메뉴 건너뛰기




Volumn 2010, Issue , 2010, Pages

Titin-isoform dependence of titin-actin interaction and its regulation by S100A1/ Ca2+ in skinned myocardium

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM BINDING PROTEIN; CALCIUM ION; CONNECTIN; GELSOLIN; PROTEIN S100A1; UNCLASSIFIED DRUG; CALCIUM; ISOPROTEIN; MUSCLE PROTEIN; PROTEIN KINASE; PROTEIN S 100; S100A1 PROTEIN;

EID: 77952490479     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2010/727239     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • Furst D. O., Osborn M., Nave R., Weber K., The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line Journal of Cell Biology 1988 106 5 1563 1572
    • (1988) Journal of Cell Biology , vol.106 , Issue.5 , pp. 1563-1572
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 2
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier H. L., Irving T. C., Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments Biophysical Journal 1995 68 3 1027 1044
    • (1995) Biophysical Journal , vol.68 , Issue.3 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 4
    • 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 5234 293 296
    • (1995) Science , vol.270 , Issue.5234 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 5
    • 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., Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence. Titin is an adjustable spring Circulation Research 1999 84 11 1339 1352
    • (1999) Circulation Research , vol.84 , Issue.11 , pp. 1339-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3
  • 6
    • 18544406997 scopus 로고    scopus 로고
    • Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity
    • Freiburg A., Trombitas K., Hell W., Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity Circulation Research 2000 86 11 1114 1121
    • (2000) Circulation Research , vol.86 , Issue.11 , pp. 1114-1121
    • Freiburg, A.1    Trombitas, K.2    Hell, W.3
  • 7
    • 34547629201 scopus 로고    scopus 로고
    • Functional genomics of chicken, mouse, and human titin supports splice diversity as an important mechanism for regulating biomechanics of striated muscle
    • Granzier H., Radke M., Royal J., Functional genomics of chicken, mouse, and human titin supports splice diversity as an important mechanism for regulating biomechanics of striated muscle American Journal of Physiology 2007 293 2 R557 R567
    • (2007) American Journal of Physiology , vol.293 , Issue.2
    • Granzier, H.1    Radke, M.2    Royal, J.3
  • 8
    • 0033962880 scopus 로고    scopus 로고
    • Differential expression of cardiac titin isoforms and modulation of cellular stiffness
    • Cazorla O., Freiburg A., Helmes M., Differential expression of cardiac titin isoforms and modulation of cellular stiffness Circulation Research 2000 86 1 59 67
    • (2000) Circulation Research , vol.86 , Issue.1 , pp. 59-67
    • Cazorla, O.1    Freiburg, A.2    Helmes, M.3
  • 9
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang M.-L., Centner T., Fornoff F., The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system Circulation Research 2001 89 11 1065 1072
    • (2001) Circulation Research , vol.89 , Issue.11 , pp. 1065-1072
    • Bang, M.-L.1    Centner, T.2    Fornoff, F.3
  • 11
    • 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 Biophysical Journal 2000 79 6 3226 3234
    • (2000) Biophysical Journal , vol.79 , Issue.6 , pp. 3226-3234
    • Trombitas, K.1    Redkar, A.2    Centner, T.3    Wu, Y.4    Labeit, S.5    Granzier, H.6
  • 13
    • 70349246846 scopus 로고    scopus 로고
    • Truncation of titins elastic PEVK region leads to cardiomyopathy with diastolic dysfunction
    • Granzier H. L., Radke M. H., Peng J., Truncation of titins elastic PEVK region leads to cardiomyopathy with diastolic dysfunction Circulation Research 2009 105 6 557 564
    • (2009) Circulation Research , vol.105 , Issue.6 , pp. 557-564
    • Granzier, H.L.1    Radke, M.H.2    Peng, J.3
  • 14
    • 0034811015 scopus 로고    scopus 로고
    • Titin-actin interaction in mouse myocardium: Passive tension modulation and its regulation by calcium/S100A1
    • Yamasaki R., Berri M., Wu Y., Titin-actin interaction in mouse myocardium: passive tension modulation and its regulation by calcium/S100A1 Biophysical Journal 2001 81 4 2297 2313
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2297-2313
    • Yamasaki, R.1    Berri, M.2    Wu, Y.3
  • 15
    • 0035834245 scopus 로고    scopus 로고
    • Interaction betweeen PEVK-titin and actin filaments origin of a viscous force component in cardiac myofibrils
    • Kulke M., Fujita-Becker S., Rostkova E., Interaction betweeen PEVK-titin and actin filaments origin of a viscous force component in cardiac myofibrils Circulation Research 2001 89 10 874 881
    • (2001) Circulation Research , vol.89 , Issue.10 , pp. 874-881
    • Kulke, M.1    Fujita-Becker, S.2    Rostkova, E.3
  • 16
    • 0036443942 scopus 로고    scopus 로고
    • PEVK domain of titin: An entropic spring with actin-binding properties
    • Linke W. A., Kulke M., Li H., PEVK domain of titin: an entropic spring with actin-binding properties Journal of Structural Biology 2002 137 1-2 194 205
    • (2002) Journal of Structural Biology , vol.137 , Issue.12 , pp. 194-205
    • Linke, W.A.1    Kulke, M.2    Li, H.3
  • 17
    • 0030022007 scopus 로고    scopus 로고
    • Calcium-dependent inhibition of in vitro thin-filament motility by native titin
    • Kellermayer M. S. Z., Granzier H. L., Calcium-dependent inhibition of in vitro thin-filament motility by native titin FEBS Letters 1996 380 3 281 286
    • (1996) FEBS Letters , vol.380 , Issue.3 , pp. 281-286
    • Kellermayer, M.S.Z.1    Granzier, H.L.2
  • 19
    • 34548783879 scopus 로고    scopus 로고
    • Interaction forces between F-actin and titin PEVK domain measured with optical tweezers
    • Bianco P., Nagy A., Kengyel A., Interaction forces between F-actin and titin PEVK domain measured with optical tweezers Biophysical Journal 2007 93 6 2102 2109
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2102-2109
    • Bianco, P.1    Nagy, A.2    Kengyel, A.3
  • 20
    • 0027448024 scopus 로고
    • Elastic filaments in situ in cardiac muscle: Deep-etch replica analysis in combination with selective removal of actin and myosin filaments
    • Funatsu T., Kono E., Higuchi H., Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments Journal of Cell Biology 1993 120 3 711 724
    • (1993) Journal of Cell Biology , vol.120 , Issue.3 , pp. 711-724
    • Funatsu, T.1    Kono, E.2    Higuchi, H.3
  • 22
  • 23
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato R., S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles International Journal of Biochemistry and Cell Biology 2001 33 7 637 668
    • (2001) International Journal of Biochemistry and Cell Biology , vol.33 , Issue.7 , pp. 637-668
    • Donato, R.1
  • 24
    • 0344896768 scopus 로고    scopus 로고
    • Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle
    • Fukuda N., Wu Y., Farman G., Irving T. C., Granzier H., Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle Journal of Physiology 2003 553 1 147 154
    • (2003) Journal of Physiology , vol.553 , Issue.1 , pp. 147-154
    • Fukuda, N.1    Wu, Y.2    Farman, G.3    Irving, T.C.4    Granzier, H.5
  • 25
    • 0034786066 scopus 로고    scopus 로고
    • Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently
    • Trombits K., Wu Y., Labeit D., Labeit S., Granzier H., Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently American Journal of Physiology 2001 281 4 H1793 H1799
    • (2001) American Journal of Physiology , vol.281 , Issue.4
    • Trombits, K.1    Wu, Y.2    Labeit, D.3    Labeit, S.4    Granzier, H.5
  • 26
    • 0025378983 scopus 로고
    • The descending of the force-sarcomere length relation of the frog revisited
    • Granzier H. L. M., Pollack G. H., The descending of the force-sarcomere length relation of the frog revisited Journal of Physiology 1990 421 595 615
    • (1990) Journal of Physiology , vol.421 , pp. 595-615
    • Granzier, H.L.M.1    Pollack, G.H.2
  • 27
    • 0024318348 scopus 로고
    • Effect of active pre-shortening on isometric and isotonic performance of single frog muscle fibres
    • Granzier H. L. M., Pollack G. H., Effect of active pre-shortening on isometric and isotonic performance of single frog muscle fibres Journal of Physiology 1989 415 299 327
    • (1989) Journal of Physiology , vol.415 , pp. 299-327
    • Granzier, H.L.M.1    Pollack, G.H.2
  • 28
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titins PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • Hidalgo C., Hudson B., Bogomolovas J., PKC phosphorylation of titins PEVK element: a novel and conserved pathway for modulating myocardial stiffness Circulation Research 2009 105 7 631 638
    • (2009) Circulation Research , vol.105 , Issue.7 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Bogomolovas, J.3
  • 29
    • 0030048904 scopus 로고    scopus 로고
    • Nonuniform elasticity of titin in cardiac myocytes: A study using immunoelectron microscopy and cellular mechanics
    • Granzier H., Helmes M., Trombits K., Nonuniform elasticity of titin in cardiac myocytes: a study using immunoelectron microscopy and cellular mechanics Biophysical Journal 1996 70 1 430 442
    • (1996) Biophysical Journal , vol.70 , Issue.1 , pp. 430-442
    • Granzier, H.1    Helmes, M.2    Trombits, K.3
  • 30
    • 0030821918 scopus 로고    scopus 로고
    • Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension
    • Trombits K., Granzier H., Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension American Journal of Physiology 1997 273 2, part 1 C662 C670
    • (1997) American Journal of Physiology , vol.273 , Issue.2 PART 1
    • Trombits, K.1    Granzier, H.2
  • 31
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., Fabiato F., Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells Journal de Physiologie 1979 75 5 463 505
    • (1979) Journal de Physiologie , vol.75 , Issue.5 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 32
    • 1242281665 scopus 로고    scopus 로고
    • Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium
    • Lahmers S., Wu Y., Call D. R., Labeit S., Granzier H., Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium Circulation Research 2004 94 4 505 513
    • (2004) Circulation Research , vol.94 , Issue.4 , pp. 505-513
    • Lahmers, S.1    Wu, Y.2    Call, D.R.3    Labeit, S.4    Granzier, H.5
  • 33
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla O., Wu Y., Irving T. C., Granzier H., Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes Circulation Research 2001 88 10 1028 1035
    • (2001) Circulation Research , vol.88 , Issue.10 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 34
    • 0032545147 scopus 로고    scopus 로고
    • Location of the binding site of the mannose-specific lectin comitin on F-actin
    • Fulgenzi G., Graciotti L., Granata A. L., Location of the binding site of the mannose-specific lectin comitin on F-actin Journal of Molecular Biology 1998 284 5 1255 1263
    • (1998) Journal of Molecular Biology , vol.284 , Issue.5 , pp. 1255-1263
    • Fulgenzi, G.1    Graciotti, L.2    Granata, A.L.3
  • 35
    • 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., An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin Cell 1992 70 1 81 92
    • (1992) Cell , vol.70 , Issue.1 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3
  • 36
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M., Winder S. J., Pastore A., Nebulin, a helical actin binding protein EMBO Journal 1994 13 8 1782 1789
    • (1994) EMBO Journal , vol.13 , Issue.8 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 37
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser M., Identification of new repeating motifs in titin Proteins 2001 43 2 145 149
    • (2001) Proteins , vol.43 , Issue.2 , pp. 145-149
    • Greaser, M.1
  • 38
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma K., Kan L.-S., Wang K., Polyproline II helix is a key structural motif of the elastic PEVK segment of titin Biochemistry 2001 40 12 3427 3438
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3427-3438
    • Ma, K.1    Kan, L.-S.2    Wang, K.3
  • 39
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson M. P., The structure and function of proline-rich regions in proteins Biochemical Journal 1994 297 2 249 260
    • (1994) Biochemical Journal , vol.297 , Issue.2 , pp. 249-260
    • Williamson, M.P.1
  • 42
    • 18744374455 scopus 로고    scopus 로고
    • Different molecular mechanics displayed by titins constitutively and differentially expressed tandem Ig segments
    • Watanabe K., Muhle-Goll C., Kellermayer M. S. Z., Labeit S., Granzier H., Different molecular mechanics displayed by titins constitutively and differentially expressed tandem Ig segments Journal of Structural Biology 2002 137 1-2 248 258
    • (2002) Journal of Structural Biology , vol.137 , Issue.12 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.Z.3    Labeit, S.4    Granzier, H.5
  • 43
    • 0037192845 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac titins PEVK and N2B spring elements
    • Watanabe K., Nair P., Labeit D., Molecular mechanics of cardiac titins PEVK and N2B spring elements The Journal of Biological Chemistry 2002 277 13 11549 11558
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11549-11558
    • Watanabe, K.1    Nair, P.2    Labeit, D.3
  • 44
    • 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., Trombits K., Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction Biophysical Journal 1997 73 4 2043 2053
    • (1997) Biophysical Journal , vol.73 , Issue.4 , pp. 2043-2053
    • Granzier, H.1    Kellermayer, M.2    Helmes, M.3    Trombits, K.4
  • 45
    • 0026665940 scopus 로고
    • A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts
    • Rodriguez E. K., Hunter W. C., Royce M. J., Leppo M. K., Douglas A. S., Weisman H. F., A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts American Journal of Physiology 1992 263 1, part 2 H293 H306
    • (1992) American Journal of Physiology , vol.263 , Issue.1 PART 2
    • Rodriguez, E.K.1    Hunter, W.C.2    Royce, M.J.3    Leppo, M.K.4    Douglas, A.S.5    Weisman, H.F.6
  • 46
    • 2342562048 scopus 로고
    • Left ventricular free wall and intraventricular pressure-sarcomere length distributions
    • Grimm A. F., Lin H. L., Grimm B. R., Left ventricular free wall and intraventricular pressure-sarcomere length distributions American Journal of Physiology 1980 239 1 H101 H107
    • (1980) American Journal of Physiology , vol.239 , Issue.1
    • Grimm, A.F.1    Lin, H.L.2    Grimm, B.R.3
  • 47
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes M., Trombits K., Granzier H., Titin develops restoring force in rat cardiac myocytes Circulation Research 1996 79 3 619 626
    • (1996) Circulation Research , vol.79 , Issue.3 , pp. 619-626
    • Helmes, M.1    Trombits, K.2    Granzier, H.3
  • 50
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments
    • Horrowits R., Podolsky R. J., The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments Journal of Cell Biology 1987 105 5 2217 2223
    • (1987) Journal of Cell Biology , vol.105 , Issue.5 , pp. 2217-2223
    • Horrowits, R.1    Podolsky, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.