Structural Characterization of Phospholamban in Cardiac Sarcoplasmic Reticulum Membranes by Cross-Linking

References

• Ambudkar I. S., Shamoo A. E. Role of phospholamban in regulating cardiac sarcoplasmic reticulum calcium pump. Membrane Biochem. 1984; 5: 119–130
   Web of Science ®Google Scholar
• Davis B. A., Schwartz A., Sarnaha F. J., Kranias E. G. 1983. Regulation of cardiac sarcoplasmic reticulum calcium transport by calcium-calmodulin-dependent phosphorylation 1983; J. EM. Chem.: 13587–13591
   Google Scholar
• Finer-Moore J., Stroud R. M. Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor. Proc. Natl. Acad. Sci. USA 1984; 81: 155–159
   PubMed Web of Science ®Google Scholar
• 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
   PubMedGoogle Scholar
• Hixson S. H., Hixson S. S. p-Azidophenacyl bromide, a versatile photolabile bifunctional reagent. Reaction with glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 1975; 14: 4251–4254
   Google Scholar
• Hixson S. H., Hixson S. S. p-Azidophenacyl bromide, a versatile photolabile bifunctional reagent. Reaction with glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 1975; 14: 4251–4254
   Google 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
• Jakab G., Kranias E. G. Phosphorylation and dephosphorylation of purified phospholamban and associated phosphatidylinositides. Biochemistry 1988; 27: 3799–3805
   PubMedGoogle Scholar
• Jones L. R., Simmerman H. K. B., Wilson W. W., Guard 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
• Kiehm D. J., Ji T. H. Photochemical cross-linking of cell membranes. J. Biol. Chem. 1977; 252: 8524–8531
   Google 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: 5685–5691
   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., Tada M., Katz A. M. 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
• Kranias E. G. 1985. Regulation of calcium transport by protein phosphatase activity associated with cardiac sarcoplasmic reticulum 1985; J. Biol. Chem.: 11006–11010
   Google Scholar
• Kranias E. G., Mandel F., Wang T., Schwartz A. Mechanism of the stimulation of calcium independent 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., Jungmann 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
• 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. L., Haiech J., De Maille J. G. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylation. Biochemistry 1979; 18: 5150–5157
   PubMed Web of Science ®Google Scholar
• Means G. E., Feney R. E. Acylating and similar reagents. Chemical Modification of Proteins. Holden-Day, San Francisco 1971
   Google Scholar
• Mitchinson C., Wilderspin A. F., Trinnaman B. J., Green N. M. Identification of a labelled peptide after stoichiometric reaction of fluorescein isothiocyanate with the Ca2+ - dependent adenosine triphosphatase of sarcoplasmic reticulum. FEBS Lett. 1982; 146: 87–92
   PubMed Web of Science ®Google 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
• Schrock A. K., Schuster G. B. Photochemistry of phenyl azide: Chemical properties of the transient intermediates. J. Am. Chem. Soc. 1984; 106: 5228–5234
   Web of Science ®Google Scholar
• Simmerman H. K. B., Collins J. H., Theibert J. L., Wegener A. D., Jones L. R. 1986. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains 1986; J. Biol. Chem.: 13333–13341
   Google Scholar
• Staros J. V. Aryl azide photolabels in biochemistry. TIBS Dec. 1980; 320–322
   Google 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
• Suzuki T., Wang J. H. The phosphorylation of purified phospholamban by cyclic AMP-dependent protein kinase is stimulated by phosphatidylinositol. J. Biol. Chem. 1986; 262: 3880–3885
   Google Scholar
• Tada M., Katz A. M. Phosphorylation of-the sarcoplasmic reticulum and sarcolemma. Annu. Rev. Physiol. 1982; 44: 401–423
   PubMed Web of Science ®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
• Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 1979; 76: 4350–4354
   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 phosphorylatable subunits. J. Biol. Chem. 1984; 259: 1834–1841
   PubMedGoogle Scholar
• Wegener A. D., Simmerman H. K. B., Lepnieks 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