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Volumn 23, Issue 5-6, 2002, Pages 457-471

Titin as a modular spring: Emerging mechanisms for elasticity control by titin in cardiac physiology and pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; MUSCLE PROTEIN;

EID: 0038583937     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023458406346     Document Type: Review
Times cited : (26)

References (74)
  • 1
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual ∼700 kDa titin isoform and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang ML, Centner T, Fornoff F, Geach AJ, Gotthardt M, McNabb M, Witt CC, Labeit D, Gregorio CC, Granzier H, et al. (2001) The complete gene sequence of titin, expression of an unusual ∼700 kDa titin isoform and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ Res 89: 1065-1072.
    • (2001) Circ Res , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6    Witt, C.C.7    Labeit, D.8    Gregorio, C.C.9    Granzier, H.10
  • 7
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla O, Wu Y, Irving TC and Granzier H (2001) Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ Res 88: 1028-1035.
    • (2001) Circ Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 10
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich E, Vancompernolle K, Huet C, Goethals M, Finidori J, Vandekerckhove J and Louvard D (1992) An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70: 81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 11
    • 0035797846 scopus 로고    scopus 로고
    • Length dependence of tension generation in rat skinned cardiac muscle: Role of titin in the Frank-Starling mechanism of the heart
    • Fukuda N, Sasaki D, Ishiwata S and Kurihara S (2001) Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circulation 104: 1639-1645.
    • (2001) Circulation , vol.104 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 13
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of a mink channel subunit with the sarcomeric protein T-cap suggests a T-tubule - Myofibril Z-line linking system
    • Furukawa T, Ono Y, Tsuchiya H, Katayama Y, Bang ML, Labeit D, Labeit S, Inagaki N and Gregorio CC (2001) Specific Interaction of a mink Channel Subunit with the Sarcomeric Protein T-cap Suggests a T-Tubule - Myofibril Z-line Linking System. J Mol Biol 213: 775-784.
    • (2001) J Mol Biol , vol.213 , pp. 775-784
    • Furukawa, T.1    Ono, Y.2    Tsuchiya, H.3    Katayama, Y.4    Bang, M.L.5    Labeit, D.6    Labeit, S.7    Inagaki, N.8    Gregorio, C.C.9
  • 15
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multi-function spring
    • Granzier H and Labeit S (2002) Cardiac titin: an adjustable multi-function spring. J Physiol (Lond) 541: 335-342.
    • (2002) J Physiol (Lond) , vol.541 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 17
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser M (2001) Identification of new repeating motifs in titin. Proteins 43: 145-149.
    • (2001) Proteins , vol.43 , pp. 145-149
    • Greaser, M.1
  • 19
    • 0035831554 scopus 로고    scopus 로고
    • Modular motif, structural folds and affinity profiles of PEVK segment of human fetal skeletal muscle titin
    • Gutierrez-Cruz G, Van Heerden AH and Wang K (2000) Modular motif, structural folds and affinity profiles of PEVK segment of human fetal skeletal muscle titin. J Biol Chem 276: 7442-7449.
    • (2000) J Biol Chem , vol.276 , pp. 7442-7449
    • Gutierrez-Cruz, G.1    Van Heerden, A.H.2    Wang, K.3
  • 20
    • 0021713707 scopus 로고
    • Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases
    • Hartzell HC and Glass DB (1984) Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases. J Biol Chem 259: 15587-15596.
    • (1984) J Biol Chem , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.B.2
  • 21
    • 0029935950 scopus 로고    scopus 로고
    • Pathogenesis of dilated cardiomyopathy and heart failure: Insights from cell morphology and biology
    • Hein S and Schaper J (1996) Pathogenesis of dilated cardiomyopathy and heart failure: insights from cell morphology and biology. Curr Opin Cardiol 11: 293-301.
    • (1996) Curr Opin Cardiol , vol.11 , pp. 293-301
    • Hein, S.1    Schaper, J.2
  • 23
    • 0033546073 scopus 로고    scopus 로고
    • Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: Titin is an adjustable spring
    • Helmes M, Trombitas K, Centner T, Kellermayer M, Labeit S, Linke A and Granzier H (1999) Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring. Circ Res 84: 1139-1352.
    • (1999) Circ Res , vol.84 , pp. 1139-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3    Kellermayer, M.4    Labeit, S.5    Linke, A.6    Granzier, H.7
  • 24
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes M, Trombitas K and Granzier H (1996) Titin develops restoring force in rat cardiac myocytes. Circ Res 79: 619-626.
    • (1996) Circ Res , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 25
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments
    • Horowits R and Podolsky RJ (1987) The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J Cell Biol 105: 2217-2223.
    • (1987) J Cell Biol , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 26
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta S, Politou AS and Pastore A (1996) Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure 4: 323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 29
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer MS, Smith SB, Granzier HL and Bustamante C (1997) Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276: 1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 32
    • 0034472181 scopus 로고    scopus 로고
    • Mechanical manipulation of single titin molecules with laser tweezers
    • Kellermayer MS, Smith S, Bustamante C and Granzier HL (2000) Mechanical manipulation of single titin molecules with laser tweezers. Adv Exp Med Biol 481: 111-126; discussion 127-128.
    • (2000) Adv Exp Med Biol , vol.481 , pp. 111-126
    • Kellermayer, M.S.1    Smith, S.2    Bustamante, C.3    Granzier, H.L.4
  • 33
    • 0035144607 scopus 로고    scopus 로고
    • Mechanical fatigue in repetitively stretched single molecules of titin
    • Kellermayer MS, Smith SB, Bustamante C and Granzier HL (2001) Mechanical fatigue in repetitively stretched single molecules of titin. Biophys J 80: 852-863.
    • (2001) Biophys J , vol.80 , pp. 852-863
    • Kellermayer, M.S.1    Smith, S.B.2    Bustamante, C.3    Granzier, H.L.4
  • 34
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S and Kolmerer B (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270: 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 36
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament strucuture
    • Linke W, Rudy D, Centner T, Gautel M, Witt C, Labeit S and Gregorio C (1999) I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament strucuture. J Cell Biol 146: 631-644.
    • (1999) J Cell Biol , vol.146 , pp. 631-644
    • Linke, W.1    Rudy, D.2    Centner, T.3    Gautel, M.4    Witt, C.5    Labeit, S.6    Gregorio, C.7
  • 37
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: Elasticity of titin filaments in vertebrate striated muscle
    • Linke WA (2000) Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol Histopathol 15: 799-811.
    • (2000) Histol Histopathol , vol.15 , pp. 799-811
    • Linke, W.A.1
  • 38
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: New facts on titin elasticity
    • Linke WA and Granzier H (1998) A spring tale: new facts on titin elasticity. Biophys J 75: 2613-2614.
    • (1998) Biophys J , vol.75 , pp. 2613-2614
    • Linke, W.A.1    Granzier, H.2
  • 39
  • 40
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke WA, Stockmeier MR, Ivemeyer M, Hosser H and Mundel P (1998) Characterizing Titin's I-Band Ig Domain Region as an Entropic Spring. J Cell Sci 111: 1567-1574.
    • (1998) J Cell Sci , vol.111 , pp. 1567-1574
    • Linke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 41
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma K, Kan L and Wang K (2001) Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochemistry 40: 3427-3438.
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.2    Wang, K.3
  • 42
    • 0028000456 scopus 로고
    • Fluctuations and supercoiling of DNA
    • Marko JF and Siggia ED (1994) Fluctuations and supercoiling of DNA. Science 265: 506-508.
    • (1994) Science , vol.265 , pp. 506-508
    • Marko, J.F.1    Siggia, E.D.2
  • 44
    • 0030982846 scopus 로고    scopus 로고
    • Connectin/titin, giant elastic protein of muscle
    • Maruyama K (1997) Connectin/titin, giant elastic protein of muscle. Faseb J 11: 341-345.
    • (1997) Faseb J , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 46
    • 0038695332 scopus 로고    scopus 로고
    • Dual roles of MURF-1 in the regulation of sarcomeric M-line structure and in the potential modulation of gene expression via its interaction with titin and GMEB-1
    • McElhinny AS, Sorimachi H, Labeit S and Gregorio CC (2002) Dual roles of MURF-1 in the regulation of sarcomeric M-line structure and in the potential modulation of gene expression via its interaction with titin and GMEB-1. J Cell Biol 57: 125-136.
    • (2002) J Cell Biol , vol.57 , pp. 125-136
    • McElhinny, A.S.1    Sorimachi, H.2    Labeit, S.3    Gregorio, C.C.4
  • 47
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva A, Kulke M, Fernandez JM and Linke WA (2001) Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys J 80: 1442-1451.
    • (2001) Biophys J , vol.80 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 49
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M, Winder SJ and Pastore A (1994) Nebulin, a helical actin binding protein. Embo J 13: 1782-1789.
    • (1994) Embo J , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 50
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM and Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276: 1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 52
    • 0017143827 scopus 로고
    • Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart
    • Solaro RJ, Moir AJ and Perry SV (1976) Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart. Nature 262: 615-617.
    • (1976) Nature , vol.262 , pp. 615-617
    • Solaro, R.J.1    Moir, A.J.2    Perry, S.V.3
  • 53
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94- specific sequence
    • Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K, et al. (1995) Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94- specific sequence. J Biol Chem 270: 31158-31162.
    • (1995) J Biol Chem , vol.270 , pp. 31158-31162
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3    Takahashi, M.4    Ishiura, S.5    Sasagawa, N.6    Sorimachi, N.7    Shimada, H.8    Tagawa, K.9    Maruyama, K.10
  • 54
    • 0028980053 scopus 로고
    • Alpha 1-adrenergic receptor stimulation decreases maximum shortening velocity of skinned single ventricular myocytes from rats
    • Strang KT and Moss RL (1995) Alpha 1-adrenergic receptor stimulation decreases maximum shortening velocity of skinned single ventricular myocytes from rats. Circ Res 77: 114-120.
    • (1995) Circ Res , vol.77 , pp. 114-120
    • Strang, K.T.1    Moss, R.L.2
  • 55
    • 0028174245 scopus 로고
    • Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats
    • Strang KT, Sweitzer NK, Greaser ML and Moss RL (1994) Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats. Circ Res 74: 542-549.
    • (1994) Circ Res , vol.74 , pp. 542-549
    • Strang, K.T.1    Sweitzer, N.K.2    Greaser, M.L.3    Moss, R.L.4
  • 56
    • 0030821918 scopus 로고    scopus 로고
    • Actin removal from cardiac myocytes shows that near Z-line titin attaches to actin while under tension
    • Trombitas K and Granzier H (1997). Actin removal from cardiac myocytes shows that near Z-line titin attaches to actin while under tension. Am J Physiol 273: C662-C670.
    • (1997) Am J Physiol , vol.273
    • Trombitas, K.1    Granzier, H.2
  • 58
    • 0031691961 scopus 로고    scopus 로고
    • PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10
    • Trombitas K, Greaser M, French G and Granzier H (1998a) PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J Struct Biol 122: 188-196.
    • (1998) J Struct Biol , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 59
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • Trombitas K, Greaser M, Labeit S, Jin JP, Kellermayer M, Helmes M and Granzier H (1998b) Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J Cell Biol 140: 853-859.
    • (1998) J Cell Biol , vol.140 , pp. 853-859
    • Trombitas, K.1    Greaser, M.2    Labeit, S.3    Jin, J.P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 60
    • 0033637514 scopus 로고    scopus 로고
    • Extensibility of isoforms of cardiac titin: Variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity
    • Trombitas K, Redkar A, Centner T, Wu Y, Labeit S and Granzier H (2000) Extensibility of isoforms of cardiac titin: variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity. Biophys J 79: 3226-3234.
    • (2000) Biophys J , vol.79 , pp. 3226-3234
    • Trombitas, K.1    Redkar, A.2    Centner, T.3    Wu, Y.4    Labeit, S.5    Granzier, H.6
  • 62
    • 0035919831 scopus 로고    scopus 로고
    • Flexibility and extensibility in the titin molecule: Analysis of electron microscope data
    • Tskhovrebova L and Trinick J (2001) Flexibility and extensibility in the titin molecule: analysis of electron microscope data. J Mol Biol 310: 755-771.
    • (2001) J Mol Biol , vol.310 , pp. 755-771
    • Tskhovrebova, L.1    Trinick, J.2
  • 64
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova L, Trinick J, Sleep JA and Simmons RM (1997) Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387: 308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 65
    • 0021297326 scopus 로고
    • Cytoskeletal matrix in striated muscle: The role of titin, nebulin and intermediate filaments
    • Wang K (1984) Cytoskeletal matrix in striated muscle: the role of titin, nebulin and intermediate filaments. Adv Exp Med Biol 170: 285-305.
    • (1984) Adv Exp Med Biol , vol.170 , pp. 285-305
    • Wang, K.1
  • 66
    • 0029805084 scopus 로고    scopus 로고
    • Titin/connectin and nebulin: Giant protein rulers of muscle structure and function
    • Wang K (1996) Titin/connectin and nebulin: giant protein rulers of muscle structure and function. Adv Biophys J 33: 123-134.
    • (1996) Adv Biophys J , vol.33 , pp. 123-134
    • Wang, K.1
  • 67
    • 18744374455 scopus 로고    scopus 로고
    • Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments
    • Watanabe K, Muhle-Goll C, Kellermayer MS, Labeit S and Granzier H (2002a) Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments. J Struct Biol 137: 248-258.
    • (2002) J Struct Biol , vol.137 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.3    Labeit, S.4    Granzier, H.5
  • 69
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson MP (1994) The structure and function of proline-rich regions in proteins. Biochem J 297: 249-260.
    • (1994) Biochem J , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 71
    • 0037056103 scopus 로고    scopus 로고
    • Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness
    • in press
    • Wu Y, Bell SP, Trombitas K, Witt CW, Labeit S, LeWinter MM and Granzier H (2002b) Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness. Circulation, in press.
    • (2002) Circulation
    • Wu, Y.1    Bell, S.P.2    Trombitas, K.3    Witt, C.W.4    Labeit, S.5    LeWinter, M.M.6    Granzier, H.7
  • 73
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • Yamasaki R, Wu Y, McNabb M, Greaser M, Labeit S and Granzier H (2002) Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ Res 90: 1181-1188.
    • (2002) Circ Res , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Labeit, S.5    Granzier, H.6
  • 74
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P, Ehler E and Gautel M (2001) Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J Cell Biol 154: 123-136.
    • (2001) J Cell Biol , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.