메뉴 건너뛰기




Volumn 8, Issue 6 SUPPL., 2002, Pages

Titin: An endosarcomeric protein that modulates myocardial stiffness in DCM

Author keywords

Cardiomyopathy; Diastole; Length dependent activation; Myocardium; Phosphorylation; Titin

Indexed keywords

CONNECTIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0036947533     PISSN: 10719164     EISSN: None     Source Type: Journal    
DOI: 10.1054/jcaf.2002.129278     Document Type: Conference Paper
Times cited : (21)

References (46)
  • 1
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S, Kolmerer B: Titins: Giant proteins in charge of muscle ultrastructure and elasticity. Science 1995;270:293-296
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 2
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier HL, Irving TC: Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments. Biophys J 1995;68:1027-1044
    • (1995) Biophys J , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 4
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann WM, Gautel M, Weber K, Furst DO: Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J 1997;16:211-220
    • (1997) EMBO J , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Furst, D.O.4
  • 6
    • 0030821918 scopus 로고    scopus 로고
    • Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension
    • Trombitas K, Granzier H: Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension. Am J Physiol 1997;273:C662-C670
    • (1997) Am J Physiol , vol.273
    • Trombitas, K.1    Granzier, H.2
  • 7
    • 0029143981 scopus 로고
    • The mechanically active domain of titin in cardiac muscle
    • Trombitas K, Jin JP, Granzier H: The mechanically active domain of titin in cardiac muscle. Circ Res 1995;77:856-861
    • (1995) Circ Res , vol.77 , pp. 856-861
    • Trombitas, K.1    Jin, J.P.2    Granzier, H.3
  • 8
    • 0030048904 scopus 로고    scopus 로고
    • Nonuniform elasticity of titin in cardiac myocytes: A study using immunoelectron microscopy and cellular mechanics
    • Granzier H, Helmes M, Trombitas K: Nonuniform elasticity of titin in cardiac myocytes: A study using immunoelectron microscopy and cellular mechanics. Biophys J 1996;70:430-442
    • (1996) Biophys J , vol.70 , pp. 430-442
    • Granzier, H.1    Helmes, M.2    Trombitas, K.3
  • 9
    • 0030855930 scopus 로고    scopus 로고
    • Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction
    • Granzier H, Kellermayer M, Helmes M, Trombitas K: Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction. Biophys J 1997;73:2043-2053
    • (1997) Biophys J , vol.73 , pp. 2043-2053
    • Granzier, H.1    Kellermayer, M.2    Helmes, M.3    Trombitas, K.4
  • 10
    • 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 WA, Granzier H: Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: Titin is an adjustable spring. Circ Res 1999;84:1339-1352
    • (1999) Circ Res , vol.84 , pp. 1339-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3    Kellermayer, M.4    Labeit, S.5    Linke, W.A.6    Granzier, H.7
  • 11
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
    • Linke WA, Rudy DE, Centner T, Gautel M, Witt C, Labeit S, Gregorio CC: I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J Cell Biol 1999;146:631-644
    • (1999) J Cell Biol , vol.146 , pp. 631-644
    • Linke, W.A.1    Rudy, D.E.2    Centner, T.3    Gautel, M.4    Witt, C.5    Labeit, S.6    Gregorio, C.C.7
  • 13
    • 0021297326 scopus 로고
    • Cytoskeletal matrix in striated muscle: The role of titin, nebulin and intermediate filaments
    • Wang K: Cytoskeletal matrix in striated muscle: The role of titin, nebulin and intermediate filaments. Adv Exp Med Biol 1984;170:285-305
    • (1984) Adv Exp Med Biol , vol.170 , pp. 285-305
    • Wang, K.1
  • 14
    • 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, Granzier H: Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ Res 2001;88:1028-1035
    • (2001) Circ Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 15
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes M, Trombitas K, Granzier H: Titin develops restoring force in rat cardiac myocytes. Circ Res 1996;79:619-626
    • (1996) Circ Res , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 18
    • 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, Granzier H: Extensibility of isoforms of cardiac titin: Variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity. Biophys J 2000;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
  • 19
    • 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, Granzier H: PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J Struct Biol 1998;122:188-196
    • (1998) J Struct Biol , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 21
    • 0034509442 scopus 로고    scopus 로고
    • Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle
    • Wu Y, Cazorla O, Labeit D, Labeit S, Granzier H: Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle. J Mol Cell Cardiol 2000;32:2151-2162
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2151-2162
    • Wu, Y.1    Cazorla, O.2    Labeit, D.3    Labeit, S.4    Granzier, H.5
  • 24
    • 0023668531 scopus 로고
    • In vivo phosphorylation of titin and nebulin in frog skeletal muscle
    • Somerville LL, Wang K: In vivo phosphorylation of titin and nebulin in frog skeletal muscle. Biochem Biophys Res Commun 1987;147:986-992
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 986-992
    • Somerville, L.L.1    Wang, K.2
  • 25
    • 0028174245 scopus 로고
    • Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats
    • Strang KT, Sweitzer NK, Greaser ML, Moss RL: Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats. Circ Res 1994;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
  • 26
    • 0027246620 scopus 로고
    • Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts
    • Gautel M, Leonard K, Labeit S: Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J 1993;12:3827-3834
    • (1993) EMBO J , vol.12 , pp. 3827-3834
    • Gautel, M.1    Leonard, K.2    Labeit, S.3
  • 27
    • 0029143271 scopus 로고
    • Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases
    • Sebestyen MG, Wolff JA, Greaser ML: Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J Cell Sci 1995;108:3029-3037
    • (1995) J Cell Sci , vol.108 , pp. 3029-3037
    • Sebestyen, M.G.1    Wolff, J.A.2    Greaser, M.L.3
  • 28
    • 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, Granzier H: Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ Res 2002;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
  • 30
    • 0035259181 scopus 로고    scopus 로고
    • Calcium, cross-bridges, and the Frank-Starling relationship
    • Fuchs F, Smith SH: Calcium, cross-bridges, and the Frank-Starling relationship. News Physiol Sci 2001;16:5-10
    • (2001) News Physiol Sci , vol.16 , pp. 5-10
    • Fuchs, F.1    Smith, S.H.2
  • 31
    • 0030198699 scopus 로고    scopus 로고
    • Sarcomere length versus interfilament spacing as determinants of cardiac myofilament Ca2+ sensitivity and Ca2+ binding
    • Fuchs F, Wang YP: Sarcomere length versus interfilament spacing as determinants of cardiac myofilament Ca2+ sensitivity and Ca2+ binding. J Mol Cell Cardiol 1996;28:1375-1383
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 1375-1383
    • Fuchs, F.1    Wang, Y.P.2
  • 32
    • 0029029477 scopus 로고
    • Osmotic compression of single cardiac myocytes eliminates the reduction in Ca2+ sensitivity of tension at short sarcomere length
    • McDonald KS, Moss RL: Osmotic compression of single cardiac myocytes eliminates the reduction in Ca2+ sensitivity of tension at short sarcomere length. Circ Res 1995;77:199-205
    • (1995) Circ Res , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 33
    • 0027436282 scopus 로고
    • Passive tension and stiffness of vertebrate skeletal and insect flight muscles: The contribution of weak cross-bridges and elastic filaments
    • Granzier HL, Wang K: Passive tension and stiffness of vertebrate skeletal and insect flight muscles: The contribution of weak cross-bridges and elastic filaments. Biophys J 1993;65:2141-2159
    • (1993) Biophys J , vol.65 , pp. 2141-2159
    • Granzier, H.L.1    Wang, K.2
  • 34
    • 0027517018 scopus 로고
    • Interplay between passive tension and strong and weak binding crossbridges in insect indirect flight muscle. A functional dissection by gelsolin-mediated thin filament removal
    • Granzier HL, Wang K: Interplay between passive tension and strong and weak binding crossbridges in insect indirect flight muscle. A functional dissection by gelsolin-mediated thin filament removal. J Gen Physiol 1993;101:235-270
    • (1993) J Gen Physiol , vol.101 , pp. 235-270
    • Granzier, H.L.1    Wang, K.2
  • 35
    • 0023896719 scopus 로고
    • Thick filament movement and isometric tension in activated skeletal muscle
    • Horowits R, Podolsky RJ: Thick filament movement and isometric tension in activated skeletal muscle. Biophys J 1988;54:165-171
    • (1988) Biophys J , vol.54 , pp. 165-171
    • Horowits, R.1    Podolsky, R.J.2
  • 36
    • 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, Podolsky RJ: The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments. J Cell Biol 1987;105:2217-2223
    • (1987) J Cell Biol , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 39
    • 0034470466 scopus 로고    scopus 로고
    • Skeletal muscle-specific calpain, p94, and connectin/titin: Their physiological functions and relationship to limb-girdle muscular dystrophy type 2A
    • Sorimachi H, Ono Y, Suzuki K: Skeletal muscle-specific calpain, p94, and connectin/titin: Their physiological functions and relationship to limb-girdle muscular dystrophy type 2A. Adv Exp Med Biol 2000;481:383-395
    • (2000) Adv Exp Med Biol , vol.481 , pp. 383-395
    • Sorimachi, H.1    Ono, Y.2    Suzuki, K.3
  • 41
    • 0029935950 scopus 로고    scopus 로고
    • Pathogenesis of dilated cardiomyopathy and heart failure: Insights from cell morphology and biology
    • Hein S, Schaper J: Pathogenesis of dilated cardiomyopathy and heart failure: Insights from cell morphology and biology. Curr Opin Cardiol 1996;11:293-301
    • (1996) Curr Opin Cardiol , vol.11 , pp. 293-301
    • Hein, S.1    Schaper, J.2
  • 44
    • 0030800315 scopus 로고    scopus 로고
    • Myocardial length-force relationship in end stage dilated cardiomyopathy and normal human myocardium: Analysis of intact and skinned left ventricular trabeculae obtained during 11 heart transplantations
    • Vahl CF, Timek T, Bonz A, Kochsiek N, Fuchs H, Schaffer L, Rosenberg M, Dillmann R, Hagl S: Myocardial length-force relationship in end stage dilated cardiomyopathy and normal human myocardium: Analysis of intact and skinned left ventricular trabeculae obtained during 11 heart transplantations. Basic Res Cardiol 1997;92:261-270
    • (1997) Basic Res Cardiol , vol.92 , pp. 261-270
    • Vahl, C.F.1    Timek, T.2    Bonz, A.3    Kochsiek, N.4    Fuchs, H.5    Schaffer, L.6    Rosenberg, M.7    Dillmann, R.8    Hagl, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.