메뉴 건너뛰기




Volumn 47, Issue 36, 2008, Pages 9522-9530

Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINES;

EID: 51549118890     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800880q     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 0016631083 scopus 로고
    • Phospholamban: A regulatory protein of the cardiac sarcoplasmic reticulum
    • Kirchberger, M., Tada, M., and Katz, A. (1975) Phospholamban: a regulatory protein of the cardiac sarcoplasmic reticulum. Recent Adv. Stud. Cardiac Struct. Metab. 5, 103-115.
    • (1975) Recent Adv. Stud. Cardiac Struct. Metab , vol.5 , pp. 103-115
    • Kirchberger, M.1    Tada, M.2    Katz, A.3
  • 3
    • 0027236766 scopus 로고
    • Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases: Effect of phospholamban antibody on enzyme activation
    • Cantilina, T., Sagara, Y., Inesi, G., and Jones, L. R. (1993) Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases: effect of phospholamban antibody on enzyme activation. J. Biol. Chem. 268, 17018-17025.
    • (1993) J. Biol. Chem , vol.268 , pp. 17018-17025
    • Cantilina, T.1    Sagara, Y.2    Inesi, G.3    Jones, L.R.4
  • 4
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban: Identification of phosphorylation sites and two major structural domains
    • Simmerman, H. K. B., Collins, J. H., Theibert, J. L., Wegener, A. D., and Jones, L. R. (1986) Sequence analysis of phospholamban: identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261, 13333-13341.
    • (1986) J. Biol. Chem , vol.261 , pp. 13333-13341
    • Simmerman, H.K.B.1    Collins, J.H.2    Theibert, J.L.3    Wegener, A.D.4    Jones, L.R.5
  • 6
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • Zamoon, J., Mascioni, A., Thomas, D. D., and Veglia, G. (2003) NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles. Biophys. J. 85, 2589-2598.
    • (2003) Biophys. J , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4
  • 7
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid, K., and Chou, J. (2005) The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc. Natl. Acad. Sci. U.S.A. 102, 10870-10875.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.2
  • 10
    • 0035339677 scopus 로고    scopus 로고
    • Cytoplasmic interactions between phospholamban residues 1-20 and the calcium-activated ATPase of the sarcoplasmic reticulum
    • Sharma, P., Patchell, V. B., Gao, Y., Evans, J. S., and Levine, B. A. (2001) Cytoplasmic interactions between phospholamban residues 1-20 and the calcium-activated ATPase of the sarcoplasmic reticulum. Biochem. J. 355, 699-706.
    • (2001) Biochem. J , vol.355 , pp. 699-706
    • Sharma, P.1    Patchell, V.B.2    Gao, Y.3    Evans, J.S.4    Levine, B.A.5
  • 11
    • 0037008735 scopus 로고    scopus 로고
    • 2+ pump revealed by intermolecular thiol cross-linking
    • 2+ pump revealed by intermolecular thiol cross-linking. J. Biol. Chem. 277, 28319-28329.
    • (2002) J. Biol. Chem , vol.277 , pp. 28319-28329
    • Jones, L.R.1    Cornea, R.L.2    Chen, Z.3
  • 12
    • 0348111454 scopus 로고    scopus 로고
    • 2+ pump revealed with use of heterobifunctional cross-linking agents
    • 2+ pump revealed with use of heterobifunctional cross-linking agents. J. Biol. Chem. 278, 48348-48356.
    • (2003) J. Biol. Chem , vol.278 , pp. 48348-48356
    • Chen, Z.1    Stokes, D.L.2    Rice, W.J.3    Jones, L.R.4
  • 15
    • 0034609576 scopus 로고    scopus 로고
    • Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase
    • Karim, C. B., Marquardt, C. G., Stamm, J. D., Barany, B., and Thomas, D. D. (2000) Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase. Biochemistry 39, 10892-10897.
    • (2000) Biochemistry , vol.39 , pp. 10892-10897
    • Karim, C.B.1    Marquardt, C.G.2    Stamm, J.D.3    Barany, B.4    Thomas, D.D.5
  • 16
    • 33746033781 scopus 로고    scopus 로고
    • Rational design of peptide inhibitors of the sarcoplasmic reticulum calcium pump
    • Afara, M., Trieber, C., Glaves, J., and Young, H. (2006) Rational design of peptide inhibitors of the sarcoplasmic reticulum calcium pump. Biochemistry 45, 8617-8627.
    • (2006) Biochemistry , vol.45 , pp. 8617-8627
    • Afara, M.1    Trieber, C.2    Glaves, J.3    Young, H.4
  • 17
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • Simmerman, H. K. B., Kobayashi, Y. M., Autry, J. M., and Jones, L. R. (1996) A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J. Biol. Chem. 271, 5941-5946.
    • (1996) J. Biol. Chem , vol.271 , pp. 5941-5946
    • Simmerman, H.K.B.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 18
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is enhanced by depolymerization
    • Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1997) Phospholamban inhibitory function is enhanced by depolymerization. J. Biol. Chem. 272, 15061-15064.
    • (1997) J. Biol. Chem , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 19
    • 0030905733 scopus 로고    scopus 로고
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J. Biol. Chem. 272, 15872-15880.
    • (1997) J. Biol. Chem , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 22
    • 33744921916 scopus 로고    scopus 로고
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain. J. Biol. Chem. 281, 14163-14172.
    • (2006) J. Biol. Chem , vol.281 , pp. 14163-14172
    • Chen, Z.1    Akin, B.L.2    Stokes, D.L.3    Jones, L.R.4
  • 25
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 26
    • 14644414175 scopus 로고    scopus 로고
    • The effects of mutation on the regulatory properties of phospholamban in co-reconstituted membranes
    • Trieber, C. A., Douglas, J., Afara, M., and Young, H. S. (2005) The effects of mutation on the regulatory properties of phospholamban in co-reconstituted membranes. Biochemistry 44, 3289-3297.
    • (2005) Biochemistry , vol.44 , pp. 3289-3297
    • Trieber, C.A.1    Douglas, J.2    Afara, M.3    Young, H.S.4
  • 27
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma, C., Gratkowski, H., Lear, J. D., and DeGrado, W. F. (2000) Asparagine-mediated self-association of a model transmembrane helix. Nat. Struct. Biol. 7, 161-166.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 29
    • 0026316017 scopus 로고
    • In vivo effect of asparagine in the hydrophobic region of the signal sequence
    • Goldstein, J., Lehnhardt, S., and Inouye, M. (1991) In vivo effect of asparagine in the hydrophobic region of the signal sequence. J. Biol. Chem. 266, 14413-14417.
    • (1991) J. Biol. Chem , vol.266 , pp. 14413-14417
    • Goldstein, J.1    Lehnhardt, S.2    Inouye, M.3
  • 32
    • 0015403570 scopus 로고
    • Phospholipid orientation in sarcoplasmic reticulum membranes: Spin-label ESR and proton NMR studies
    • Eletr, S., and Inesi, G. (1972) Phospholipid orientation in sarcoplasmic reticulum membranes: spin-label ESR and proton NMR studies. Biochim. Biophys. Acta 282, 174-179.
    • (1972) Biochim. Biophys. Acta , vol.282 , pp. 174-179
    • Eletr, S.1    Inesi, G.2
  • 33
    • 0025019294 scopus 로고
    • Three-dimensional crystals of Ca-ATPase from sarcoplasmic reticulum: Symmetry and molecular packing
    • Stokes, D. L., and Green, N. M. (1990) Three-dimensional crystals of Ca-ATPase from sarcoplasmic reticulum: symmetry and molecular packing. Biophys. J. 57, 1-14.
    • (1990) Biophys. J , vol.57 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 35
    • 4244120872 scopus 로고
    • Microdetermination of phosphorous
    • Chen, P. S., Toribara, T. Y., and Warner, H. (1956) Microdetermination of phosphorous. Anal. Chem. 28, 1756-1758.
    • (1956) Anal. Chem , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 36
    • 0023521436 scopus 로고
    • Diffusion of dihydropyridine calcium channel antagonists in cardiac sarcolemmal lipid multibilayers
    • Chester, D. W., Herbette, L. G., Mason, R. P., Joslyn, A. F., and Triggle, D. J. (1987) Diffusion of dihydropyridine calcium channel antagonists in cardiac sarcolemmal lipid multibilayers. Biophys. J. 52, 1021-1030.
    • (1987) Biophys. J , vol.52 , pp. 1021-1030
    • Chester, D.W.1    Herbette, L.G.2    Mason, R.P.3    Joslyn, A.F.4    Triggle, D.J.5
  • 37
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. H., Hass, S. M., Beiber, L. L., and Tolbert, N. E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210.
    • (1978) Anal. Biochem , vol.87 , pp. 206-210
    • Markwell, M.H.1    Hass, S.M.2    Beiber, L.L.3    Tolbert, N.E.4
  • 38
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV Proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV Proteinase. Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 39
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 41
    • 0026752838 scopus 로고
    • 2+-ATPase: Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving detergents
    • 2+-ATPase: mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving detergents. Biochim. Biophys. Acta 1107, 283-298.
    • (1992) Biochim. Biophys. Acta , vol.1107 , pp. 283-298
    • Levy, D.1    Gulik, A.2    Bluzat, A.3    Rigaud, J.-L.4
  • 42
    • 0037461273 scopus 로고    scopus 로고
    • Defining the molecular components of calcium transport regulation in a reconstituted membrane system
    • Reddy, L. G., Cornea, R. L., Winters, D. L., McKenna, E., and Thomas, D. D. (2003) Defining the molecular components of calcium transport regulation in a reconstituted membrane system. Biochemistry 42, 4585-4592.
    • (2003) Biochemistry , vol.42 , pp. 4585-4592
    • Reddy, L.G.1    Cornea, R.L.2    Winters, D.L.3    McKenna, E.4    Thomas, D.D.5
  • 43
    • 0037027332 scopus 로고    scopus 로고
    • Comparable levels of Ca-ATPase inhibition by phospholamban in slow-twitch skeletal and cardiac sarcoplasmic reticulum
    • Ferrington, D., Yao, Q., Squier, T., and Bigelow, D. (2002) Comparable levels of Ca-ATPase inhibition by phospholamban in slow-twitch skeletal and cardiac sarcoplasmic reticulum. Biochemistry 41, 13289-13296.
    • (2002) Biochemistry , vol.41 , pp. 13289-13296
    • Ferrington, D.1    Yao, Q.2    Squier, T.3    Bigelow, D.4
  • 46
    • 0030660411 scopus 로고    scopus 로고
    • Comparison of the kinetic effects of phospholamban phosphorylation and anti-phospholamban monoclonal antibody on the calcium pump in purified cardiac sarcoplasmic reticulum membranes
    • Antipenko, A. Y., Spielman, A. I., Sassaroli, M., and Kirchberger, M. A. (1997) Comparison of the kinetic effects of phospholamban phosphorylation and anti-phospholamban monoclonal antibody on the calcium pump in purified cardiac sarcoplasmic reticulum membranes. Biochemistry 36, 12903-12910.
    • (1997) Biochemistry , vol.36 , pp. 12903-12910
    • Antipenko, A.Y.1    Spielman, A.I.2    Sassaroli, M.3    Kirchberger, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.