메뉴 건너뛰기




Volumn 263, Issue 1, 2004, Pages 131-136

Phosphorylation of phospholamban in ischemia-reperfusion injury: Functional role of Thr17 residue

Author keywords

Ischemia reperfusion; Isolated perfused heart; Phospholamban phosphorylation

Indexed keywords

CALCIUM CHANNEL L TYPE; CALCIUM ION; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; PHOSPHOLAMBAN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; SERINE; SODIUM CALCIUM EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN; THREONINE;

EID: 4544302288     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000041854.72511.14     Document Type: Article
Times cited : (19)

References (21)
  • 1
    • 0034509410 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractile function
    • Brittsan A, Kranias EG: Phospholamban and cardiac contractile function. J Mol Cell Cardiol 32: 2131-2139, 2000
    • (2000) J. Mol. Cell Cardiol. , vol.32 , pp. 2131-2139
    • Brittsan, A.1    Kranias, E.G.2
  • 2
    • 0022857821 scopus 로고
    • 2+ pump and blocking of phospholamban phosphorylation and dephosphorylation by a phospholamban monoclonal antibody
    • 2+ pump and blocking of phospholamban phosphorylation and dephosphorylation by a phospholamban monoclonal antibody. J Biol Chem 261: 7018-7023, 1986
    • (1986) J. Biol. Chem. , vol.261 , pp. 7018-7023
    • Suzuki, T.1    Wang, J.H.2
  • 4
    • 0031702491 scopus 로고    scopus 로고
    • Molecular regulation of phospholamban function and expression
    • Tada M, Toyofuku T: Molecular regulation of phospholamban function and expression. Trends Cardiovasc Med 8: 330-340, 1998
    • (1998) Trends Cardiovasc. Med. , vol.8 , pp. 330-340
    • Tada, M.1    Toyofuku, T.2
  • 6
    • 0030479505 scopus 로고    scopus 로고
    • Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart
    • Mundiña-Weilenmann C, Vittone L, Ortale M, Chiappe de Cingolani, G, 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
    • Mundiña-Weilenmann, C.1    Vittone, L.2    Ortale, M.3    Chiappe de Cingolani, G.4    Mattiazzi, A.5
  • 7
    • 2642614533 scopus 로고    scopus 로고
    • Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart
    • Vittone L, Mundiña-Weilenmann C, Said M, Mattiazzi A: Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart. J Biol Chem 273: 9804-9811, 1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 9804-9811
    • Vittone, L.1    Mundiña-Weilenmann, C.2    Said, M.3    Mattiazzi, A.4
  • 8
    • 0034502334 scopus 로고    scopus 로고
    • Phosphorylation of phospholamban at threonine-17 in the absence and presence of β-adrenergic stimulation in neonatal rat cardiomyocytes
    • Bartel S, Vetter D, Schlegel WP, Wallukat G, Krause EG, Karczewski P: Phosphorylation of phospholamban at threonine-17 in the absence and presence of β-adrenergic stimulation in neonatal rat cardiomyocytes. J Mol Cell Cardiol 32: 2173-2185, 2000
    • (2000) J. Mol. Cell Cardiol. , vol.32 , pp. 2173-2185
    • Bartel, S.1    Vetter, D.2    Schlegel, W.P.3    Wallukat, G.4    Krause, E.G.5    Karczewski, P.6
  • 9
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo W, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG: 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
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 10
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo W, Chu G, Sato Y, Zhou Z, Kadambi VJ, Kranias EG: 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    Chu, G.2    Sato, Y.3    Zhou, Z.4    Kadambi, V.J.5    Kranias, E.G.6
  • 11
    • 0034623718 scopus 로고    scopus 로고
    • 16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to β-agonists
    • 16) 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    Lester, J.W.2    Young, K.B.3    Luo, W.4    Zhai, J.5    Kranias, E.G.6
  • 12
    • 33750888567 scopus 로고    scopus 로고
    • Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning
    • Osada M, Netticadan T, Tamura K, Dhalla NS: Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning. Am J Physiol 274: H2025-H2034, 1998
    • (1998) Am. J. Physiol. , vol.274
    • Osada, M.1    Netticadan, T.2    Tamura, K.3    Dhalla, N.S.4
  • 13
    • 0033194562 scopus 로고    scopus 로고
    • 2+/calmodulin protein kinase phosphorylation of cardiac SR proteins in ischemia-reperfusion
    • 2+/calmodulin protein kinase phosphorylation of cardiac SR proteins in ischemia-reperfusion. Am J Physiol 277: C384-C391, 1999
    • (1999) Am. J. Physiol. , vol.277
    • Netticadan, T.1    Temsah, R.2    Osada, M.3    Dhalla, N.S.4
  • 16
    • 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, Mundiña-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    Mundiña-Weilenmann, C.2    Said, M.3    Ferrero, P.4    Mattiazzi, A.5
  • 17
    • 0000104030 scopus 로고    scopus 로고
    • Role of troponin I proteolysis in the pathogenesis of stunned myocardium
    • Gao WD, Atar D, Liu Y, Pérez NG, Murphy A, Marbán E: Role of troponin I proteolysis in the pathogenesis of stunned myocardium. Circ Res 80: 393-399, 1997
    • (1997) Circ. Res. , vol.80 , pp. 393-399
    • Gao, W.D.1    Atar, D.2    Liu, Y.3    Pérez, N.G.4    Murphy, A.5    Marbán, E.6
  • 18
    • 0030062069 scopus 로고    scopus 로고
    • Effects of acidosis on phosphorylation of phospholamban and troponin I in rat cardiac muscle
    • Mundiña-Weilenmann C, Vittone L, Cingolani H, Orchard C: Effects of acidosis on phosphorylation of phospholamban and troponin I in rat cardiac muscle. Am J Physiol 270: C107-C114, 1996
    • (1996) Am. J. Physiol. , vol.270
    • Mundiña-Weilenmann, C.1    Vittone, L.2    Cingolani, H.3    Orchard, C.4
  • 20
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher DR, Kovacs RJ, Schulman H, Cefali DC, Jones LR: Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 266: 11144-11152, 1991
    • (1991) J. Biol. Chem. , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.