Calcium cycling proteins of the cardiac sarcoplasmic reticulum: Molecular regulation of the phospholamban-SERCA Ca2+ pump system and its pathophysiological consequences

Circulation Journal

Volumn 67, Issue 9, 2003, Pages 729-737

  Tada, Michihiko ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM; PHOSPHOLAMBAN; PROTEIN SERCA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; CALCIUM SIGNALING; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME STRUCTURE; HEART MUSCLE; HUMAN; METABOLIC REGULATION; MOLECULAR MECHANICS; NONHUMAN; PATHOPHYSIOLOGY; PROTEIN PROTEIN INTERACTION; REVIEW; SARCOPLASMIC RETICULUM; STRUCTURE ANALYSIS;

EID: 0041819495     PISSN: 13469843     EISSN: None     Source Type: Journal    
DOI: 10.1253/circj.67.729     Document Type: Review

References (47)

1. 2+-ATPase. In: Page E, Fozzard, HA, Solaro, RJ, editors. The handbook of physiology, Section 2, The cardiovascular system: Vol. 2; 2001: 301-334.
2. Tada M, Toyofuku T. Molecular regulation of phospholamban function and expression. Trends Cardiovasc Med 1998; 8: 330-340.
3. Tada M, Katz AM. Phosphorylation of the sarcoplasmic reticulum and sarcolemma. Annu Rev Physiol 1982; 44: 401-423.
4. Tada M, Inui M, Yamada M, Kadoma M, Kuzuya T, Abe H, 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.
5. 2+-pump from cardiac sarcoplasmic reticulum. Methods Enzymol 1988; 157: 107-154.
6. MacLennan DH. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem 1970; 245: 4508-4518.
7. 2+-ATPase gene. J Biol Chem 1988; 263: 15024-15031.
8. Toyoshima C, Sasabe H, Stokes DL. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane [published erratum appears in Nature May 20 1993; 363(6426): 286]. Nature 1993; 362: 467-471.
9. Zhang P, Toyoshima C, Yonekura K, Green NM, Stokes DL. Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution. Nature 1998; 392: 835-839.
10. 2+-ATPase. Nature 1989; 339: 476-478.
11. 2+-ATPase of sarcoplasmic reticulum (SERCA1a). J Biol Chem 1996; 271: 31412-31419.
12. Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 2000; 405: 647-655.
13. Tada M, Yamamoto T, Tonomura Y. Molecular mechanism of active calcium transport by sarcoplasmic reticulum. Physiol Rev 1978; 58: 1-79.
14. 2+-ATPases. J Biol Chem 1997; 272: 28815-28818.
15. Green NM, MacLennan DH. ATP driven ion pumps: An evolutionary mosaic. Biochem Soc Trans 1989; 17: 819-822.
16. 2+-dependent ATPase of the sarcoplasmic reticulum. Annu Rev Biochem 1979; 48: 275-292.
17. 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.
18. Tada M, Kirchberger MA, Repke DI, Katz AM. The stimulation of calcium transport in cardiac sarcoplasmic reticulum by adenosine 3′:5′ -monophosphate-dependent protein kinase. J Biol Chem 1974; 249: 6174-6180.
19. Tada M, Kirchberger MA, Li HC. Phosphoprotein phosphatase-catalyzed dephosphorylation of the 22,000 dalton phosphoprotein of cardiac sarcoplasmic reticulum. J Cyclic Nucleotide Res 1975; 1: 329-338.
20. 2+-dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase. Role of the 22,000-dalton protein. J Biol Chem 1979; 254: 319-326.
21. Inui M, Kadoma M, Tada M. Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum. J Biol Chem 1985; 260: 3708-3715.
22. Jones LR, Simmerman HK, Wilson WW, Gurd FR, Wegener AD. Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum. J Biol Chem 1985; 260: 7721-7730.
23. Fujii J, Ueno A, Kitano K, Tanaka S, Kadoma M, Tada M. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. J Clin Invest 1987; 79: 301-304.
24. Watanabe Y, Kijima Y, Kadoma M, Tada M, Takagi T. Molecular weight determination of phospholamban oligomer in the presence of sodium dodecyl sulfate: Application of low-angle laser light scattering photometry. J Biochem (Tokyo) 1991; 110: 40-45.
25. Cornea RL, Jones LR, Autry JM, Thomas DD. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 1997; 36: 2960-2967.
26. Fujii J, Maruyama K, Tada M, MacLennan DH. Expression and site-specific mutagenesis of phospholamban: Studies of residues involved in phosphorylation and pentamer formation. J Biol Chem 1989; 264: 12950-12955.
27. 2+ pump of sarcoplasmic reticulum. Nature 1989; 342: 90-92.
28. 2+ pump ATPase. J Biol Chem 1992; 267: 1674-1679.
29. 2+ transport step of the Ca (2+)-ATPase. Biochem J 1994; 303: 511-516.
30. Toyofuku T, Kurzydlowski K, Tada M, MacLennan DH. Identification of regions in the Ca (2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban. J Biol Chem 1993; 268: 2809-2815.
31. Toyofuku T, Kurzydlowski K, Tada M, MacLennan DH. Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca (2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J Biol Chem 1994; 269: 22929-22932.
32. Toyofuku T, Kurzydlowski K, Tada M, MacLennan DH. Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca (2+)-ATPase of sarcoplasmic reticulum. J Biol Chem 1994; 269: 3088-3094.
33. 2+-ATPase through intramembrane interactions. J Biol Chem 1996; 271: 21726-21731.
34. Kimura Y, Kurzydlowski K, Tada M, MacLennan DH. Phospholamban inhibitory function is activated by depolymerization. J Biol Chem 1997; 272: 15061-15064.
35. 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.
36. 2+-ATPase forms a functional interaction site with phospholamban. J Biol Chem 1999; 274: 32855-32862.
37. 2+ ATPase. Proc Natl Acad Sci USA 2003; 100: 467-472.
38. 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.
39. 2+ ATPase studied by fluorescence. Nature 1978; 273: 396-398.
40. 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.
41. Li M, Reddy LG, Bennett R, Silva ND Jr, Jones LR, Thomas DD. A fluorescence energy transfer method for analyzing protein oligomeric structure: Application to phospholamban. Biophys J 1999; 76: 2587-2599.
42. Fabiato A, Fabiato F. Relaxing and inotropic effects of cyclic AMP on skinned cardiac cells. Nature 1975; 253: 556-558.
43. Reuter H. Localization of beta adrenergic receptors, and effects of noradrenaline and cyclic nucleotides on action potentials, ionic currents and tension in mammalian cardiac muscle. J Physiol 1974; 242: 429-451.
44. 2+-ATPase and phospholamban mRNA expression in response to pressure overload and thyroid hormone. Proc Natl Acad Sci USA 1989; 86: 2966-2970.
45. Luo W, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res 1994; 75: 401-409.
46. Minamisawa S, Hoshijima M, Chu G, Ward CA, Frank K, Gu Y, et al. Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy. Cell 1999; 99: 313-322.
47. Haghighi K, Schmidt AG, Hoit BD, Brittsan AG, Yatani A, Lester JW, et al. Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure. J Biol Chem 2001; 276: 24145-24152.