Regulation of the Skeletal Sarcoplasmic Reticulum Ca²⁺ Pump by Phospholamban in Reconstituted Phospholipid Vesicles

References

• Cuppoletti J., Blumenthal K.M., Malinowska D.H. melittin inhibition of the gastric (H+ + K+) ATPase and photoaffinity labeling with [125I]Azidosalicylyl melittin. Arch. Biochem. Biophys. 1989; 275: 263–270
   Google 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: 13587–13591
   Google Scholar
• Fiske C.H., SubbaRow J. The colorimetric determination of phosphorus. J. Biol. Chem. 1925; 66: 375–400
   Google Scholar
• Garrison J.C. Methods Enzymol. 1983; 99: 20–36
   PubMed Web of Science ®Google Scholar
• Ikemoto N. Structure and function of the calcium pump protein of sarcoplasmic reticulum. Annu. Rev. Physiol. 1982; 44: 297–317
   Google 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
• James P., Inui M., Tada M., Chiesi M., Carafoli E. Nature and site of phospholamban regulation of the Ca2+ pump of sarcoplasmic reticulum. Nature 1989; 342: 90–92
   PubMed Web of Science ®Google Scholar
• Ji I., Shin J., Ji T.H. Radioiodination of a photoactivable heterobifunctional reagent. Anal. Biochem. 1985; 151: 348–349
   Google Scholar
• Kim H.W., Steenaart N.A.E., Ferguson D.G., Kranias E.G. Functional reconstitution of the cardiac sarcoplasmic reticulum Ca2+-ATPase with phospholamban in phospholipid vesicles. J. Biol. Chem. 1990; 265: 1702–1709
   Google Scholar
• Kirchberger M.A., Antonetz T. Calmodulin-mediated regulation of calcium transport and (Ca2+ + Mg2+)-activated ATPase activity in isolated cardiac sarcoplasmic reticulum. J. Biol. Chem. 1982; 257: 5685–5691
   PubMed Web of Science ®Google Scholar
• Kirchberger M.A., Borchman D., Kasinathan C. Proteolytic activation of the canine cardiac sarcoplasmic reticulum calcium pump. Biochemistry 1986; 25: 5485–5492
   Google Scholar
• Kovacs R.J., Nelson M.T., Simmerman H.K.B., Jones L.K. Phospholamban forms Ca2+-selective channels in lipid bilayers. J. Biol. Chem. 1988; 263: 18364–18368
   Google 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 kinase. Biochemistry 1980; 19: 5434–5439
   PubMed Web of Science ®Google Scholar
• Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• LaRaia P.J., Morkin E. Activation of synthetic processes in cardiac hypertrophy. Circ. Res. 1974; 35: 298–305
   Google Scholar
• Le Peuch C.L., Haiech J., Demaille J.G. Calcium and cyclic nucleotide dependent regulatory mechanisms during development of chick embryo skeletal muscle. Biochemistry 1979; 18: 5150–5157
   PubMed Web of Science ®Google Scholar
• Movsesian M.A., Nishikawa M., Adelstein R.S. Phosphorylation of phospholamban by calcium-activated, phospholipid-dependent protein kinase. Stimulation of cardiac SR calcium uptake. J. Biol. Chem. 1984; 259: 8029–8032
   PubMedGoogle Scholar
• Nakamura Y., Tonomura Y. Changes in affinity for calcium ions with the formation of two kinds of phosphoenzyme in the Ca2+ + Mg2+-dependent ATPase of sarcoplasmic reticulum. J. Biochem. 1982; 91: 449–461
   Google Scholar
• Simmerman H.K.B., Collins J.H., Theibert J.L., Wegner A.D., Jones L.R. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 1986; 261: 13333–13341
   PubMed Web of Science ®Google Scholar
• Stewart P.S., MacLennan D.H. Surface particles of sarcoplasmic reticulum membranes. Structural features of adenosine triphosphatase. J. Biol. Chem. 1974; 249: 985–993
   PubMed Web of Science ®Google Scholar
• Stewart P.S., MacLennan D.H., Shamoo A.E. Isolation and characterization of tryptic fragments of the adenosine triphosphatase of sarcoplasmic reticulum. J. Biol. Chem. 1976; 251: 712–719
   PubMed Web of Science ®Google 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
• Szymańska G., Kim H.W., Kranias E.G. Reconstitution of the skeletal sarcoplasmic reticulum Ca2+-pump: Influence of negatively charged phospholipids. Biochim. Biophys. Acta 1991; 1091: 127–134
   Google Scholar
• Tada M., Kirchberger M.A., Katz A.M. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′,5′-monophosphate-dependent protein kinase. J. Biol. Chem. 1975; 250: 2640–2647
   PubMed Web of Science ®Google Scholar
• Wakabayashi S., Shigekawa M. Rapid reconstitution and characterization of highly-efficient sarcoplasmic reticulum Ca2+ pump. Biochim. Biophys. Acta 1985; 813: 266–276
   Google Scholar
• Young E.F., McKee M.J., Ferguson D.G., Kranias E.G. Structural characterization of phospholamban in cardiac sarcoplasmic reticulum membranes by cross-linking. Membrane Biochem 1989; 8: 95–106
   Web of Science ®Google Scholar