메뉴 건너뛰기




Volumn 4, Issue 7, 2003, Pages 566-577

Phospholamban: A crucial regulator of cardiac contractility

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; ADENOSINE TRIPHOSPHATASE (CALCIUM); BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CONTRACTILE PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; ISOPRENALINE; PHOSPHOLAMBAN; RYANODINE RECEPTOR;

EID: 0038464639     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1151     Document Type: Review
Times cited : (849)

References (116)
  • 1
    • 0032498894 scopus 로고    scopus 로고
    • Murine cardiac function: A cautionary tail
    • Kass, D. A., Hare, J. M. & Georgakopoulos, D. Murine cardiac function: a cautionary tail. Circ. Res. 82, 519-522 (1998).
    • (1998) Circ. Res. , vol.82 , pp. 519-522
    • Kass, D.A.1    Hare, J.M.2    Georgakopoulos, D.3
  • 2
    • 0023769896 scopus 로고
    • From epinephrine to cyclic AMR
    • Levitzki, A. From epinephrine to cyclic AMR Science 241, 800-806 (1988).
    • (1988) Science , vol.241 , pp. 800-806
    • Levitzki, A.1
  • 3
    • 0037059457 scopus 로고    scopus 로고
    • Calcium and cardiac rhythms: Physiological and palhophysiological
    • Bers, D. M. Calcium and cardiac rhythms: physiological and palhophysiological. Circ. Res. 90, 14-17 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 14-17
    • Bers, D.M.1
  • 4
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman, H. K. & Jones, L. R. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78, 921-947 (1998).
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 6
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura, Y., Kurzydlowski, K., Tada, M. & MacLennan, D. H. Phospholamban inhibitory function is activated by depolymerization. J. Biol. Chem. 272, 15061-15064 (1997). Scanning mutagenesis of the PLN transmembrane helix shows two faces: one interacts with SERCA, so that mutants remain pentameric but lose Inhibitory function; the other interacts with PLN, so that mutants become monomeric and gain inhibitory function. It is deduced that the PLN monomer is the active inhibitory species.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 7
    • 0034616217 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo
    • Zhai, J. et al. Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo. J. Biol. Chem. 275, 10538-10544 (2000). Superinhibition of SERCA2a by a PLN mutant results in dilated cardiomyopathy in a mouse model.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10538-10544
    • Zhai, J.1
  • 8
    • 0034685881 scopus 로고    scopus 로고
    • The transgenic expression of highly inhibitory monomeric forms of phospholamban in mouse heart impairs cardiac contractility
    • Zvaritch, E. et al. The transgenic expression of highly inhibitory monomeric forms of phospholamban in mouse heart impairs cardiac contractility. J. Biol. Chem. 275, 14985-14991 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14985-14991
    • Zvaritch, E.1
  • 9
    • 0035968264 scopus 로고    scopus 로고
    • Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure
    • Haghighi, K. et al. Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure. J. Biol. Chem. 276, 24145-24152 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24145-24152
    • Haghighi, K.1
  • 10
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo, W. et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ. Res. 75, 401-409 (1994). The first clear evidence of the important role of PLN in the regulation of cardiac contractility in a whole animal.
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.1
  • 11
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi, J. et al. Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J. Clin. Invest. 97, 533-539 (1996). Only about 40% of SERCA2a molecules are inhibited by PLN under normal conditions, even though PLN is in molar excess over SERCA2a.
    • (1996) J. Clin. Invest. , vol.97 , pp. 533-539
    • Kadambi, J.1
  • 12
    • 0029830352 scopus 로고    scopus 로고
    • Phospholamban: A prominent regulator of myocardial contractility
    • Koss, K. L. & Kranias, E. G. Phospholamban: a prominent regulator of myocardial contractility. Circ. Res. 79, 1059-1063 (1996).
    • (1996) Circ. Res. , vol.79 , pp. 1059-1063
    • Koss, K.L.1    Kranias, E.G.2
  • 13
    • 0033615645 scopus 로고    scopus 로고
    • Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy
    • Minamisawa, S. et al. Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy. Cell 99, 313-322 (1999). PLN ablation can reverse heart failure in a cardiomyopathic mouse model that is induced by a mutation in a structural protein.
    • (1999) Cell , vol.99 , pp. 313-322
    • Minamisawa, S.1
  • 14
    • 0033621151 scopus 로고    scopus 로고
    • 2+-ATPase activity and cardiac myocyte contractility
    • 2+-ATPase activity and cardiac myocyte contractility. Circulation 100, 974-980 (1999).
    • (1999) Circulation , vol.100 , pp. 974-980
    • He, H.1
  • 15
    • 0036341380 scopus 로고    scopus 로고
    • Chronic suppression of heart-failure progression by a pseudophosphorylated mutant of phospholamban via in vivo cardiac rAAV gene delivery
    • Hoshijima, M. et al. Chronic suppression of heart-failure progression by a pseudophosphorylated mutant of phospholamban via in vivo cardiac rAAV gene delivery. Nature Med. 8, 864-871 (2002).
    • (2002) Nature Med. , vol.8 , pp. 864-871
    • Hoshijima, M.1
  • 16
    • 0037470512 scopus 로고    scopus 로고
    • Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban
    • Schmitt, J. P. et al. Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban. Science 299, 1410-1413 (2003). A human PLN mutation that is associated with heart failure in man inhibits PKA, leading to a lack of PLN phosphorylation and chronic inhibition of SERCA2a.
    • (2003) Science , vol.299 , pp. 1410-1413
    • Schmitt, J.P.1
  • 17
    • 85047687537 scopus 로고    scopus 로고
    • Human phospholamban null results in lethal dilated cardiomyopathy: Critical difference between mouse and man
    • Haghighi, K. et al. Human phospholamban null results in lethal dilated cardiomyopathy: critical difference between mouse and man. J. Clin. Invest. 111, 869-876 (2003). In contrast to the beneficial effects of PLN ablation in mice, the absence of PLN in man might be associated with heart failure.
    • (2003) J. Clin. Invest. , vol.111 , pp. 869-876
    • Haghighi, K.1
  • 18
    • 0015450657 scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate-dependent protein kinase stimulation of calcium uptake by canine cardiac microsomes
    • Kirchberger, M. A., Tada, M., Repke, D. I. & Katz, A. M. Cyclic adenosine 3′,5′-monophosphate-dependent protein kinase stimulation of calcium uptake by canine cardiac microsomes. J. Mol. Cell. Cardiol. 4, 673-680 (1972).
    • (1972) J. Mol. Cell. Cardiol. , vol.4 , pp. 673-680
    • Kirchberger, M.A.1    Tada, M.2    Repke, D.I.3    Katz, A.M.4
  • 19
    • 0031794676 scopus 로고    scopus 로고
    • Discovery of phospholamban. A personal history
    • Ketz, A. M. Discovery of phospholamban. A personal history. Ann. NY Acad. Sci. 853, 9-19 (1998).
    • (1998) Ann. NY Acad. Sci. , vol.853 , pp. 9-19
    • Ketz, A.M.1
  • 20
    • 0016689752 scopus 로고
    • Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase
    • 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. 250, 2640-2647 (1975). Identification of PLN as a crucial player in β-adrenergic stimulation of the heart.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2640-2647
    • Tada, M.1    Kirchberger, M.A.2    Katz, A.M.3
  • 21
    • 0016280110 scopus 로고
    • Adenosine 3′,5′-monophosphate dependent membrane phosphorylation: A possible mechanism for the control of microsomal calcium transport in heart muscle
    • La Raia, 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. 35, 298-306 (1974).
    • (1974) Circ. Res. , vol.35 , pp. 298-306
    • La Raia, P.J.1    Morkin, E.2
  • 24
    • 0020477578 scopus 로고
    • Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart
    • Kranias, E. G. & Solaro, R. J. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature 298, 182-184 (1982). PLN is phosphorylated when elevated levels of catecholamines stimulate contractility of intact hearts.
    • (1982) Nature , vol.298 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 25
    • 0024360671 scopus 로고
    • Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation
    • Wegener, A. D., Simmerman, H. K., Lindemann, J. P. & Jones, L. R. Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation. J. Biol. Chem. 264, 11468-11474 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 11468-11474
    • Wegener, A.D.1    Simmerman, H.K.2    Lindemann, J.P.3    Jones, L.R.4
  • 26
    • 0027480875 scopus 로고
    • Intracellular mechanisms mediating reversal of β-adrenergic stimulation in intact beating hearts
    • Talosi, L., Edes, L. & Kranias, E. G. Intracellular mechanisms mediating reversal of β-adrenergic stimulation in intact beating hearts. Am. J. Physiol. 264, H791-H797 (1993).
    • (1993) Am. J. Physiol. , vol.264
    • Talosi, L.1    Edes, L.2    Kranias, E.G.3
  • 28
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts
    • Garvey, J. L., Kranias, E. G. & Solaro, R. J. Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. Biochem. J. 249, 709-714 (1988).
    • (1988) Biochem. J. , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 29
    • 0030479505 scopus 로고    scopus 로고
    • Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart
    • Mundina-Weilenmann, C., Vittone, L., Ortale, M., de Cingolani, G. C. & Mattiazzi, A. Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart. J. Biol. Chem. 271, 33561-33567 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 33561-33567
    • Mundina-Weilenmann, C.1    Vittone, L.2    Ortale, M.3    De Cingolani, G.C.4    Mattiazzi, A.5
  • 30
    • 0023119953 scopus 로고
    • Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban
    • Fujii, J. et al. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. J. Clin. Invest. 79, 301-304 (1987).
    • (1987) J. Clin. Invest. , vol.79 , pp. 301-304
    • Fujii, J.1
  • 31
    • 0031281867 scopus 로고    scopus 로고
    • Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: Absence of structural mutations in five patients with Brody disease
    • Odermatt, A. et al. Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease. Genomics 45, 541-553 (1997).
    • (1997) Genomics , vol.45 , pp. 541-553
    • Odermatt, A.1
  • 32
  • 33
    • 0028999102 scopus 로고
    • Solution structure of the cytoplasmic domain of phopholamban: Phosphorylation leads to a local perturbation in secondary structure
    • Mortishire-Smith, R. J. et al. Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure. Biochemistry 34, 7603-7613 (1995).
    • (1995) Biochemistry , vol.34 , pp. 7603-7613
    • Mortishire-Smith, R.J.1
  • 34
    • 0033040491 scopus 로고    scopus 로고
    • Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer
    • Pollesello, P., Annila, A. & Ovaska, M. Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer. Biophys. J. 76, 1784-1795 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 1784-1795
    • Pollesello, P.1    Annila, A.2    Ovaska, M.3
  • 35
    • 0033783112 scopus 로고    scopus 로고
    • NMR structure of phospholamban
    • Lamberth, S. et al. NMR structure of phospholamban. Helvetica Chimica Acta 83, 2141-2152 (2000).
    • (2000) Helvetica Chimica Acta , vol.83 , pp. 2141-2152
    • Lamberth, S.1
  • 36
    • 0037080181 scopus 로고    scopus 로고
    • Structure and orientation of sarcolipin in lipid environments
    • Mascioni, A., Karim, C., Barany, G., Thomas, D. D. & Veglia, G. Structure and orientation of sarcolipin in lipid environments. Biochemistry 41, 475-482 (2002).
    • (2002) Biochemistry , vol.41 , pp. 475-482
    • Mascioni, A.1    Karim, C.2    Barany, G.3    Thomas, D.D.4    Veglia, G.5
  • 38
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 39
    • 0027405626 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban
    • 2+-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban. J. Biol. Chem. 268, 2809-2815 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 2809-2815
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 40
    • 0032755399 scopus 로고    scopus 로고
    • 2+-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites
    • 2+-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites. J. Biol. Chem. 274, 32855-32862 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32855-32862
    • Asahi, M.1    Kimura, Y.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 41
    • 0028168416 scopus 로고
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J. Biol. Chem. 269, 22929-22932 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 44
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane α-helices of phospholamban, a cardiac ion channel
    • Arkin, I. T. et al. Structural organization of the pentameric transmembrane α-helices of phospholamban, a cardiac ion channel. EMBO J. 13, 4757-4764 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4757-4764
    • Arkin, I.T.1
  • 45
    • 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., Kobayashi, Y. M., Autry, J. M. & Jones, L. R. A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J. Biol. Chem. 271, 5941-5946 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 5941-5946
    • Simmerman, H.K.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 46
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams, P. D., Arkin, I. T., Engelman, D. M. & Brunger, A. T. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Struct. Biol. 2, 154-162 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 47
    • 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).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 50
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (2000).
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 51
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R. et al. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420 (1991).
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1
  • 52
    • 12244255136 scopus 로고    scopus 로고
    • A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics
    • Hutter, M. C. et al. A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics. Chembiochem. 3, 1200-1208 (2002).
    • (2002) Chembiochem. , vol.3 , pp. 1200-1208
    • Hutter, M.C.1
  • 54
    • 9244255361 scopus 로고    scopus 로고
    • Phospholamban gene dosage effects in the mammalian heart
    • Luo, W. et al. Phospholamban gene dosage effects in the mammalian heart. Circ. Res. 78, 839-847 (1996).
    • (1996) Circ. Res. , vol.78 , pp. 839-847
    • Luo, W.1
  • 56
    • 0031922664 scopus 로고    scopus 로고
    • Cardiac myocyte calcium transport in phospholamban knockout mouse: Relaxation and endogenous CaMKII effects
    • Li, L., Chu, G., Kranias, E. G. & Bers, D. M. Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects. Am. J. Physiol. 274, H1335-H1347 (1998).
    • (1998) Am. J. Physiol. , vol.274
    • Li, L.1    Chu, G.2    Kranias, E.G.3    Bers, D.M.4
  • 57
    • 33750702216 scopus 로고    scopus 로고
    • Regulatory effects of phospholamban on cardiac function in intact mice
    • Lorenz, J. N. & Kranias, E. G. Regulatory effects of phospholamban on cardiac function in intact mice. Am. J. Physiol. 273, H2826-H2831 (1997).
    • (1997) Am. J. Physiol. , vol.273
    • Lorenz, J.N.1    Kranias, E.G.2
  • 58
    • 33750879037 scopus 로고    scopus 로고
    • 5-Adrenergic regulation of cAMP and protein phosphorylation in phospholamban-knockout mouse hearts
    • Kiss, E. et al. 5-adrenergic regulation of cAMP and protein phosphorylation in phospholamban-knockout mouse hearts. Am. J. Physiol. 272, H785-H790 (1997).
    • (1997) Am. J. Physiol. , vol.272
    • Kiss, E.1
  • 59
    • 0031283324 scopus 로고    scopus 로고
    • Amount of calcium in the sarcoplasmic reticulum: Influence on excitation-contraction coupling in heart muscle
    • Santana, L. F., Gomez, A. M., Kranias, E. G. & Lederer, W. J. Amount of calcium in the sarcoplasmic reticulum: influence on excitation-contraction coupling in heart muscle. Heart Vessels Suppl. 12, 44-49 (1997).
    • (1997) Heart Vessels , Issue.SUPPL. 12 , pp. 44-49
    • Santana, L.F.1    Gomez, A.M.2    Kranias, E.G.3    Lederer, W.J.4
  • 61
    • 10544246896 scopus 로고    scopus 로고
    • Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts
    • Chu, G. et al. Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts. Circ. Res. 79, 1064-1076 (1996).
    • (1996) Circ. Res. , vol.79 , pp. 1064-1076
    • Chu, G.1
  • 63
    • 0034973920 scopus 로고    scopus 로고
    • The enhanced contractility of the phospholamban-deficient mouse heart persists with aging
    • Slack, J. P. et al. The enhanced contractility of the phospholamban-deficient mouse heart persists with aging. J. Mol. Cell. Cardiol. 33, 1031-1040 (2001).
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1031-1040
    • Slack, J.P.1
  • 64
    • 0036164401 scopus 로고    scopus 로고
    • Hypertrophy and functional alterations in hyperdynamic phospholamban-knockout mouse hearts under chronic aortic stenosis
    • Kiriazis, H. et al. Hypertrophy and functional alterations in hyperdynamic phospholamban-knockout mouse hearts under chronic aortic stenosis. Cardiovasc. Res. 53, 372-381 (2002).
    • (2002) Cardiovasc. Res. , vol.53 , pp. 372-381
    • Kiriazis, H.1
  • 65
    • 0037307565 scopus 로고    scopus 로고
    • Ablation of PLB exacerbates ischemic injury to a lesser extent in female than male mice: Protective role of NO
    • Cross, H. R., Kranias, E. G., Murphy, E. & Steenbergen, C. Ablation of PLB exacerbates ischemic injury to a lesser extent in female than male mice: protective role of NO. Am. J. Physiol. Heart Circ. Physiol. 284, H683-H690 (2003).
    • (2003) Am. J. Physiol. Heart Circ. Physiol. , vol.284
    • Cross, H.R.1    Kranias, E.G.2    Murphy, E.3    Steenbergen, C.4
  • 66
    • 0030910704 scopus 로고    scopus 로고
    • Targeted ablation of the phospholamban gene is assodated with a marked decrease in sensitivity in aortic smooth muscle
    • Lalli, J., Harrer, J. M., Luo, W., Kranias, E. G. & Paul, R. J. Targeted ablation of the phospholamban gene is assodated with a marked decrease in sensitivity in aortic smooth muscle. Circ. Res. 80, 506-513 (1997).
    • (1997) Circ. Res. , vol.80 , pp. 506-513
    • Lalli, J.1    Harrer, J.M.2    Luo, W.3    Kranias, E.G.4    Paul, R.J.5
  • 67
    • 0030838634 scopus 로고    scopus 로고
    • Phospholamban ablation enhances relaxation in the murine soleus
    • Slack, J. P., Grupp, I. L., Luo, W. & Kranias, E. G. Phospholamban ablation enhances relaxation in the murine soleus. Am. J. Physiol. 273, C1-C6 (1997).
    • (1997) Am. J. Physiol. , vol.273
    • Slack, J.P.1    Grupp, I.L.2    Luo, W.3    Kranias, E.G.4
  • 68
    • 0035884612 scopus 로고    scopus 로고
    • Phospholamban regulation of bladder contractility: Evidence from gene-altered mouse models
    • Nobe, K., Sutliff, R. L., Kranias, E. G. & Paul, R. J. Phospholamban regulation of bladder contractility: evidence from gene-altered mouse models. J. Physiol. 535, 867-878 (2001).
    • (2001) J. Physiol. , vol.535 , pp. 867-878
    • Nobe, K.1    Sutliff, R.L.2    Kranias, E.G.3    Paul, R.J.4
  • 69
    • 0033006097 scopus 로고    scopus 로고
    • Phospholamban is present in endothelial cells and modulates endothelium-dependent relaxation. Evidence from phospholamban gene-ablated mice
    • Sutliff, R. L., Hoying, J. B., Kadambi, V. J., Kranias, E. G. & Paul, R. J. Phospholamban is present in endothelial cells and modulates endothelium-dependent relaxation. Evidence from phospholamban gene-ablated mice. Circ. Res. 84, 360-364 (1999).
    • (1999) Circ. Res. , vol.84 , pp. 360-364
    • Sutliff, R.L.1    Hoying, J.B.2    Kadambi, V.J.3    Kranias, E.G.4    Paul, R.J.5
  • 70
    • 0035852663 scopus 로고    scopus 로고
    • Interactions between phospholamban and β-adrenergic drive may lead to cardiomyopathy and early mortality
    • Dash, R. et al. Interactions between phospholamban and β-adrenergic drive may lead to cardiomyopathy and early mortality. Circulation 103, 889-896 (2001).
    • (2001) Circulation , vol.103 , pp. 889-896
    • Dash, R.1
  • 72
    • 0025947645 scopus 로고
    • Dependence of cardiac sarcoplasmic reticulum calcium pump activity on the phosphorylation status of phospholamban
    • Colyer, J. & Wang, J. H. Dependence of cardiac sarcoplasmic reticulum calcium pump activity on the phosphorylation status of phospholamban. J. Biol. Chem. 266, 17486-17493 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 17486-17493
    • Colyer, J.1    Wang, J.H.2
  • 73
    • 0034697029 scopus 로고    scopus 로고
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban. J. Biol. Chem. 275, 12129-12135 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 12129-12135
    • Brittsan, A.G.1    Carr, A.N.2    Schmidt, A.G.3    Kranias, E.G.4
  • 74
    • 0036839002 scopus 로고    scopus 로고
    • 2+ uptake as a primary cause of heart failure
    • 2+ uptake as a primary cause of heart failure. Cardiovasc. Res. 56, 248-259 (2002).
    • (2002) Cardiovasc. Res. , vol.56 , pp. 248-259
    • Schmidt, A.G.1
  • 75
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo, W. et al. Transgenic approaches to define the functional role of dual site phospholamban phosphorylation. J. Biol. Chem. 273, 4734-4739 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4734-4739
    • Luo, W.1
  • 76
    • 0034623718 scopus 로고    scopus 로고
    • A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to β-agonists
    • Chu, G. et al. A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to β-agonists. J. Biol. Chem. 275, 38938-38943 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38938-38943
    • Chu, G.1
  • 77
    • 0036169814 scopus 로고    scopus 로고
    • Time course and mechanisms of phosphorylation of phospholamban residues in ischemia-reperfused rat hearts. Dissociation of phospholamban phosphorylation pathways
    • Vittone, L., Mundina-Weilenmann, C., Said, M., Ferrero, P. & Mattiazzi, A. Time course and mechanisms of phosphorylation of phospholamban residues in ischemia-reperfused rat hearts. Dissociation of phospholamban phosphorylation pathways. J. Mol. Cell. Cardiol. 34, 39-50 (2002).
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 39-50
    • Vittone, L.1    Mundina-Weilenmann, C.2    Said, M.3    Ferrero, P.4    Mattiazzi, A.5
  • 78
    • 0034697901 scopus 로고    scopus 로고
    • Frequency-encoding Thr17 phospholamban phesphorylation is independent of Ser16 phosphorylation in cardiac myocytes
    • Hagemann, D. et al. Frequency-encoding Thr17 phospholamban phesphorylation is independent of Ser16 phosphorylation in cardiac myocytes. J. Biol. Chem. 275, 22532-22536 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 22532-22536
    • Hagemann, D.1
  • 79
    • 0026542534 scopus 로고
    • Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure
    • Beuckelmann, D. J., Nabauer, M. & Erdmann, E. Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure. Circulation 85, 1046-1055 (1992).
    • (1992) Circulation , vol.85 , pp. 1046-1055
    • Beuckelmann, D.J.1    Nabauer, M.2    Erdmann, E.3
  • 81
    • 0028101383 scopus 로고
    • 2+-ATPase in failing and nonfailing human myocardium
    • 2+-ATPase in failing and nonfailing human myocardium. Circ. Res. 75, 434-442 (1994).
    • (1994) Circ. Res. , vol.75 , pp. 434-442
    • Hasenfuss, G.1
  • 82
    • 0028882650 scopus 로고
    • 2+-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts
    • 2+-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts. Circulation 92, 3220-3228 (1995).
    • (1995) Circulation , vol.92 , pp. 3220-3228
    • Schwinger, R.H.1
  • 83
    • 0031739443 scopus 로고    scopus 로고
    • Frequency dependent force generation correlates with sarcoplasmic calcium ATPase activity in human myocardium
    • Frank, K., Bolck, B., Bavendiek, U., & Schwinger, R. H. Frequency dependent force generation correlates with sarcoplasmic calcium ATPase activity in human myocardium. Basic Res. Cardiol. 93, 405-411 (1998).
    • (1998) Basic Res. Cardiol. , vol.93 , pp. 405-411
    • Frank, K.1    Bolck, B.2    Bavendiek, U.3    Schwinger, R.H.4
  • 84
    • 0028100606 scopus 로고
    • 2+-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium
    • 2+-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium. Circulation 90, 653-657 (1994).
    • (1994) Circulation , vol.90 , pp. 653-657
    • Movsesian, M.A.1    Karimi, M.2    Green, K.3    Jones, L.R.4
  • 85
    • 0029092577 scopus 로고
    • Alterations of sarcoplasmic reticulum proteins in failing human dilated cardiomyopathy
    • Meyer, M. et al. Alterations of sarcoplasmic reticulum proteins in failing human dilated cardiomyopathy. Circulation 92, 778-784 (1995).
    • (1995) Circulation , vol.92 , pp. 778-784
    • Meyer, M.1
  • 86
    • 0033105384 scopus 로고    scopus 로고
    • 2+-sensitivity of SERCA2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation
    • 2+-sensitivity of SERCA2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation. J. Mol. Cell. Cardiol. 31, 479-491 (1999).
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 479-491
    • Schwinger, R.H.1
  • 87
  • 88
    • 0033534053 scopus 로고    scopus 로고
    • Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a
    • del Monte, F. et al. Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a. Circulation 100, 2308-2311 (1999).
    • (1999) Circulation , vol.100 , pp. 2308-2311
    • Del Monte, F.1
  • 89
    • 12944332074 scopus 로고    scopus 로고
    • Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure
    • Miyamoto, M. I. et al. Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure. Proc. Natl Acad. Sci. USA 97, 793-798 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 793-798
    • Miyamoto, M.I.1
  • 90
    • 0035908945 scopus 로고    scopus 로고
    • 2+-ATPase in a rat model of heart failure
    • 2+-ATPase in a rat model of heart failure. Circulation 104, 1424-1429 (2001).
    • (2001) Circulation , vol.104 , pp. 1424-1429
    • Del Monte, F.1
  • 91
    • 0030805905 scopus 로고    scopus 로고
    • 2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation
    • 2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation. J. Clin. Invest. 100, 380-389 (1997).
    • (1997) J. Clin. Invest. , vol.100 , pp. 380-389
    • He, H.1
  • 92
    • 0032576586 scopus 로고    scopus 로고
    • 2+-ATPase increases cardiac contractility in transgenic mouse hearts
    • 2+-ATPase increases cardiac contractility in transgenic mouse hearts. Circ. Res. 83, 1205-1214 (1998).
    • (1998) Circ. Res. , vol.83 , pp. 1205-1214
    • Baker, D.L.1
  • 93
    • 0034624993 scopus 로고    scopus 로고
    • Adenovirus-based phospholamban antisense expression as a novel approach to improve cardiac contractile dysfunction: Comparison of a constitutive viral versus an endothelin-1-responsive cardiac promoter
    • Eizema, K. et al. Adenovirus-based phospholamban antisense expression as a novel approach to improve cardiac contractile dysfunction: comparison of a constitutive viral versus an endothelin-1-responsive cardiac promoter. Circulation 101, 2193-2199 (2000).
    • (2000) Circulation , vol.101 , pp. 2193-2199
    • Eizema, K.1
  • 95
    • 0035937762 scopus 로고    scopus 로고
    • Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation
    • Sato, Y. et al. Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation. J. Biol. Chem. 278, 9392-9399 (2001).
    • (2001) J. Biol. Chem. , vol.278 , pp. 9392-9399
    • Sato, Y.1
  • 96
    • 0035048223 scopus 로고    scopus 로고
    • Alterations in cardiac adrenergic signaling and calcium cycling differentially affect the progression of cardiomyopathy
    • Freeman, K. et al. Alterations in cardiac adrenergic signaling and calcium cycling differentially affect the progression of cardiomyopathy. J. Clin. Invest. 107, 967-974 (2001).
    • (2001) J. Clin. Invest. , vol.107 , pp. 967-974
    • Freeman, K.1
  • 97
    • 0037362850 scopus 로고    scopus 로고
    • Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy
    • Song, Q. et al. Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy. J. Clin. Invest. 111, 859-867 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 859-867
    • Song, Q.1
  • 98
    • 0035895592 scopus 로고    scopus 로고
    • AKAP-mediated targeting of protein kinase a regulates contractility in cardiac myocytes
    • Fink, M. A. et al. AKAP-mediated targeting of protein kinase a regulates contractility in cardiac myocytes. Circ. Res. 88, 291-297 (2001).
    • (2001) Circ. Res. , vol.88 , pp. 291-297
    • Fink, M.A.1
  • 99
    • 0033551089 scopus 로고    scopus 로고
    • Functional effects of endothelin and regulation of endothelin receptors in isolated human nonfailing and failing myocardium
    • Pieske, B. et al. Functional effects of endothelin and regulation of endothelin receptors in isolated human nonfailing and failing myocardium. Circulation 99, 1802-1809 (1999).
    • (1999) Circulation , vol.99 , pp. 1802-1809
    • Pieske, B.1
  • 101
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot, A. S. & Potter, J. D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16, 535-559 (1987).
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 102
    • 0033624484 scopus 로고    scopus 로고
    • 2+ signalling and muscle disease
    • 2+ signalling and muscle disease. Eur. J. Biochem. 267, 5291-5297 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5291-5297
    • MacLennan, D.H.1
  • 104
    • 0035895322 scopus 로고    scopus 로고
    • Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia
    • Priori, S. G. et al. Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia. Circulation 103, 196-200 (2001).
    • (2001) Circulation , vol.103 , pp. 196-200
    • Priori, S.G.1
  • 105
    • 0035969990 scopus 로고    scopus 로고
    • Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia
    • Laitinen, P. J. et al. Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia. Circulation 103, 485-490 (2001).
    • (2001) Circulation , vol.103 , pp. 485-490
    • Laitinen, P.J.1
  • 106
    • 0037131020 scopus 로고    scopus 로고
    • Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia
    • Postma, A. V. et al. Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia. Circ. Res. 91, e21-e26 (2002).
    • (2002) Circ. Res. , vol.91
    • Postma, A.V.1
  • 107
    • 0032978357 scopus 로고    scopus 로고
    • 2+ pump, cause Darier disease
    • 2+ pump, cause Darier disease. Nature Genet. 21, 271-277 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 271-277
    • Sakuntabhai, A.1
  • 108
    • 0026450976 scopus 로고
    • Sarcolipin, the 'proteolipid' of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide
    • Wawrzynow, A. et al. Sarcolipin, the 'proteolipid' of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch. Biochem. Biophys. 298, 620-623 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 620-623
    • Wawrzynow, A.1
  • 109
    • 0034656175 scopus 로고    scopus 로고
    • Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm
    • Gayan-Ramirez, G., Vanzeir, L., Wuytack, F. & Decramer, M. Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm. J. Physiol. 524, 387-397 (2000).
    • (2000) J. Physiol. , vol.524 , pp. 387-397
    • Gayan-Ramirez, G.1    Vanzeir, L.2    Wuytack, F.3    Decramer, M.4
  • 110
    • 0038237303 scopus 로고    scopus 로고
    • Atrial-specific expression of sarcolipin is regulated during development and hypertrophic remodeling
    • Minamisawa, S. et al. Atrial-specific expression of sarcolipin is regulated during development and hypertrophic remodeling. J. Biol. Chem. 278, 9570-9575 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 9570-9575
    • Minamisawa, S.1
  • 113
    • 0038031808 scopus 로고    scopus 로고
    • 2+-ATPase (SERCA1a) by binding to transmembrane helices alone or in association with phospholamban
    • 2+-ATPase (SERCA1a) by binding to transmembrane helices alone or in association with phospholamban. Proc. Natl Acad. Sci. USA 100, 5040-5045 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5040-5045
    • Asahi, M.1
  • 114
    • 0018401053 scopus 로고
    • 2+-dependent ATPase of the sarcoplasmic reticulum
    • 2+-dependent ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 48, 275-293 (1979).
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-293
    • De Meis, L.1    Vianna, A.L.2
  • 116
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • Cornea, R. L., Jones, L. R., Autry, J. M. & Thomas, D. D. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 36, 2960-2967 (1997).
    • (1997) Biochemistry , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.