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Volumn 293, Issue 5, 2007, Pages

Triadin is a critical determinant of cellular Ca cycling and contractility in the heart

Author keywords

adrenergic receptor stimulation; Ca signaling; Cardiac function; Force frequency relationship; Hypertrophy; Sarcoplasmic reticulum; Transgenic mice

Indexed keywords

BETA ADRENERGIC RECEPTOR; CAFFEINE; CALCIUM; ISOPRENALINE; JUNCTIN; PROTEIN; TRIADIN; UNCLASSIFIED DRUG;

EID: 36148929388     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00799.2007     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 0028300397 scopus 로고
    • Relaxation in rabbit and rat cardiac cells - species-dependent differences in cellular mechanisms
    • Bassani JWM, Bassani RA, Bers DM. Relaxation in rabbit and rat cardiac cells - species-dependent differences in cellular mechanisms. J Physiol 476: 279-293, 1994.
    • (1994) J Physiol , vol.476 , pp. 279-293
    • Bassani, J.W.M.1    Bassani, R.A.2    Bers, D.M.3
  • 2
    • 0029029280 scopus 로고
    • Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani JWM, Yuan WL, Bers DM. Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am J Physiol Cell Physiol 268: C1313-C1319, 1995.
    • (1995) Am J Physiol Cell Physiol , vol.268
    • Bassani, J.W.M.1    Yuan, W.L.2    Bers, D.M.3
  • 3
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers DM. Cardiac excitation-contraction coupling. Nature 415: 198-205, 2002.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 6
    • 0034463866 scopus 로고    scopus 로고
    • Chronic elevation of calmodulin in the ventricles of transgenic mice increases the autonomous activity of calmodulin-dependent protein kinase II, which regulates atrial natriuretic factor gene expression
    • Colomer JM, Means AR. Chronic elevation of calmodulin in the ventricles of transgenic mice increases the autonomous activity of calmodulin-dependent protein kinase II, which regulates atrial natriuretic factor gene expression. Mol Endocrinol 14: 1125-1136, 2000.
    • (2000) Mol Endocrinol , vol.14 , pp. 1125-1136
    • Colomer, J.M.1    Means, A.R.2
  • 7
    • 34548014295 scopus 로고    scopus 로고
    • Tuning cardiac performance in ischemic heart disease and failure by modulating myofilament function
    • Day S, Westfall M, Metzger J. Tuning cardiac performance in ischemic heart disease and failure by modulating myofilament function. J Mol Med 85: 911-921, 2007.
    • (2007) J Mol Med , vol.85 , pp. 911-921
    • Day, S.1    Westfall, M.2    Metzger, J.3
  • 11
    • 0025822785 scopus 로고
    • Isolation and characterization of the mouse cardiac myosin heavy-chain genes
    • Gulick J, Subramaniam A, Neumann J, Robbins J. Isolation and characterization of the mouse cardiac myosin heavy-chain genes. J Biol Chem 266: 9180-9185, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 9180-9185
    • Gulick, J.1    Subramaniam, A.2    Neumann, J.3    Robbins, J.4
  • 12
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Gyorke I, Hester N, Jones LR, Gyorke S. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 86: 2121-2128, 2004.
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 15
    • 0027322997 scopus 로고
    • 2+ transport ATPase of cardiac sarcoplasmic reticulum
    • 2+ transport ATPase of cardiac sarcoplasmic reticulum. J Biol Chem 268: 11486-11488, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11486-11488
    • Jones, L.R.1    Field, L.J.2
  • 17
    • 0029618249 scopus 로고
    • Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum
    • Jones LR, Zhang L, Sanborn K, Jorgensen AO, Kelley J. Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum. J Biol Chem 270: 30787-30796, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 30787-30796
    • Jones, L.R.1    Zhang, L.2    Sanborn, K.3    Jorgensen, A.O.4    Kelley, J.5
  • 24
    • 0034625374 scopus 로고    scopus 로고
    • Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction
    • Kobayashi YM, Alseikhan BA, Jones LR. Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction. J Biol Chem 275: 17639-17646, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17639-17646
    • Kobayashi, Y.M.1    Alseikhan, B.A.2    Jones, L.R.3
  • 25
    • 0033214441 scopus 로고    scopus 로고
    • Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium
    • Kobayashi YM, Jones LR. Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium. J Biol Chem 274: 28660-28668, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 28660-28668
    • Kobayashi, Y.M.1    Jones, L.R.2
  • 28
    • 0031922664 scopus 로고    scopus 로고
    • Cardiac myocyte calcium transport in phospholamban knockout mouse: Relaxation and endogenous CaMKII effects
    • Li L, Chu GX, Kranias EG, Bers DM. Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects. Am J Physiol Heart Circ Physiol 274: H1335-H1347, 1998.
    • (1998) Am J Physiol Heart Circ Physiol , vol.274
    • Li, L.1    Chu, G.X.2    Kranias, E.G.3    Bers, D.M.4
  • 29
    • 0023002371 scopus 로고
    • Developmental changes in cardiac sarcoplasmic reticulum in sheep
    • Mahony L, Jones LR. Developmental changes in cardiac sarcoplasmic reticulum in sheep. J Biol Chem 261: 15257-15265, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 15257-15265
    • Mahony, L.1    Jones, L.R.2
  • 30
    • 33846858884 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase (CaMK) in excitation-contraction coupling in the heart
    • 2+/calmodulin-dependent protein kinase (CaMK) in excitation-contraction coupling in the heart. Cardiovasc Res 73: 631-640, 2007.
    • (2007) Cardiovasc Res , vol.73 , pp. 631-640
    • Maier, L.S.1    Bers, D.M.2
  • 32
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks AR. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 101: 365-376, 2000.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Jayaraman, T.4    Burkhoff, D.5    Rosemblit, N.6    Marks, A.R.7
  • 36
    • 0035216866 scopus 로고    scopus 로고
    • Calcium signaling mechanisms in dedifferentiated cardiac myocytes: Comparison with neonatal and adult cardiomyocytes
    • Poindexter BJ, Smith JR, Buja LM, Bick RJ. Calcium signaling mechanisms in dedifferentiated cardiac myocytes: comparison with neonatal and adult cardiomyocytes. Cell Calcium 30: 373-382, 2001.
    • (2001) Cell Calcium , vol.30 , pp. 373-382
    • Poindexter, B.J.1    Smith, J.R.2    Buja, L.M.3    Bick, R.J.4
  • 37
    • 0017342054 scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Porzio MA, Pearson AM. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim Biophys Acta 490: 27-34, 1977.
    • (1977) Biochim Biophys Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 38
    • 0032561337 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice
    • Sato Y, Ferguson DG, Sako H, Dorn GW, Kadambi VJ, Yatani A, Hoit BD, Walsh RA, Kranias EG. Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice. J Biol Chem 273: 28470-28477, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 28470-28477
    • Sato, Y.1    Ferguson, D.G.2    Sako, H.3    Dorn, G.W.4    Kadambi, V.J.5    Yatani, A.6    Hoit, B.D.7    Walsh, R.A.8    Kranias, E.G.9
  • 39
    • 28444498920 scopus 로고    scopus 로고
    • Regulation of cardiac sarcoplasmic reticulum Ca release by luminal [Ca] and altered gating assessed with a mathematical model
    • Shannon TR, Wang F, Bers DM. Regulation of cardiac sarcoplasmic reticulum Ca release by luminal [Ca] and altered gating assessed with a mathematical model. Biophys J 89: 4096-4110, 2005.
    • (2005) Biophys J , vol.89 , pp. 4096-4110
    • Shannon, T.R.1    Wang, F.2    Bers, D.M.3
  • 41
    • 16444375139 scopus 로고    scopus 로고
    • Triadin overexpression stimulates excitation-contraction coupling and increases predisposition to cellular arrhythmia in cardiac myocytes
    • Terentyev D, Cala SE, Houle TD, Viatchenko-Karpinski S, Gyorke I, Terentyeva R, Williams SC, Gyorke S. Triadin overexpression stimulates excitation-contraction coupling and increases predisposition to cellular arrhythmia in cardiac myocytes. Circ Res 96: 651-658, 2005.
    • (2005) Circ Res , vol.96 , pp. 651-658
    • Terentyev, D.1    Cala, S.E.2    Houle, T.D.3    Viatchenko-Karpinski, S.4    Gyorke, I.5    Terentyeva, R.6    Williams, S.C.7    Gyorke, S.8
  • 42
    • 34547852387 scopus 로고    scopus 로고
    • Protein-protein interactions between triadin and calsequestrin are involved in modulation of sarcoplasmic reticulum calcium release in cardiac myocytes
    • Terentyev D, Viatchenko-Karpinski S, Vedamoorthyrao S, Oduru S, Gyorke I, Williams SC, Gyorke S. Protein-protein interactions between triadin and calsequestrin are involved in modulation of sarcoplasmic reticulum calcium release in cardiac myocytes. J Physiol 583: 71-80, 2007.
    • (2007) J Physiol , vol.583 , pp. 71-80
    • Terentyev, D.1    Viatchenko-Karpinski, S.2    Vedamoorthyrao, S.3    Oduru, S.4    Gyorke, I.5    Williams, S.C.6    Gyorke, S.7
  • 43
    • 36148978296 scopus 로고    scopus 로고
    • Overlapping roles of junctin and triadin in junctional SR
    • Tijskens P, Franzini-Armstrong C, Jones LR. Overlapping roles of junctin and triadin in junctional SR. Biophys J 82: 177A-178A, 2002.
    • (2002) Biophys J , vol.82
    • Tijskens, P.1    Franzini-Armstrong, C.2    Jones, L.R.3
  • 44
    • 31444432542 scopus 로고    scopus 로고
    • Ryanodine receptor/calcium release channel PKA phosphorylation: A critical mediator of heart failure progression
    • Wehrens XHT, Lehnart SE, Reiken S, Vest JA, Wronska A, Marks AR. Ryanodine receptor/calcium release channel PKA phosphorylation: A critical mediator of heart failure progression. Proc Natl Acad Sci USA 103: 511-518, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 511-518
    • Wehrens, X.H.T.1    Lehnart, S.E.2    Reiken, S.3    Vest, J.A.4    Wronska, A.5    Marks, A.R.6
  • 46
    • 0034977701 scopus 로고    scopus 로고
    • Structural alterations in cardiac calcium release units resulting from overexpression of junctin
    • Zhang L, Franzini-Armstrong C, Ramesh V, Jones LR. Structural alterations in cardiac calcium release units resulting from overexpression of junctin. J Mol Cell Cardiol 33: 233-247, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 233-247
    • Zhang, L.1    Franzini-Armstrong, C.2    Ramesh, V.3    Jones, L.R.4
  • 47
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • Zhang L, Kelley J, Schmeisser G, Kobayashi YM, Jones LR. Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 272: 23389-23397, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.