber AG, et al. Functional and structural assessment of intercellular communication. Increased conduction velocity and enhanced connexin expression in dibutyryl cAMP-treated cultured cardiac myocytes. Circ Res 1996;79:174-183.
77. [77] Laird DW, Puranam KL, Revel JP. Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes. Biochem J 1991;273:67-72.
78. [78] Beyer EC, Goodenough DA. Connexin family of gap junction proteins. J Membr Biol 1990;116:187-194.
79. [79] Lefkowitz RJ, Caron MG. Regulation of adrenergic receptor function by phosphorylation. Curr Top Cell Regul 1986;28:209-231.
80. [80] Hosey MM, Kwatra MM, Ptasienski J, et al. Regulation of receptor function by protein phosphorylation. Ann NY Acad Sci 1990;588:155-163.
81. [81] Premont RT, Inglese J, Lefkowitz RJ. Protein kinases that phosphorylate activated G protein-coupled receptors. FASEB J 1995;9:175-182.
82. [82] Palczewski K. GTP-binding-protein-coupled receptor kinases. Eur J Biochem 1997;248:261-269.
83. [83] Lefkowitz R. G-protein coupled receptor kinases. Cell 1993;74:409-412.
84. [84] Inglese J, Freedman NJ, Koch WJ, et al. Structure and mechanism of the G protein-coupled receptor kinases. J Biol Chem 1993;268:23735-23738.
85. [85] Lefkowitz RJ, Cotecchia S, Kjelsberg MA, et al. Adrenergic receptors: recent insights into their mechanism of activation and desensitization. Adv Sec Mess Phosphoprot Res 1993;28:1-9.
86. [86] Lohse M. Molecular mechanisms of membrane receptor desensitization. Biochim Biophys Acta 1993;1179:171-188.
87. [87] Iino M, Furugohri T, Fukuzawa A, et al. Asp278 of human β-adrenergic receptor kinase 1 is essential for phosphorylation activity. Biochem Biophys Res Comm 1997;239:548-551.
88. [88] Sibley DR, Benovic JL, Caron MG, et al. Regulation of transmembrane signaling by receptor phosphorylation. Cell 1987;48:913-922.
89. 2-adrenergic receptor. J Biol Chem 1996;271:13796-13803.
90. 1B-adrenergic receptor. J Biol Chem 1997;272:28712-28719.
91. [91] Lohse M. G-protein-coupled receptor kinases and the heart. Trends Cardiovasc Med 1995;5:63-68.
92. [92] Kwatra MM, Hosey MM. Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist. J Biol Chem 1986;261:12429-12432.
93. [93] Kwatra MM, Leung E, Maan AC, et al. Correlation of agonist-induced phosphorylation of chick heart muscarinic receptors with receptor desensitization. J Biol Chem 1987;262:16314-16321.
94. 2 muscarinic receptor: agonist-induced phosphorylation and comparison of properties with the chick heart receptor. Mol Pharmacol 1989;35:553-558.
95. [95] Kwatra MM, Benovic JL, Caron MG, et al. Phosphorylation of chick heart muscarinic cholinergic receptors by the beta-adrenergic receptor kinase. Biochemistry 1989;28:4543-4547.
96. [96] Haga K, Haga T. Agonist-dependent phosphorylation of cerebral and atrial muscarinic receptors: blockade of the phosphorylation of GTP-binding regulatory proteins and its reversal by guanine nucleotides. Biomed Res 1989;10:293-299.
97. [97] Grover AK, Khan I. Calcium pump isoforms: diversity, selectivity and plasticity. Cell Calcium 1992;73:9-17.
98. [98] Kadambi VJ, Kranias EG. Phospholamban: a protein coming of age. Biochem Biophys Res Comm 1997;239:1-5.
99. 2+ release channel. J Biol Chem 1993;268:13765-13768.
100. 2+ release channels and their regulation by endogenous effectors. Annu Rev Physiol 1994;56:485-508.
101. [101] Campbell KP, MacLennan DH, Jorgensen AO, et al. Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53000 dalton glycoprotein. J Biol Chem 1983;258:1197-1204.
102. [102] Koss KL, Kranias EG. Phospholamban: a prominent regulator of myocardial contractility. Circ Res 1996;79:1059-1063.
103. [103] Luo W, Grupp IL, Harrer J, et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ Res 1994;75.
104. [104] Arkin IT, Adams PD, Brunger AT, et al. Structural perspectives of phospholamban, a helical transmembrane pentamer. Annu Rev Biophys Biomol Struct 1997;26:157-179.
105. 2+-ATPases. J Biol Chem 1997;272:28815-28818.
106. [106] Fujii J, Ueno A, Kitano K, et al. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. J Clin Invest 1987;79:301-304.
107. [107] Harrer JM, Kranias EG. Characterization of the molecular form of cardiac phospholamban. Mol Cell Biochem 1994;140:185-193.
108. [108] Wegener AD, Jones LR. Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits. J Biol Chem 1984;259:1834-1841.
109. [109] Simmerman HK, Collins JH, Theibert JL, et al. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J Biol Chem 1986;261:13333-13341.
110. 2+ pump of sarcoplasmic reticulum. Nature 1989;342:90-92.
111. [111] Cornea RL, Jones LR, Autry JM, et al. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 1997;36:2960-2967.
112. 2+-selective channels in lipid bilayers. J Biol Chem 1988;263:18364-18368.
113. [113] Cook EA, Huggins JP, Sathe G, et al. The expression of canine cardiac phospholamban in heterologous systems. Biochem J 1988;264:533-538.
114. [114] Fujii J, Maruyama K, Tada M, et al. Expression and site-specific mutagenesis of phospholamban. Studies of residues involved in phosphorylation and pentamer formation. J Biol Chem 1989;264:12950-12955.
115. [115] Watanabe Y, Kijima Y, Kadoma M, et al. Molecular weight determination of phospholamban oligomer in the presence of sodium dodecyl sulfate: application of low-angle laser light scattering photometry. J Biochem 1991;110:40-45.
116. [116] Adams PD, Arkin IT, Engelman DM, et al. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Struct Biol 1995;2:154-162.
117. [117] Kirchberger MA, Borchman D, Kasinathan C. Proteolytic activation of the canine cardiac sarcoplasmic reticulum calcium pump. Biochemistry 1986;25:5484-5492.
118. [118] Huggins JP, England PJ. Evidence for a phosphorylation-induced conformational change in phospholamban from the effects of three proteases. FEBS Lett 1987;217:32-36.
119. [119] Huggins JP, England PJ. Phosphorylation protects membrane-bound phospholamban from the effects of proteases. Biochem Soc Trans 1987;15:685.
120. [120] Simmerman HK, Lovelace DE, Jones LR. Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligomeric protein of cardiac sarcoplasmic reticulum. Biochim Biophys Acta 1989;997:322-329.
121. 2+)-ATPase: mechanism of regulation and site of monoclonal antibody interaction. J Biol Chem 1991;266:11270-11275.
122. [122] Colyer J, Wang JH. Dependence of cardiac sarcoplasmic reticulum calcium pump activity on the phosphorylation status of phospholamban. J Biol Chem 1991;266:17486-17493.
123. [123] Negash S, Chen LT, Bigelow DJ, et al. Phosphorylation of phospholamban by cAMP-dependent protein kinase enhances interactions between Ca-ATPase polypeptide chains in sarcoplasmic reticulum membranes. Biochemistry 1996;35:11247-11259.
124. [124] Tada M, Kirchberger MA. Regulation of calcium transport by cyclic AMP. A proposed mechanism for the beta-adrenergic control of myocardial contractility. Acta Cardiol 1975;30:231-237.
125. 2+ transport by cyclic 3′,5′-AMP-dependent and calcium-calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Biochim Biophys Acta 1985;844:193-199.
126. [126] Le Peuch CJ, Haiech J, Demaille JG. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations. Biochemistry 1979;18:5150-5157.
127. [127] Davis BA, Schwartz A, Samaha FJ, et al. Regulation of cardiac sarcoplasmic reticulum calcium transport by calcium-calmodulin-dependent phosphorylation. J Biol Chem 1983;258:13587-13591.
128. [128] Movsesian MA, Nishikawa M, Adelstein RS. Phosphorylation of phospholamban by calcium-activated, phospholipid-dependent protein kinase. Stimulation of cardiac sarcoplasmic reticulum calcium uptake. J Biol Chem 1984;259:8029-8032.
129. [129] Edes I, Kranias EG. Phospholamban and troponin I are substrates for protein kinase C in vitro but not in intact beating guinea pig hearts. Circ Res 1990;67:394-400.
130. [130] Raeymaekers L, Hofmann F, Casteels R. Cyclic GMP-dependent protein kinase phosphorylates phospholamban in isolated sarcoplasmic reticulum from cardiac and smooth muscle. Biochem J 1988;252:269-273.
131. [131] Maslennikov IV, Sobol AG, Anagli J, et al. The secondary structure of phospholamban: a two-dimensional NMR study. Biochem Biophys Res Commun 1995;217:1200-1207.
132. [132] Quirk PG, Patchell VB, Colyer J, et al. Conformational effects of serine phosphorylation in phospholamban peptides. Eur J Biochem 1996;236:85-91.
133. 2+-pump stimulation. Biochem J 1996;316:201-207.
134. [134] Kirchberger MA, Tada M, Katz AM. 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.
135. [135] La Raia PJ, Morkin E. Phosphorylation-dephosphorylation of cardiac microsomes: a possible mechanism for control of calcium uptake by cyclic AMP. Recent Adv Stud Cardiac Struct Metab 1974;4:417-426.
136. [136] Tada M, Kirchberger MA, Katz AM. Phosphorylation of a 22000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase. J Biol Chem 1975;250:2640-2647.
137. [137] Kranias EG, Mandel F, Wang T, et al. 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.
138. 2+-dependent ATPase and calcium transport by cardiac sarcoplasmic reticulum. Effect of cyclic AMP-dependent protein kinase-catalyzed phosphorylation of phospholamban. J Biol Chem 1980;255:1985-1992.
139. 2+-dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3′5′-monophosphate-dependent protein kinase: role of the 22000 dalton protein. J Biol Chem 1979;254:319-326.
140. 2+ binding sites of cardiac sarcoplasmic reticulum. J Bioenerg Biomembr 1983;15:179-194.
141. [141] Antipenko AY, Spielman AL, Sassaroli M, et al. Comparison of the kinetic effects of phospholamban phosphorylation and anti-phospholamban monoclonal antibody on the calcium pump in purified cardiac sarcoplasmic reticulum membranes. Biochemistry 1997;36:12903-12910.
142. [142] Katz AM, Tada M, Kirchberger MA. Control of calcium transport in the myocardium by the cyclic AMP-Protein kinase system. Adv Cycl Nucleot Res 1975;5:453-472.
143. [143] Kirchberger MA, Wong D. Calcium efflux from isolated cardiac sarcoplasmic reticulum. J Biol Chem 1978;253:6941-6945.
144. [144] Edes I, Solaro RJ, Kranias EG. Changes in phosphoinositide turnover in isolated guinea pig hearts stimulated with isoproterenol. Circ Res 1989;65:989-996.
145. [145] Garvey JL, Kranias EG, Solaro RJ. Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. Biochem J 1988;249:709-714.
146. [146] Jakab G, Rapundalo ST, Solaro RJ, et al. Phosphorylation of phospholipids in isolated guinea pig hearts stimulated with isoprenaline. Biochem J 1988;251:189-194.
147. [147] Kranias EG, Garvey JL, Srivastava RD, et al. Phosphorylation and functional modifications of sarcoplasmic reticulum and myofibrils in isolated rabbit hearts stimulated with isoprenaline. Biochem J 1985;226:113-121.
148. [148] Kiss E, Edes I, Sato Y, et al. β-adrenergic regulation of cAMP and protein phosphoylation in phospholamban-knockout mouse hearts. Am J Physiol 1997;272:H785-H790.
149. [149] Neumann J, Gupta RC, Schmitz W, et al. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circ Res 1991;69:1450-1457.
150. [150] Watanabe AM, Lindemann JP, Fleming JW. Mechanisms of muscarinic modulation of protein phosphorylation in intact ventricles. Fed Proc 1984;43:2618-2623.
151. [151] England PJ, Shahid M. Effects of forskolin on contractile responses and protein phosphorylation in the isolated perfused rat heart. Biochem J 1987;246:687-695.
152. [152] Reeves ML, England PJ, Murray KJ. Increased protein phosphorylation in guinea pig hearts perfused with a selective phosphodiesterase inhibitor. Biochem Soc Trans 1989;17:169-170.
153. [153] Murray KJ, Reeves ML, England PJ. Protein phosphorylation and compartments of cyclic AMP in the control of cardiac contraction. Mol Cell Biochem 1989;89:175-179.
154. [154] Neumann J, Boknik P, Schmitz W, et al. Comparison of the stereoselective effects of a thiadiazinone derivative on contractile parameters and protein phosphorylation in the mammalian ventricle. J Cardiovasc Pharmacol 1995;25:789-793.
155. [155] Miyakoda G, Yoshida A, Takisawa H, et al. Beta-adrenergic regulation of contractility and protein phosphorylation in spontaneously beating isolated rat myocardial cells. J Biochem Tokyo 1987;102:211-224.
156. [156] Sulakhe PV, Vo XT. Regulation of phospholamban and troponin-I phosphorylation in the intacl rat cardiomyocytes by adrenergic and cholinergic stimuli: roles of cyclic nucleotides, calcium, protein kinases and phosphatases and depolarization. Mol Cell Biochem 1995;149/150:103-126.
157. 2+ dynamics, contractility, or phospholamban phosphorylation. J Biol Chem 1994;269:19151-19156.
158. 2-adrenoceplor activation by zinterol causes protein phosphorylation, contractile effects and relaxant effects through a cAMP pathway in human atrium. Mol Cell Biochem 1996;163/164:113-123.
159. 2+ sensitivity of cardiac myofibrils and sarcoplasmic reticulum in guinea pig heart. Circ Res 1995;77:107-113.
160. [160] Iwasa Y, Hosey MM. Cholinergic antagonism of beta-adrenergic stimulation of cardiac membrane protein phosphorylation in situ. J Biol Chem 1983;258:4571-4575.
161. 2+ transport in guinea pig ventricles. J Biol Chem 1985;260:13122-13129.
162. [162] Neumann J, Boknik P, Bodor GS, et al. Effects of adenosine receptor and muscarinic cholinergic receptor agonists on cardiac protein phosphorylation. Influence of pertussis toxin. J Pharmacol Exp Ther 1994;269:1310-1318.
163. 2-specific muscarinic cholinergic receptor-mediated inhibition of cardiac regulatory protein phosphorylation. Am J Physiol 1994;266:H1138-H1144.
164. 1-adenosine receptor-mediated inhibition of isoproterenol-stimulated protein phosphorylation in ventricular myocytes. Evidence against a cAMP-dependent effect. Circ Res 1993;72:65-74.
165. [165] George EE, Romano FD, Dobson JG Jr. Adenosine and acetylcholine reduce isoproterenol-induced protein phosphorylation of rat myocytes. J Mol Cell Cardiol 1991;23:749-764.
166. [166] Fenton RA, Dobson JG Jr. Adenosine and calcium alter adrenergic-induced intact heart protein phosphorylation. Am J Physiol 1984;246:H559-H565.
167. 1-adrenoceptor stimulation inhibits the isoproterenol-induced effects on myocardial contractility and protein phosphorylation. Eur J Pharmacol 1995;287:57-64.
168. [168] Gupta RC, Davis BA, Kranias EG. Mechanism of the stimulation of cardiac sarcoplasmic reticulum calcium pump by calmodulin. Membr Biochem 1987;7:73-86.
169. 2+/calmodulin-dependent protein kinase. J Biol Chem 1994;269:26492-26496.
170. 2+-pumping ATPase in cardiac sarcoplasmic reticulum by calcium/calmodulin-dependent protein kinase. Basic Res Cardiol 1997;92:25-35.
171. 2+/calmodulin-dependent protein kinase. J Biol Chem 1993;268:8394-8397.
172. [172] Karczewski P, Bartel S, Krause EG. Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts. Biochem J 1990;266:115-122.
173. [173] Vittone L, Mundina C, Chiappe de Cingolani G, et al. cAMP and calcium-dependent mechanisms of phospholamban phosphorylation in intact hearts. Am J Physiol 1990;258:H318-H325.
174. 2+-calmodulin-dependent protein kinase system. J Mol Cell Cardiol 1992;24:387-396.
175. [175] Mundina-Weilenmann C, Vittone L, Ortale M, et al. Immunodetection of phosphorylation sites gives new insight into the mechanisms underlying phospholamban phosphorylation in the intact heart. J Biol Chem 1996;271:33561-33567.
176. [176] Tada M, Inui M, Yamada M, et al. 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.
177. [177] Wegener AD, Simmerman HK, Lindemann JP, et al. Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to beta-adrenergic stimulation. J Biol Chem 1989;264:11468-11474.
178. [178] Iwasa Y, Hosey MM. Phosphorylation of cardiac sarcolemma proteins by the calcium-activated phospholipid-dependent protein kinase. J Biol Chem 1984;259:534-540.
179. 2+/calmodulin-dependent protein kinase. Mol Cell Biochem 1996;155:91-103.
180. [180] Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 1989;58:453-508.
181. [181] Kirchberger MA, Raffo A. Decrease in calcium transport associated with phosphoprotein phosphatase-catalyzed dephosphorylation of cardiac sarcoplasmic reticulum. J Cycl Nucl Res 1977;3:45-53.
182. [182] Kranias EG. Regulation of calcium transport by protein phosphatase activity associated with cardiac sarcoplasmic reticulum. J Biol Chem 1985;260:11006-11010.
183. [183] Kranias EG, Di Salvo J. A phospholamban protein phosphatase activity associated with cardiac sarcoplasmic reticulum. J Biol Chem 1986;261:10029-10032.
184. [184] Kranias EG, Steenaart NAE, Di Salvo J. Purification and characterization of phospholamban phosphatase from cardiac muscle. J Biol Chem 1988;263:15681-15687.
185. [185] MacDougall LK, Jones LR, Cohen P. Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban. Eur J Biochem 1991;196:725-734.
186. [186] Steenaart NAE, Ganim JR, Di Salvo J, et al. The phospholamban phosphatase associated with cardiac sarcoplasmic reticulum is a type 1 enzyme. Arch Biochem Biophys 1992;293:17-24.
187. [187] Sulakhe PV, Vo XT, Morris TE, et al. Protein phosphorylation in rat cardiac microsomes: effects of inhibitors of protein kinase A and of phosphatases. Mol Cell Biochem 1997;175:109-115.
188. [188] Inui M, Saito A, Fleischer S. Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures. J Biol Chem 1987;262:15637-15642.
189. [189] Fabiato A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol 1983;245:C1-C14.
190. [190] Fleischer S, Inui M. Biochemistry and biophysics of excitation-contraction coupling. Annu Rev Biophys Biophys Chem 1989;18:333-364.
191. [191] Lai FA, Erickson HP, Rousseau E, et al. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 1988;331:315-319.
192. 2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum. J Biol Chem 1990;265:13472-13483.
193. [193] Smith JS, Imagawa T, Ma J, et al. Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum. J Gen Physiol 1988;92:1-26.
194. [194] Tinker A, Lindsay ARG, Williams A. A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum. J Gen Physiol 1992;100:495-517.
195. 2+, adenine nucleotide and calmodulin. J Biol Chem 1987;262:3065-3073.
196. [196] Witcher DR, Kovacs RJ, Schulman H, et al. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 1991;266:11144-11152.
197. [197] Strand MA, Louis CF, Mickelson JR. Phosphorylation of the porcine skeletal and cardiac muscle sarcoplasmic reticulum ryanodine receptor. Biochim Biophys Acta 1993;1175:319-326.
198. [198] Takasago T, Imagawa T, Shigekawa M. Phosphorylation of the cardiac ryanodine receptor by cAMP-dependent protein kinase. J Biochem Tokyo 1989;106:872-877.
199. [199] Yoshida A, Takahashi M, Imagawa T, et al. Phosphorylation of ryanodine receptors in rat myocytes during beta-adrenergic stimulation. J Biochem Tokyo 1992;111:186-190.
200. [200] Campbell KP, MacLennan DH. Purification and characterization of the 53000-dalton glycoprotein from the sarcoplasmic reticulum. J Biol Chem 1981;256:4626-4632.
201. [201] Jorgensen AO, Campbell KP. Evidence for the presence of calsequestrin in two structurally different regions of myocardial sarcoplasmic reticulum. J Cell Biol 1984;98:1597-1602.
202. [202] Kawamoto RM, Brunschwig JP, Kim KC, et al. Isolation, characterization and localization of the spanning protein from skeletal muscle triads. J Cell Biol 1986;103:1405-1414.
203. [203] Franzini-Armstrong C, Kenney LJ, Varriano-Marston E. The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. J Cell Biol 1987;105:49-56.
204. [204] Ikemoto N, Ronjat M, Meszaros LG, et al. Postulated role of calsequestrin in the regulation of calcium release from sarcoplasmic reticulum. Biochemistry 1989;28:6764-6771.
205. [205] Yano K, Zarain Herzberg A. Sarcoplasmic reticulum calsequestrins: structural and functional properties. Mol Cell Biochem 1994;135:61-70.
206. [206] Scott BT, Simmerman HKB, Collins JH, et al. Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. J Biol Chem 1988;263:8958-8964.
207. [207] Cala SE, Jones LR. Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. J Biol Chem 1991;266:391-398.
208. [208] Cala SE, Miles K. Phosphorylation of the cardiac isoform of calsequestrin in cultured rat myotubes and rat skeletal muscle. Biochim Biophys Acta 1992;1118:277-287.
209. 2+-calmodulin stimulate the formation of polyphosphoinositides in a sarcoplasmic reticulum preparation of rabbit heart. FEBS Lett 1984;176:235-238.
210. [210] Varsanyi M, Messer M, Brandt N, et al. Phosphatidylinositol 4,5′-diphosphate formation in rabbit skeletal and heart muscle membrane. Biochem Biophys Res Commun 1986;138:1395-1404.
211. [211] Zot A, Potter JD. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu Rev Biophys Biophys Chem 1987;16:535-559.
212. [212] Wilkinson JM, Grand RJA. Comparison of amino acid sequence of troponin I from different striated muscles. Nature 1978;271:31-35.
213. [213] Perry SV, Cole HA. Phosphorylation of troponin and the effects of interactions between components of the complex. Biochem J 1974;141:733-743.
214. [214] Cole HA, Perry SV. The phosphorylation of troponin I from cardiac muscle. Biochem J 1975;149:525-533.
215. [215] Reddy YS. Phosphorylation of cardiac regulatory proteins by cyclic AMP-dependent protein kinase. Am J Physiol 1976;231:1330-1336.
216. [216] Moir AJ, Perry SV. The sites of phosphorylation of rabbit cardiac troponin I by adenosine 3′ :5′-cyclic monophosphate-dependent protein kinase. Effect of interaction with troponin C. Biochem J 1977;167:333-343.
217. 2+ dependence of cardiac myofibril ATPase activity. FEBS Lett 1976;70:11-16.
218. [218] Holroyde MJ, Howe E, Solaro RJ. Modification of calcium requirements for activation of cardiac myofibrillar ATPase by cyclic AMP dependent phosphorylation. Biochem Biophys Acta 1979;586:63-69.
219. 2+-regulatory site of bovine cardiac troponin. J Biol Chem 1982;257:260-263.
220. [220] Wattanapermpool J, Guo X, Solaro J. The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar activity only when it is phosphorylated. J Mol Cell Cardiol 1995;27:1383-1391.
221. [221] Keane NE, Quirk PG, Gao Y, et al. The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase. Structural consequences and functional implications. Eur J Biochem 1997;248:329-337.
222. [222] Dong W-J, Chandra M, Xing J, et al. Phosphorylation-induced distance change in a cardiac muscle troponin I mutant. Biochemistry 1997;36:6754-6761.
223. [223] Chandra M, Dong W-J, Pan B-S, et al. Effects of protein kinase A phosphorylation on signaling between cardiac troponin I and the N-terminal domain of cardiac troponin C. Biochemistry 1997;36:13305-13311.
224. [224] England PJ. Correlation between contraction and phosphorylation of the inhibitory subunit of troponin in perfused rat heart. FEBS Lett 1975;50:57-60.
225. [225] England PJ. Studies on the phosphorylation of the inhibitory subunit of troponin during modification of contraction in perfused rat heart. Biochem J 1976;160:295-304.
226. [226] Moir AJ, Solaro RJ, Perry SV. The site of phosphorylation of troponin I in the perfused rabbit heart: the effect of adrenaline. Biochem J 1980;185:505-513.
227. [227] Hofmann PA, Lange JHr. Effects of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats. Circ Res 1994;74:718-726.
228. [228] Rosenthal RA, Lowenstein JM. Inhibition of phosphorylation of troponin I in rat heart by adenosine and 5′-chloro-5′-deoxyadenosine. Biochem Pharmacol 1991;42:685-692.
229. [229] Neumann J, Boknik P, Herzig S, et al. Evidence for physiological functions of protein phosphatases in the heart: evaluation with okadaic acid. Am J Physiol 1993;265:H257-H266.
230. [230] Neumann J, Boknik P, Herzig S, et al. Biochemical and electrophysiological mechanisms of the positive inotropic effect of calyculin A, a protein phosphatase inhibitor. J Pharmacol Exp Ther 1994;271:535-541.
231. [231] Neumann J, Herzig S, Boknik P, et al. On the cardiac contractile, biochemical and electrophysiological effects of cantharidin, a phosphatase inhibitor. J Pharmacol Exp Ther 1995;274:530-539.
232. 2+-dependent protein kinase. Biochem J 1983;209:189-195.
233. [233] Noland TA Jr, Raynor RL, Kuo JF. Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J Biol Chem 1989;264:20778-20785.
234. 2+-stimulated actomyosin MgATPase activity. J Biol Chem 1991;266:4974-4978.
235. [235] Jideama NM, Noland TA, Raynor RL, et al. Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties. J Biol Chem 1996;271:23277-23283.
236. [236] Liu JD, Wood JG, Raynor RL, et al. Subcellular distribution and immunocytochemical localization of protein kinase C in myocardium and phosphorylation of troponin in isolated myocytes stimulated by isoproterenol or phorbol ester. Biochem Biophys Res Commun 1989;162:1105-1110.
237. [237] Damron DS, Darvish A, Murphy L, et al. Arachidonic acid-dependent phosphorylation of troponin I and myosin light chain 2 in cardiac myocytes. Circ Res 1995;76:1011-1019.
238. [238] Gando S, Nishihira J, Hattori Y, et al. Endothelin-1 does not phosphorylate phospholamban and troponin I in intact beating rat hearts. Eur J Pharmacol 1995;289:175-180.
239. [239] Frearson N, Solaro RJ, Perry SV. Changes in phosphorylation of P light chain of myosin in perfused rabbit heart. Nature 1976;264:801-802.
240. [240] Ezrailson EG, Potter JD, Michael L, et al. Positive inotropy induced by ouabain, by increased frequency, by X537A (R02-2985), by calcium and by isoproterenol: the lack of correlation with phosphorylation of Tn-I. J Mol Cell Cardiol 1977;9:693-698.
241. [241] Heeley DA, Moir AJG, Perry SV. Phosphorylation of tropomyosin during development in mammalian striated muscle. FEBS Lett 1982;146:115.
242. 2+-dependent actomyosin MgATPase activity and troponin T binding to tropomyosin:F-actin complex. Biochem J 1992;288:123-129.
243. [243] Malhotra A, Huang S, Bhan A. Subunit function in cardiac myosin: effect of removal of LC2 (18000 molecular weight) on enzymatic properties. Biochemistry 1979;18:461-467.
244. [244] Barany K, Barany M, Hager SR, et al. Myosin light chain and membrane protein phosphorylation in various muscles. Fed Proc 1983;42:27-32.
245. [245] England PJ. The significance of phosphorylation of myosin light chains in heart. J Mol Cell Cardiol 1984;16:591-595.
246. [246] Jeacocke SA, England PJ. Phosphorylation of myosin light chains in perfused rat heart. Effect of adrenaline and increased cytoplasmic calcium ions. Biochem J 1980;188:763-768.
247. [247] Westwood SA, Perry SV. The effect of adrenaline on the phosphorylation of the P light chain of myosin and troponin I in the perfused rabbit heart. Biochem J 1981;197:185-193.
248. [248] Kopp SJ, Barany M. Phosphorylation of the 19000-dalton light chain of myosin in perfused rat heart under the influence of negative and positive inotropic agents. J Biol Chem 1979;254:1207-1212.
249. [249] Resink TJ, Gevers W, Noakes TD. Effects of extracellular calcium concentrations on myosin P light chain phosphorylation in hearts from running-trained rats. J Mol Cell Cardiol 1981;13:753-765.
250. [250] Resink TJ, Gevers W, Noakes TD, et al. Increased cardiac myosin ATPase activity as a biochemical adaptation to running training: enhanced response to catecholamines and a role for myosin phosphorylation. J Mol Cell Cardiol 1981;13:679-694.
251. [251] Herring BP, England PJ. The turnover of phosphate bound to myosin light chain-2 in perfused rat heart. Biochem J 1986;240:205-214.
252. [252] Moos C, Offer G, Starr R, et al. Interaction of C-protein with myosin, myosin rod and light meromyosin. J Mol Biol 1975;97:1-9.
253. [253] Moos C, Feng IM. Effect of C-protein on actomyosin ATPase. Biochim Biophys Acta 1980;632:141-149.
254. 2+-calmodulin-dependent protein kinases. J Biol Chem 1984;259:15587-15596.
255. r 150000 in perfused rat heart and the tentative identification of this as C-protein. FEBS Lett 1980;122:129-132.
256. [256] Onorato JJ, Rudolph SA. Regulation of protein phosphorylation by inotropic agents in isolated rat myocardial cells. J Biol Chem 1981;256:10697-10703.
257. [257] Neumann J, Boknik P, Kaspareit G, et al. Effects of the phosphatase inhibitor calyculin A on the phosphorylation of C-protein in mammalian ventricular cardiomyocytes. Biochem Pharmacol 1995;49:1583-1588.
258. [258] Iyer RB, Koritz SB, Kirchberger MA. A regulation of the level of phosphorylated phospholamban by inhibitor-1 in rat heart preparations in vitro. Mol Cell Endocrinol 1988;55:1-6.
259. [259] Meek DW, Street AJ. Nuclear protein phosphorylation and growth control. Biochem J 1992;287:1-15.
260. [260] Goldspink PH, Russell B. The cAMP response element binding protein is expressed and phosphorylated in cardiac myocytes. Circ Res 1994;74:1042-1049.
261. [261] Muller F, Boknik P, Horst A, et al. cAMP response element binding protein is expressed and phosphorylated in the human heart. Circulation 1995;92:2041-2043.
262. [262] Montminy MR, Gonzalez GA, Yamamoto KK. Characteristics of the cAMP response unit. In: Cohen P, Foulkes JG, editors. The Hormonal Regulation of Gene Transcription. Amsterdam:Elsevier, 1991:161-71.
263. [263] Muller FU, Boknik P, Horst A, et al. In vivo isoproterenol treatment leads to downregulation of the mRNA encoding the cAMP response element binding protein in the rat heart. Biochem Biophys Res Commun 1995;215:1043-1049.
264. [264] Murphy AM, Thompson WR, Peng LF, et al. Regulation of the rat cardiac troponin I gene by the transcription factor GATA-4. Biochem J 1997;322:393-401.
265. [265] Chen JJ, Liew CC. Phosphorylation of an acid-soluble nuclear protein in response to catecholamine in cultured rat cardiocytes. Biochem Biophys Res Commun 1993;190:754-759.
266. [266] Pickett-Gies CA, Walsh DA. Phosphorylase kinase. In: Boyer PD, editor. The Enzymes. Orlando, Fl:Academic Press, 1986:395-459.
267. [267] Hayes JS. Coordination of cardiac contractility and metabolism by protein phosphorylation. In: Solaro RJ, editor. Protein Phosphorylation in Heart Muscle. Boca Raton, Fl:CRC Press, 1986:17-54.
268. [268] Ramachandran C, Gros J, Waelkens E, et al. The interrelationship between cAMP-dependent α and β subunit phosphorylation in the regulation of phosphorylase kinase activity. J Biol Chem 1987;262:3210-3218.
269. [269] Sul HS, Cooper RH, Whitehouse S, et al. Cardiac phosphorylase kinase. Modulation of the activity by cAMP-dependent and cAMP-dependent phosphorylation of the alpha- subunit. J Biol Chem 1982;257:3484-3490.
270. [270] Sul HS, Walsh DA. Cardiac phosphorylase kinase. Deactivation by selective dephosphorylation of alpha′ and beta subunits. J Biol Chem 1982;257:10324-10328.
271. [271] Hayes JS, Meyer SE. Regulation of guinea pig heart phosphorylase kinase by cAMP, protein kinase and calcium. Am J Physiol 1981;240:E340-E349.
272. [272] McCullough TE, Walsh DA. Phosphorylation and dephosphorylation of phosphorylase kinase in the perfused rat heart. J Biol Chem 1979;254:7345-7352.
273. [273] Angelos KL, Ramachandran C, Walsh DA. Subunit phosphorylation and activation of phosphorylase kinase in perfused rat hearts. J Biol Chem 1987;262:3219-3226.
274. [274] Bartel S, Karczewski P, Krause EG. Protein phosphorylation and cardiac function: cholinergic-adrenergic interaction. Cardiovasc Res 1993;27:1948-1953.
275. [275] Koss KL, Grupp IL, Kranias EG. The relative phospholamban and SERCA2 ratio: a critical determinant of myocardial contractility. Basic Res Cardiol 1997;92:17-24.
276. [276] Boyett MR, Frampton JE, Harrison SM, et al. The role of intracellular calcium, sodium and pH in rate-dependent changes of cardiac contractile force. In: Noble MIMSeed WA, editor. The Interval Force Relationship of the Heart: Bowditch Revisited. Cambridge, UK:Cambridge Univ. Press, 1992.
277. 2+ transient in rat heart is independent of phospholamban phosphorylation. Am J Physiol 1997;273:H695-706.
278. [278] Puceat M, Hilal Dandan R, Strulovici B, et al. Differential regulation of protein kinase C isoforms in isolated neonatal and adult rat cardiomyocytes. J Biol Chem 1994;269:16938-16944.
279. [279] Johnson JA, Adak S, Mochly-Rosen D. Prolonged phorbol ester treatment down-regulates protein kinase C isozymes and increases contraction rate in neonatal cardiac myocytes. Life Sci 1995;57:1027-1038.
280. [280] Johnson JA, Gray MO, Chen C-H, et al. A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function. J Biol Chem 1996;271:24962-24966.
281. [281] Sugden PH, Bogoyevitch MA. Intracellular signalling through protein kinases in the heart. Cardiovasc Res 1995;30:478-492.
282. [282] Page C, Doubell AF. Mitogen-activated protein kinase (MAPK) in cardiac tissues. Mol Cell Biochem 1996;157:49-57.
283. [283] Clerk A, Bogoyevitch MA, Anderson MB, et al. Differential activation of protein kinase C isoforms by endothelin-1 and phenylephrine and subsequent stimulation of p42 and p44 mitogen-activated protein kinases in ventricular myocytes cultured from neonatal rat hearts. J Biol Chem 1994;269:32848-32857.
284. 1-adrenergic receptor signaling in cardiomyocytes. J Biol Chem 1996;217:31185-31190.
285. 1-adrenergic receptor and Ras activation and is associated with in vitro and in vivo cardiac hypertrophy. J Biol Chem 1997;272.
286. [286] Bogoyevitch MA, Glennon PE, Andersson MB, et al. Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy. J Biol Chem 1994;269:1110-1119.
287. 2+-dependent signaling. Circ Res 1995;76:1-15.
288. 2-terminal kinase in cultured cardiac myocytes of neonatal rats. Circ Res 1997;80:139-146.
289. [289] Sadoshima J, Aoki H, Izumo S. Angiotensin II and serum differentially regulate expression of cyclins, activity of cyclin-dependent kinases, and phosphorylation of retinoblastoma gene product in neonatal cardiac myocytes. Circ Res 1997;80:228-241.
290. 3 generation. Biochem J 1996;318:723-728.
291. [291] Laderoute KR, Webster KA. Hypoxia/reoxygenation stimulates jun kinase activity through redox signalling in cardiac myocytes. Circ Res 1997;80:336-344.
292. [292] Clerk A, Sugden PH. Activation of p21-activated protein kinase a (αPAK) by hyperosmotic shock in neonatal ventricular myocytes. FEBS Lett 1997;403:23-25.
293. [293] Mizukami Y, Yoshida K. Mitogen-activated protein kinase translocates to the nucleus during ischemia and is activated during reperfusion. Biochem J 1997;323:785-790.
294. [294] Mizukami Y, Yoshioka K, Morimoto S, et al. A novel mechanism of JNKl activation. Nuclear translocation and activation of JNKl during ischemia and reperfusion. J Biol Chem 1997;272:16657-16662.
295. [295] Yamazaki T, Komuro I, Kudoh S, et al. Mechanical stress activates protein kinase cascade of phosphorylation in neonatal rat cardiac myocytes. J Clin Invest 1995;96:438-446.
296. [296] Mubagwa K. Sarcoplasmic reticulum function during myocardial ischemia and reperfusion. Cardiovasc Res 1995;30:166-175.
297. [297] Luciani GB, D'Agnalo A, Mazzucco A, et al. Effects of ischemia on sarcoplasmic reticulum and contractile myofilament activity in human myocardium. Am J Physiol 1993;265:H1334-H1341.
298. [298] Ward CA, Moffat MP. Signal transduction mechanisms in the ischemic and reperfused myocardium. In: Karmazyn M, editor. Myocardial Ischemia: Mechanisms, Reperfusion, Protection. Basel, Switzerland:Birkhauser Verlag, 1996:191-207.
299. 32P incorporation into phospholamban-like protein of sarcolemma due to myocardial ischaemia in anaesthetized pigs. J Mol Cell Cardiol 1986;18:115-125.
300. 2+ transport regulating proteins in the sarcolemma during myocardial ischemia. In: Rupp H, editor. Regulation of Heart Function. Basic Concepts and Clinical Applications. New York, NY:Thieme Stratton, 1986:350-6.
301. [301] van der Giessen WJ, Verdouw PD, ten Cate FJ, et al. In vitro cyclic AMP induced phosphorylation of phospholamban: an early marker of long-term recovery of function following reperfusion of ischaemic myocardium?. Cardiovasc Res 1988;22:714-718.
302. [302] Krause EG, England PJ. Effect of isoproterenol on protein phosphorylation in myocardial ischaemia. Gen Physiol Biophys 1984;3:193-199.
303. [303] Li P, Hofmann PA, Li B, et al. Myocardial infarction alters myofilament calcium sensitivity and mechanical behavior of myocytes. Am J Physiol 1997;272:H360-H370.
304. [304] Chiappe de Mon LE, Chiappe de Cingolani GE, Cingolani HE. Effect of acidosis on heart cAMP-dependent protein kinase. Arch Int Physiol Biochem 1978;86:277-287.
305. [305] Mundina-Weilenmann C, Vittone L, Cingolani HE, et al. Effects of acidosis on phosphorylation of phospholamban and troponin I in rat cardiac muscle. Am J Physiol 1996;270:C107-C114.
306. [306] Prasad K, Kalra J, Chaudhary AK, et al. Effects of polymorphonuclear leukocyte-derived oxygen free radicals and hypochlorous acid on cardiac function and some biochemical parameters. Am Heart J 1990;119:538-550.
307. [307] Prasad K, Kalra J, Chan WP, et al. Effects of oxygen free radicals on cardiovascular function at organ and cellular levels. Am Heart J 1989;117:1196-1202.
308. 2+ of myofibrils isolated froms stunned and non-stunned porcine myocardium. Mol Cell Biochem 1997;176:211-218.
309. [309] Brand T, Sharma HS, Fleischmann KE, et al. Proto-oncogene expression in porcine myocardium subjected to ischemia and reperfusion. Circ Res 1992;71:1351-1360.
310. [310] Webster KA, Discher DJ, Bishopric NH. Induction and nuclear accumulation of fos and jun proto-oncogenes in hypoxic cardiac myocytes. J Biol Chem 1993;268:16852-16858.
311. [311] Bogoyevitch MA, Gillespie-Brown J, Kettermen AJ, et al. Stimulation of the stress-activated mitogen-activated protein kinase subfamilies in perfused heart. p38/RK mitogen-activated protein kinases and c-jun N-terminal kinases are activated by ischemia/reperfusion. Circ Res 1996;79:162-173.
312. [312] Knight RJ, Buxton DB. Stimulation of c-jun kinase and mitogen-activated protein kinase by ischemia and reperfusion in the perfused rat heart. Biochem Biophys Res Commun 1996;218:83-88.
313. [313] Seko Y, Takahashi M, Tobe K, et al. Hypoxia and hypoxia/reoxygenation activate p65(PAK), p38mitogen-activated protein kinase (MAPK), and stress-activated protein kinase (SAPK) in cultured rat cardiac myocytes. Biochem Biophys Res Commun 1997;239.
314. [314] Murry CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 1986;74:1124-1136.
315. [315] Rapundalo ST, Edmunds JJ, Gallagher KP. Myocardial preconditioning: cellular mechanisms and perspectives for pharmacological induction. Curr Pharm Design 1995;1:483-506.
316. [316] Downey JM, Cohen MV. Signal transduction in ischemic preconditioning. Alfred Benzon Symp 1997;41:339-358.
317. [317] Brooks G, Walsh R, Downey JM. Phosphorylation of 80K/MARKS, a specific substrate of protein kinase C occurs after 5′ ischemia but only in preconditioned hearts. Circulation 1993;88:I-101.
318. [318] Armstrong SC, Ganote CE. Effects of the protein phosphatase inhibitors okadaic acid and calyculin A on metabolically inhibited and ischaemic isolated myocytes. J Mol Cell Cardiol 1992;24:869-884.
319. [319] Armstrong SC, Hoover DB, Delacey MH, et al. Translocation of PKC, protein phosphatase inhibition and preconditioning of rabbit cardiomyocytes. J Mol Cell Cardiol 1996;28:1479-1492.
320. [320] Armstrong SC, Kao R, Gao W, et al. Comparison of in vitro preconditioning responses of isolated pig and rabbit cardiomyocytes: Effects of a protein phosphatase inhibitor, fostriecin. J Mol Cell Cardiol 1997;29:3009-3024.
321. [321] Weinbrenner C, Liu G-S, Cohen MV, et al. Phosphorylation of tyrosine 182 of p38 mitogen-activated protein kinase correlates with the protection of preconditioning in the rabbit heart. J Mol Cell Cardiol 1997;29:2383-2391.
322. ATP channels, and ischemic preconditioning in dogs. Am J Physiol 1993;264:H1327-H1336.
323. [323] Downey JM, Cohen MV, Ytrehus K, et al. Cellular mechanisms in ischemic preconditioning: the role of adenosine and protein kinase C. Ann NY Acad Sci 1994;723:82-98.
324. [324] Cohen MV, Downey JM. Ischaemic preconditioning: can the protection be bottled?. Lancet 1993;342:6.
325. [325] Ganote C, Armstrong S. Ischaemia and the myocyte cytoskeleton: review and speculation. Cardiovasc Res 1993;27:1387-1403.
326. [326] Cooper DR, de Ruiz-Galaretta CM, Fanjul LF, et al. Insulin but not phorbol ester treatment increases phosphorylation of vinculin by protein kinase C in BC3H-1 myocytes. FEBS Lett 1987;214:122-126.
327. [327] Yamazaki T, Komuro I, Yazaki Y. Molecular mechanism of cardiac cellular hypertrophy by mechanical stress. J Mol Cell Cardiol 1995;27:133-140.
328. [328] Takano H, Komuro I, Zou Y, et al. Activation of p70 S6 protein kinase is necessary for angiotensin II-induced hypertrophy in neonatal rat cardiac myocytes. FEBS Lett 1996;379:255-259.
329. [329] Sadoshima J, Qiu Z, Morgan JP, et al. Tyrosine kinase activation is an immediate and essential step in hypotonic cell swelling-induced ERK activation and c-fos gene expression in cardiac myocytes. EMBO J 1996;15:5535-5546.
330. [330] Sunga PS, Rabkin SW. Angiotensin II-induced protein phosphorylation in the hypertrophic heart of the Dahl rat. Hypertension 1992;20:633-642.
331. [331] Bogoyevitch MA, Ketterman AJ, Sugden PH. Cellular stresses differentially activate c-jun N-terminal protein kinases and extracellular signal-regulated protein kinases in cultured ventricular myocytes. J Biol Chem 1995;270:29710-29717.
332. [332] Post GR, Goldstein D, Thuerauf DJ, et al. Dissociation of p44 and p42 mitogen-activated protein kinase activation from receptor-induced hypertrophy in neonatal rat ventricular myocytes. J Biol Chem 1996;271:8452-8457.
333. [333] Kwiatkowska-Patzer B, Domanska-Janik K. Increased 19 kDa protein phosphorylation and protein kinase C activity in pressure-overload cardiac hypertrophy. Basic Res Cardiol 1991;86:402-409.
334. 2-adrenoceptors in the human heart: properties, function and alterations in chronic heart failure. Pharmacol Rev 1991;43:203-242.
335. [335] Böhm M, Reiger B, Schwinger RH, et al. cAMP concentrations, cAMP dependent protein kinase activity and phospholamban in non-failing and failing myocardium. Cardiovasc Res 1994;28:1713-1719.
336. [336] Boateng S, Seymour AM, Dunn M, et al. Inhibition of endogenous phosphatase activity and measurement of sarcoplasmic reticulum calcium uptake: a possible role of phospholamban phosphorylation in the hypertrophied myocardium. Biochem Biophys Res Commun 1997;239:701-705.
337. [337] Bartel S, Stein B, Eschenhagen T, et al. Protein phosphorylation in isolated trabeculae from non-failing and failing human hearts. Mol Cell Biochem 1996;157.
338. [338] Bodor GS, Oakeley AE, Allen PD, et al. Troponin I phosphorylation in the normal and failing adult human heart. Circulation 1997;96:1495-1500.
339. [339] Wolff MR, Whitesell LF, Moss RL. Calcium sensitivity of isometric tension is increased in canine experimental heart failure. Circ Res 1995;76:781-789.
340. [340] Wolff MR, Buck SH, Stoker SW, et al. Myofibrillar calcium sensitivity of isometric tension is increased in human dilated cardiomyopathies. J Clin Invest 1996;98:167-176.
341. [341] Liu X, Shao Q, Dhalla NS. Myosin light chain phosphorylation in cardiac hypertrophy and failure due to myocardial infarction. J Mol Cell Cardiol 1995;27:2611-2621.
342. [342] Morano I, Haddicke K, Haase H, et al. Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart. J Mol Cell Cardiol 1997;29:1177-1187.
343. [343] Geenen DL, Malhotra A, Scheuer J. Regional variation in rat cardiac myosin isoenzymes and ATPase activity after infarction. Am J Physiol 1989;256:H745-H750.
344. [344] Malhotra A, Reich D, Reich D, et al. Experimental diabetes is associated with functional activation of protein kinase C epsilon and phosphorylation of troponin I in the heart, which are prevented by angiotensin II receptor blockade. Circ Res 1997;81:1027-1033.
345. [345] McConnell BK, Moravec CS, Morano I, et al. Troponin I phosphorylation in spontaneously hypertensive rat heart: effect of β-adrenergic stimulation. Am J Physiol 1997;273:H1440-H1451.
346. [346] Moravec CS, Keller E, Bond M. Decrease inotropic response to beta-adrenergic stimulation and normal sarcoplasmic reticulum calcium stores in the spontaneously hypertensive rat heart. J Mol Cell Cardiol 1995;27:632-639.
347. [347] Krebs EG, Beavo JA. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem 1979;48:923-959.
348. 2-adenosine receptor agonist, in the mammalian ventricle. J Cardiovasc Pharmacol 1997;30:750-758.
349. 2+-dependent in intact beating hearts. FEBS Lett 1997;409:131-136.
350. [350] McConnell BK, Moravec CS, Bond M. Troponin I phosphorylation and myofilament calcium sensitivity during decompensated cardiac hypertrophy. Am J Physiol 1998;274:H385-H396.