메뉴 건너뛰기




Volumn 1-2, Issue , 2012, Pages 173-186

Cardiovascular Mechanotransduction

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882913713     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-381510-1.00014-4     Document Type: Chapter
Times cited : (8)

References (142)
  • 1
    • 0347477365 scopus 로고    scopus 로고
    • Mechanobiology and diseases of mechanotransduction
    • Ingber D.E. Mechanobiology and diseases of mechanotransduction. Ann Med 2003, 35:564-577.
    • (2003) Ann Med , vol.35 , pp. 564-577
    • Ingber, D.E.1
  • 4
    • 0016681078 scopus 로고
    • Wall stress and patterns of hypertrophy in the human left ventricle
    • Grossman W., Jones D., McLaurin L.P. Wall stress and patterns of hypertrophy in the human left ventricle. J Clin Invest 1975, 56:56-64.
    • (1975) J Clin Invest , vol.56 , pp. 56-64
    • Grossman, W.1    Jones, D.2    McLaurin, L.P.3
  • 5
    • 41449086790 scopus 로고    scopus 로고
    • Cardiac plasticity
    • Hill J.A., Olson E.N. Cardiac plasticity. N Engl J Med 2008, 358:1370-1380.
    • (2008) N Engl J Med , vol.358 , pp. 1370-1380
    • Hill, J.A.1    Olson, E.N.2
  • 7
    • 74049114704 scopus 로고    scopus 로고
    • Intramyocardial fibroblast myocyte communication
    • Kakkar R., Lee R.T. Intramyocardial fibroblast myocyte communication. Circ Res 2010, 106:47-57.
    • (2010) Circ Res , vol.106 , pp. 47-57
    • Kakkar, R.1    Lee, R.T.2
  • 8
    • 67249152096 scopus 로고    scopus 로고
    • Cardiac fibroblasts: at the heart of myocardial remodeling
    • Porter K.E., Turner N.A. Cardiac fibroblasts: at the heart of myocardial remodeling. Pharmacol Ther 2009, 123:255-278.
    • (2009) Pharmacol Ther , vol.123 , pp. 255-278
    • Porter, K.E.1    Turner, N.A.2
  • 9
    • 0002720876 scopus 로고
    • The influence of venous filling upon the rate of the heart
    • Bainbridge F.A. The influence of venous filling upon the rate of the heart. J Physiol 1915, 50:65-84.
    • (1915) J Physiol , vol.50 , pp. 65-84
    • Bainbridge, F.A.1
  • 10
    • 85137116247 scopus 로고    scopus 로고
    • Starling EH. The Linacre Lecture on the law of the heart. Cambridge;1915
    • Starling EH. The Linacre Lecture on the law of the heart. Cambridge;1915.
  • 11
    • 0032944254 scopus 로고    scopus 로고
    • The role of calcium in the response of cardiac muscle to stretch
    • Calaghan S.C., White E. The role of calcium in the response of cardiac muscle to stretch. Progr Biophys Mol Biol 1999, 71:59-90.
    • (1999) Progr Biophys Mol Biol , vol.71 , pp. 59-90
    • Calaghan, S.C.1    White, E.2
  • 13
    • 0033151961 scopus 로고    scopus 로고
    • Length modulation of active force in rat cardiac myocytes: is titin the sensor?
    • Cazorla O., Vassort G., Garnier D., Le Guennec J.Y. Length modulation of active force in rat cardiac myocytes: is titin the sensor?. J Mol Cell Cardiol 1999, 31:1215-1227.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1215-1227
    • Cazorla, O.1    Vassort, G.2    Garnier, D.3    le Guennec, J.Y.4
  • 14
    • 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. Biophys J 1995, 68:1027-1044.
    • (1995) Biophys J , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 15
    • 78549249481 scopus 로고    scopus 로고
    • Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel component of the sarcomeric M-band and is involved in stretch sensing
    • Will R.D., Eden M., Just S., Hansen A., Eder A., Frank D., et al. Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel component of the sarcomeric M-band and is involved in stretch sensing. Circ Res 2010, 107:1253-1264.
    • (2010) Circ Res , vol.107 , pp. 1253-1264
    • Will, R.D.1    Eden, M.2    Just, S.3    Hansen, A.4    Eder, A.5    Frank, D.6
  • 16
    • 0030272704 scopus 로고    scopus 로고
    • Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes
    • Bloom S., Lockard V.G., Bloom M. Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes. J Mol Cell Cardiol 1996, 28:2123-2127.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 2123-2127
    • Bloom, S.1    Lockard, V.G.2    Bloom, M.3
  • 17
    • 0031172831 scopus 로고    scopus 로고
    • Stretch-activated ion channels in the heart
    • Hu H., Sachs F. Stretch-activated ion channels in the heart. J Mol Cell Cardiol 1997, 29:1511-1523.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1511-1523
    • Hu, H.1    Sachs, F.2
  • 18
    • 0033712474 scopus 로고    scopus 로고
    • Stretch-activated currents in ventricular myocytes: amplitude and arrhythmogenic effects increase with hypertrophy
    • Kamkin A., Kiseleva I., Isenberg G. Stretch-activated currents in ventricular myocytes: amplitude and arrhythmogenic effects increase with hypertrophy. Cardiovasc Res 2000, 48:409-420.
    • (2000) Cardiovasc Res , vol.48 , pp. 409-420
    • Kamkin, A.1    Kiseleva, I.2    Isenberg, G.3
  • 19
    • 0037843239 scopus 로고    scopus 로고
    • Ion selectivity of stretch-activated cation currents in mouse ventricular myocytes
    • Kamkin A., Kiseleva I., Isenberg G. Ion selectivity of stretch-activated cation currents in mouse ventricular myocytes. Pflugers Arch 2003, 446:220-231.
    • (2003) Pflugers Arch , vol.446 , pp. 220-231
    • Kamkin, A.1    Kiseleva, I.2    Isenberg, G.3
  • 20
    • 0037373465 scopus 로고    scopus 로고
    • Activation and inactivation of a non-selective cation conductance by local mechanical deformation of acutely isolated cardiac fibroblasts
    • Kamkin A., Kiseleva I., Isenberg G. Activation and inactivation of a non-selective cation conductance by local mechanical deformation of acutely isolated cardiac fibroblasts. Cardiovasc Res 2003, 57:793-803.
    • (2003) Cardiovasc Res , vol.57 , pp. 793-803
    • Kamkin, A.1    Kiseleva, I.2    Isenberg, G.3
  • 22
    • 0037440018 scopus 로고    scopus 로고
    • Streptomycin and intracellular calcium modulate the response of single guinea-pig ventricular myocytes to axial stretch
    • Belus A., White E. Streptomycin and intracellular calcium modulate the response of single guinea-pig ventricular myocytes to axial stretch. J Physiol 2003, 546:501-509.
    • (2003) J Physiol , vol.546 , pp. 501-509
    • Belus, A.1    White, E.2
  • 23
    • 0035138535 scopus 로고    scopus 로고
    • Mechanical stress stimulates phospholipase C activity and intracellular calcium ion levels in neonatal rat cardiomyocytes
    • Ruwhof C., van Wamel J.T., Noordzij L.A., Aydin S., Harper J.C., van der Laarse A. Mechanical stress stimulates phospholipase C activity and intracellular calcium ion levels in neonatal rat cardiomyocytes. Cell Calcium 2001, 29:73-83.
    • (2001) Cell Calcium , vol.29 , pp. 73-83
    • Ruwhof, C.1    van Wamel, J.T.2    Noordzij, L.A.3    Aydin, S.4    Harper, J.C.5    van der Laarse, A.6
  • 24
    • 0032583085 scopus 로고    scopus 로고
    • 2+]i in rat atrial myocytes: role of increased troponin C affinity and stretch-activated ion channels
    • 2+]i in rat atrial myocytes: role of increased troponin C affinity and stretch-activated ion channels. Circ Res 1998, 83:1165-1177.
    • (1998) Circ Res , vol.83 , pp. 1165-1177
    • Tavi, P.1    Han, C.2    Weckstrom, M.3
  • 25
    • 0035338924 scopus 로고    scopus 로고
    • Cardiac mechanotransduction: from sensing to disease and treatment
    • Tavi P., Laine M., Weckstrom M., Ruskoaho H. Cardiac mechanotransduction: from sensing to disease and treatment. Trends Pharmacol Sci 2001, 22:254-260.
    • (2001) Trends Pharmacol Sci , vol.22 , pp. 254-260
    • Tavi, P.1    Laine, M.2    Weckstrom, M.3    Ruskoaho, H.4
  • 26
    • 0027234582 scopus 로고
    • Targeted developmental overexpression of calmodulin induces proliferative and hypertrophic growth of cardiomyocytes in transgenic mice
    • Gruver C.L., DeMayo F., Goldstein M.A., Means A.R. Targeted developmental overexpression of calmodulin induces proliferative and hypertrophic growth of cardiomyocytes in transgenic mice. Endocrinology 1993, 133:376-388.
    • (1993) Endocrinology , vol.133 , pp. 376-388
    • Gruver, C.L.1    DeMayo, F.2    Goldstein, M.A.3    Means, A.R.4
  • 27
    • 0034685545 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II and calcineurin play critical roles in endothelin-1-induced cardiomyocyte hypertrophy
    • 2+/calmodulin-dependent kinase II and calcineurin play critical roles in endothelin-1-induced cardiomyocyte hypertrophy. J Biol Chem 2000, 275:15239-15245.
    • (2000) J Biol Chem , vol.275 , pp. 15239-15245
    • Zhu, W.1    Zou, Y.2    Shiojima, I.3    Kudoh, S.4    Aikawa, R.5    Hayashi, D.6
  • 28
    • 0034635987 scopus 로고    scopus 로고
    • Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases
    • Lu J., McKinsey T.A., Nicol R.L., Olson E.N. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc Natl Acad Sci U S A 2000, 97:4070-4075.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Nicol, R.L.3    Olson, E.N.4
  • 30
    • 3242772151 scopus 로고    scopus 로고
    • Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs
    • Molkentin J.D. Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs. Cardiovasc Res 2004, 63:467-475.
    • (2004) Cardiovasc Res , vol.63 , pp. 467-475
    • Molkentin, J.D.1
  • 31
    • 0037134462 scopus 로고    scopus 로고
    • Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins
    • Frey N., Olson E.N. Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. J Biol Chem 2002, 277:13998-14004.
    • (2002) J Biol Chem , vol.277 , pp. 13998-14004
    • Frey, N.1    Olson, E.N.2
  • 34
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits
    • Crespo P., Xu N., Simonds W.F., Gutkind J.S. Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits. Nature 1994, 369:418-420.
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 35
    • 0029002493 scopus 로고
    • A direct interaction between G-protein beta gamma subunits and the Raf-1 protein kinase
    • Pumiglia K.M., LeVine H., Haske T., Habib T., Jove R., Decker S.J. A direct interaction between G-protein beta gamma subunits and the Raf-1 protein kinase. J Biol Chem 1995, 270:14251-14254.
    • (1995) J Biol Chem , vol.270 , pp. 14251-14254
    • Pumiglia, K.M.1    LeVine, H.2    Haske, T.3    Habib, T.4    Jove, R.5    Decker, S.J.6
  • 36
    • 0034681226 scopus 로고    scopus 로고
    • Gbetagamma-dependent phosphoinositide 3-kinase activation in hearts with in vivo pressure overload hypertrophy
    • Naga Prasad S.V., Esposito G., Mao L., Koch W.J., Rockman H.A. Gbetagamma-dependent phosphoinositide 3-kinase activation in hearts with in vivo pressure overload hypertrophy. J Biol Chem 2000, 275:4693-4698.
    • (2000) J Biol Chem , vol.275 , pp. 4693-4698
    • Naga Prasad, S.V.1    Esposito, G.2    Mao, L.3    Koch, W.J.4    Rockman, H.A.5
  • 37
    • 0031859711 scopus 로고    scopus 로고
    • Equibiaxial strain and strain rate stimulate early activation of G proteins in cardiac fibroblasts
    • Gudi S.R., Lee A.A., Clark C.B., Frangos J.A. Equibiaxial strain and strain rate stimulate early activation of G proteins in cardiac fibroblasts. Am J Physiol Cell Physiol 1998, 274:C1424-C1428.
    • (1998) Am J Physiol Cell Physiol , vol.274 , pp. C1424-C1428
    • Gudi, S.R.1    Lee, A.A.2    Clark, C.B.3    Frangos, J.A.4
  • 38
    • 0032543959 scopus 로고    scopus 로고
    • Enhanced Galphaq signaling: a common pathway mediates cardiac hypertrophy and apoptotic heart failure
    • Adams J.W., Sakata Y., Davis M.G., Sah V.P., Wang Y., Liggett S.B., et al. Enhanced Galphaq signaling: a common pathway mediates cardiac hypertrophy and apoptotic heart failure. Proc Natl Acad Sci USA 1998, 95:10140-10145.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10140-10145
    • Adams, J.W.1    Sakata, Y.2    Davis, M.G.3    Sah, V.P.4    Wang, Y.5    Liggett, S.B.6
  • 39
    • 0027176441 scopus 로고
    • The alpha 1A-adrenergic receptor subtype mediates biochemical, molecular, and morphologic features of cultured myocardial cell hypertrophy
    • Knowlton K.U., Michel M.C., Itani M., Shubeita H.E., Ishihara K., Brown J.H., et al. The alpha 1A-adrenergic receptor subtype mediates biochemical, molecular, and morphologic features of cultured myocardial cell hypertrophy. J Biol Chem 1993, 268:15374-15380.
    • (1993) J Biol Chem , vol.268 , pp. 15374-15380
    • Knowlton, K.U.1    Michel, M.C.2    Itani, M.3    Shubeita, H.E.4    Ishihara, K.5    Brown, J.H.6
  • 40
    • 0034970775 scopus 로고    scopus 로고
    • MEK1/2-ERK1/2 mediates alpha1-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes
    • Xiao L., Pimental D.R., Amin J.K., Singh K., Sawyer D.B., Colucci W.S. MEK1/2-ERK1/2 mediates alpha1-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes. J Mol Cell Cardiol 2001, 33:779-787.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 779-787
    • Xiao, L.1    Pimental, D.R.2    Amin, J.K.3    Singh, K.4    Sawyer, D.B.5    Colucci, W.S.6
  • 41
    • 0033844365 scopus 로고    scopus 로고
    • The alpha(1)-adrenoceptor subtype- and protein kinase C isoform-dependence of Norepinephrine's actions in cardiomyocytes
    • Rohde S., Sabri A., Kamasamudran R., Steinberg S.F. The alpha(1)-adrenoceptor subtype- and protein kinase C isoform-dependence of Norepinephrine's actions in cardiomyocytes. J Mol Cell Cardiol 2000, 32:1193-1209.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 1193-1209
    • Rohde, S.1    Sabri, A.2    Kamasamudran, R.3    Steinberg, S.F.4
  • 42
    • 0030807080 scopus 로고    scopus 로고
    • Rapamycin inhibits alpha 1-adrenergic receptor-stimulated cardiac myocyte hypertrophy but not activation of hypertrophy-associated genes. Evidence for involvement of p70 S6 kinase
    • Boluyt M.O., Zheng J.S., Younes A., Long X., O'Neill L., Silverman H., et al. Rapamycin inhibits alpha 1-adrenergic receptor-stimulated cardiac myocyte hypertrophy but not activation of hypertrophy-associated genes. Evidence for involvement of p70 S6 kinase. Circ Res 1997, 81:176-186.
    • (1997) Circ Res , vol.81 , pp. 176-186
    • Boluyt, M.O.1    Zheng, J.S.2    Younes, A.3    Long, X.4    O'Neill, L.5    Silverman, H.6
  • 43
    • 0035170002 scopus 로고    scopus 로고
    • Beta-adrenoceptor stimulation attenuates the hypertrophic effect of alpha-adrenoceptor stimulation in adult rat ventricular cardiomyocytes
    • Schafer M., Ponicke K., Heinroth-Hoffmann I., Brodde O.E., Piper H.M., Schluter K.D. Beta-adrenoceptor stimulation attenuates the hypertrophic effect of alpha-adrenoceptor stimulation in adult rat ventricular cardiomyocytes. J Am Coll Cardiol 2001, 37:300-307.
    • (2001) J Am Coll Cardiol , vol.37 , pp. 300-307
    • Schafer, M.1    Ponicke, K.2    Heinroth-Hoffmann, I.3    Brodde, O.E.4    Piper, H.M.5    Schluter, K.D.6
  • 44
    • 0034602839 scopus 로고    scopus 로고
    • Beta(2)-adrenergic receptor overexpression exacerbates development of heart failure after aortic stenosis
    • Du X.J., Autelitano D.J., Dilley R.J., Wang B., Dart A.M., Woodcock E.A. beta(2)-adrenergic receptor overexpression exacerbates development of heart failure after aortic stenosis. Circulation 2000, 101:71-77.
    • (2000) Circulation , vol.101 , pp. 71-77
    • Du, X.J.1    Autelitano, D.J.2    Dilley, R.J.3    Wang, B.4    Dart, A.M.5    Woodcock, E.A.6
  • 45
    • 34247113814 scopus 로고    scopus 로고
    • Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology
    • Higuchi S., Ohtsu H., Suzuki H., Shirai H., Frank G.D., Eguchi S. Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology. Clin Sci 2007, 112:417-428.
    • (2007) Clin Sci , vol.112 , pp. 417-428
    • Higuchi, S.1    Ohtsu, H.2    Suzuki, H.3    Shirai, H.4    Frank, G.D.5    Eguchi, S.6
  • 46
    • 0033811089 scopus 로고    scopus 로고
    • Angiotensin II-induced cardiac hypertrophy is associated with different mitogen-activated protein kinase activation in normotensive and hypertensive mice
    • Pellieux C., Sauthier T., Aubert J.F., Brunner H.R., Pedrazzini T. Angiotensin II-induced cardiac hypertrophy is associated with different mitogen-activated protein kinase activation in normotensive and hypertensive mice. J Hypertens 2000, 18:1307-1317.
    • (2000) J Hypertens , vol.18 , pp. 1307-1317
    • Pellieux, C.1    Sauthier, T.2    Aubert, J.F.3    Brunner, H.R.4    Pedrazzini, T.5
  • 47
    • 0030765570 scopus 로고    scopus 로고
    • Role of angiotensin II in activation of the JAK/STAT pathway induced by acute pressure overload in the rat heart
    • Pan J., Fukuda K., Kodama H., Makino S., Takahashi T., Sano M., et al. Role of angiotensin II in activation of the JAK/STAT pathway induced by acute pressure overload in the rat heart. Circ Res 1997, 81:611-617.
    • (1997) Circ Res , vol.81 , pp. 611-617
    • Pan, J.1    Fukuda, K.2    Kodama, H.3    Makino, S.4    Takahashi, T.5    Sano, M.6
  • 48
    • 2942751868 scopus 로고    scopus 로고
    • Mechanical stress activates angiotensin II type 1 receptor without the involvement of angiotensin II
    • Zou Y., Akazawa H., Qin Y., Sano M., Takano H., Minamino T., et al. Mechanical stress activates angiotensin II type 1 receptor without the involvement of angiotensin II. Nature Cell Biol 2004, 6:499-506.
    • (2004) Nature Cell Biol , vol.6 , pp. 499-506
    • Zou, Y.1    Akazawa, H.2    Qin, Y.3    Sano, M.4    Takano, H.5    Minamino, T.6
  • 49
    • 77955494734 scopus 로고    scopus 로고
    • Mechanical stress-evoked but angiotensin II-independent activation of angiotensin II type 1 receptor induces cardiac hypertrophy through calcineurin pathway
    • Zhou N., Li L., Wu J., Gong H., Niu Y., Sun A., et al. Mechanical stress-evoked but angiotensin II-independent activation of angiotensin II type 1 receptor induces cardiac hypertrophy through calcineurin pathway. Biochem Biophys Res Commun 2010, 397:263-269.
    • (2010) Biochem Biophys Res Commun , vol.397 , pp. 263-269
    • Zhou, N.1    Li, L.2    Wu, J.3    Gong, H.4    Niu, Y.5    Sun, A.6
  • 50
    • 0033711108 scopus 로고    scopus 로고
    • The extracellular matrix and the cytoskeleton in heart hypertrophy and failure
    • Jane-Lise S., Corda S., Chassagne C., Rappaport L. The extracellular matrix and the cytoskeleton in heart hypertrophy and failure. Heart Fail Rev 2000, 5:239-250.
    • (2000) Heart Fail Rev , vol.5 , pp. 239-250
    • Jane-Lise, S.1    Corda, S.2    Chassagne, C.3    Rappaport, L.4
  • 51
    • 0035134028 scopus 로고    scopus 로고
    • Semiquantitative analysis of collagen types in the hypertrophied left ventricle
    • Linehan K.A., Seymour A.-M.L., Williams P.E. Semiquantitative analysis of collagen types in the hypertrophied left ventricle. J Anat 2001, 198:83-92.
    • (2001) J Anat , vol.198 , pp. 83-92
    • Linehan, K.A.1    Seymour, A.-M.L.2    Williams, P.E.3
  • 53
    • 0035827723 scopus 로고    scopus 로고
    • Integrins and the myocardium
    • Ross R.S., Borg T.K. Integrins and the myocardium. Circ Res 2001, 88:1112-1119.
    • (2001) Circ Res , vol.88 , pp. 1112-1119
    • Ross, R.S.1    Borg, T.K.2
  • 54
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling
    • Calderwood D.A., Shattil S.J., Ginsberg M.H. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem 2000, 275:22607-22610.
    • (2000) J Biol Chem , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 55
    • 0036734093 scopus 로고    scopus 로고
    • A reevaluation of integrins as regulators of angiogenesis
    • Hynes R.O. A reevaluation of integrins as regulators of angiogenesis. Nat Med 2002, 8:918-921.
    • (2002) Nat Med , vol.8 , pp. 918-921
    • Hynes, R.O.1
  • 57
    • 3242753503 scopus 로고    scopus 로고
    • Molecular and mechanical synergy: crosstalk between integrins and growth factor receptors
    • Ross R.S. Molecular and mechanical synergy: crosstalk between integrins and growth factor receptors. Cardiovasc Res 2004, 63:381-390.
    • (2004) Cardiovasc Res , vol.63 , pp. 381-390
    • Ross, R.S.1
  • 60
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: the Achilles' heel of Herculean muscle
    • Ervasti J.M. Costameres: the Achilles' heel of Herculean muscle. J Biol Chem 2003, 278:13591-13594.
    • (2003) J Biol Chem , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 61
    • 0034634653 scopus 로고    scopus 로고
    • Integrin activation and focal complex formation in cardiac hypertrophy
    • Laser M., Willey C.D., Jiang W., Cooper G., Menick D.R., Zile M.R., et al. Integrin activation and focal complex formation in cardiac hypertrophy. J Biol Chem 2000, 275:35624-35630.
    • (2000) J Biol Chem , vol.275 , pp. 35624-35630
    • Laser, M.1    Willey, C.D.2    Jiang, W.3    Cooper, G.4    Menick, D.R.5    Zile, M.R.6
  • 63
    • 0028324634 scopus 로고
    • Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin
    • Wood C.K., Turner C.E., Jackson P., Critchley D.R. Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin. J Cell Sci 1994, 107:709-717.
    • (1994) J Cell Sci , vol.107 , pp. 709-717
    • Wood, C.K.1    Turner, C.E.2    Jackson, P.3    Critchley, D.R.4
  • 64
    • 0028980418 scopus 로고
    • Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK
    • Tachibana K., Sato T., D'Avirro N., Morimoto C. Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J Exper Med 1995, 182:1089-1099.
    • (1995) J Exper Med , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 65
    • 0032525330 scopus 로고    scopus 로고
    • Fl1 Integrins participate in the hypertrophic response of rat ventricular myocytes
    • Ross R.S., Pham C., Shai S.-Y., Goldhaber J.I., Fenczik C., Glembotski C.C., et al. fl1 Integrins participate in the hypertrophic response of rat ventricular myocytes. Circ Res 1998, 82:1160-1172.
    • (1998) Circ Res , vol.82 , pp. 1160-1172
    • Ross, R.S.1    Pham, C.2    Shai, S.-Y.3    Goldhaber, J.I.4    Fenczik, C.5    Glembotski, C.C.6
  • 66
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li F., Zhang Y., Wu C. Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J Cell Sci 1999, 112:4589-4599.
    • (1999) J Cell Sci , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 67
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S., Calderwood D.A., Ginsberg M.H. Integrin cytoplasmic domain-binding proteins. J Cell Sci 2000, 113:3563-3571.
    • (2000) J Cell Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 68
    • 44349136151 scopus 로고    scopus 로고
    • Cardiac developmental defects and eccentric right ventricular hypertrophy in cardiomyocyte focal adhesion kinase (FAK) conditional knockout mice
    • Peng X., Wu X., Druso J.E., Wei H., Park A.Y.-J., Kraus M.S. Cardiac developmental defects and eccentric right ventricular hypertrophy in cardiomyocyte focal adhesion kinase (FAK) conditional knockout mice. Proc Natl Acad Sci USA 2008, 105:6638-6643.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6638-6643
    • Peng, X.1    Wu, X.2    Druso, J.E.3    Wei, H.4    Park, A.Y.-J.5    Kraus, M.S.6
  • 69
    • 0042266791 scopus 로고    scopus 로고
    • Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes
    • Torsoni A.S., Constancio S.S., Nadruz W., Hanks S.K., Franchini K.G. Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes. Circ Res 2003, 93:140-147.
    • (2003) Circ Res , vol.93 , pp. 140-147
    • Torsoni, A.S.1    Constancio, S.S.2    Nadruz, W.3    Hanks, S.K.4    Franchini, K.G.5
  • 71
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases
    • Calalb M.B., Polte T.R., Hanks S.K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 1995, 15:954-963.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 72
    • 0036084426 scopus 로고    scopus 로고
    • Load-induced focal adhesion kinase activation in the myocardium: role of stretch and contractile activity
    • Domingos P.P., Fonseca P.M., Nadruz W., Franchini K.G. Load-induced focal adhesion kinase activation in the myocardium: role of stretch and contractile activity. Am J Physiol Heart Circ Physiol 2002, 282:H556-H564.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282 , pp. H556-H564
    • Domingos, P.P.1    Fonseca, P.M.2    Nadruz, W.3    Franchini, K.G.4
  • 73
    • 0035947577 scopus 로고    scopus 로고
    • Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397
    • Salazar E.P., Rozengurt E. Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397. J Biol Chem 2001, 276:17788-17795.
    • (2001) J Biol Chem , vol.276 , pp. 17788-17795
    • Salazar, E.P.1    Rozengurt, E.2
  • 75
    • 0034705523 scopus 로고    scopus 로고
    • A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes
    • Taylor J.M., Rovin J.D., Parsons J.T. A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes. J Biol Chem 2000, 275:19250-19257.
    • (2000) J Biol Chem , vol.275 , pp. 19250-19257
    • Taylor, J.M.1    Rovin, J.D.2    Parsons, J.T.3
  • 76
    • 0033609354 scopus 로고    scopus 로고
    • Pulsatile stretch activates mitogen-activated protein kinase (mapk) family members and focal adhesion kinase (p125fak) in cultured rat cardiac myocytes
    • Seko Y., Seko Y., Takahashi N., Tobe K., Kadowaki T., Yazaki Y. Pulsatile stretch activates mitogen-activated protein kinase (mapk) family members and focal adhesion kinase (p125fak) in cultured rat cardiac myocytes. Biochem Biophys Res Comm 1999, 259:8-14.
    • (1999) Biochem Biophys Res Comm , vol.259 , pp. 8-14
    • Seko, Y.1    Seko, Y.2    Takahashi, N.3    Tobe, K.4    Kadowaki, T.5    Yazaki, Y.6
  • 77
    • 0033612355 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces activation and subcellular translocation of focal adhesion kinase (p125fak) in cultured rat cardiac myocytes
    • Takahashi N., Seko Y., Noiri E., Tobe K., Kadowaki T., Sabe H., et al. Vascular endothelial growth factor induces activation and subcellular translocation of focal adhesion kinase (p125fak) in cultured rat cardiac myocytes. Circ Res 1999, 84:1194-1202.
    • (1999) Circ Res , vol.84 , pp. 1194-1202
    • Takahashi, N.1    Seko, Y.2    Noiri, E.3    Tobe, K.4    Kadowaki, T.5    Sabe, H.6
  • 78
  • 79
    • 24044533528 scopus 로고    scopus 로고
    • Distinct pathways regulate expression of cardiac electrical and mechanical junction proteins in response to stretch
    • Yamada K., Green K.G., Samarel A.M., Saffitz J.E. Distinct pathways regulate expression of cardiac electrical and mechanical junction proteins in response to stretch. Circ Res 2005, 97:346-353.
    • (2005) Circ Res , vol.97 , pp. 346-353
    • Yamada, K.1    Green, K.G.2    Samarel, A.M.3    Saffitz, J.E.4
  • 80
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen H.C., Guan J.L. Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1994, 91:10148-10152.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10148-10152
    • Chen, H.C.1    Guan, J.L.2
  • 82
    • 25444524533 scopus 로고    scopus 로고
    • RhoA/ROCK signaling is critical to FAK activation by cyclic stretch in cardiac myocytes
    • Torsoni A.S., Marin T.M., Velloso L.A., Franchini K.G. RhoA/ROCK signaling is critical to FAK activation by cyclic stretch in cardiac myocytes. Am J Physiol Heart Circ Physiol 2005, 289:H1488-H1496.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , pp. H1488-H1496
    • Torsoni, A.S.1    Marin, T.M.2    Velloso, L.A.3    Franchini, K.G.4
  • 84
    • 33748250034 scopus 로고    scopus 로고
    • Integrin-linked kinase, a novel component of the cardiac mechanical stretch sensor, controls contractility in the zebrafish heart
    • Bendig G., Grimmler M., Huttner I.G., Wessels G., Dahme T., Just S., et al. Integrin-linked kinase, a novel component of the cardiac mechanical stretch sensor, controls contractility in the zebrafish heart. Genes Dev 2006, 20:2361-2372.
    • (2006) Genes Dev , vol.20 , pp. 2361-2372
    • Bendig, G.1    Grimmler, M.2    Huttner, I.G.3    Wessels, G.4    Dahme, T.5    Just, S.6
  • 85
    • 18844363699 scopus 로고    scopus 로고
    • ILK mediates actin filament rearrangements and cell migration and invasion through PI3K//Akt//Rac1 signaling
    • Qian Y., Zhong X., Flynn D.C., Zheng J.Z., Qiao M., Wu C., et al. ILK mediates actin filament rearrangements and cell migration and invasion through PI3K//Akt//Rac1 signaling. Oncogene 2005, 24:3154-3165.
    • (2005) Oncogene , vol.24 , pp. 3154-3165
    • Qian, Y.1    Zhong, X.2    Flynn, D.C.3    Zheng, J.Z.4    Qiao, M.5    Wu, C.6
  • 86
    • 27144445241 scopus 로고    scopus 로고
    • Role of the integrin-linked kinase//PINCH1//alpha-parvin complex in cardiac myocyte hypertrophy
    • Chen H., Huang X.N., Yan W., Chen K., Guo L., Tummalapali L., et al. Role of the integrin-linked kinase//PINCH1//alpha-parvin complex in cardiac myocyte hypertrophy. Lab Invest 2005, 85:1342-1356.
    • (2005) Lab Invest , vol.85 , pp. 1342-1356
    • Chen, H.1    Huang, X.N.2    Yan, W.3    Chen, K.4    Guo, L.5    Tummalapali, L.6
  • 87
    • 11144225205 scopus 로고    scopus 로고
    • Integrin-linked kinase: a cancer therapeutic target unique among its ILK
    • Hannigan G., Troussard A.A., Dedhar S. Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Natl Rev Cancer 2005, 5:51-63.
    • (2005) Natl Rev Cancer , vol.5 , pp. 51-63
    • Hannigan, G.1    Troussard, A.A.2    Dedhar, S.3
  • 88
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y., Huang Y., Zhang Y., Hua Y., Wu C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol 2001, 153:585-598.
    • (2001) J Cell Biol , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 89
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne M., Tan C., Gray V., Rue L., Woodgett J., Dedhar S. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci USA 1998, 95:11211-11216.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5    Dedhar, S.6
  • 90
    • 62349105876 scopus 로고    scopus 로고
    • Cardiac regulation by phosphoinositide 3-kinases and PTEN
    • Oudit G.Y., Penninger J.M. Cardiac regulation by phosphoinositide 3-kinases and PTEN. Cardiovasc Res 2009, 82:250-260.
    • (2009) Cardiovasc Res , vol.82 , pp. 250-260
    • Oudit, G.Y.1    Penninger, J.M.2
  • 91
    • 33751226584 scopus 로고    scopus 로고
    • Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice
    • Lu H., Fedak P.W.M., Dai X., Du C., Zhou Y.-Q., Henkelman M., et al. Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice. Circulation 2006, 114:2271-2279.
    • (2006) Circulation , vol.114 , pp. 2271-2279
    • Lu, H.1    Fedak, P.W.M.2    Dai, X.3    Du, C.4    Zhou, Y.-Q.5    Henkelman, M.6
  • 92
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • White D.E., Coutu P., Shi Y.-F., Tardif J.-C., Nattel S., Arnaud R., et al. Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Devel 2006, 20:2355-2360.
    • (2006) Genes Devel , vol.20 , pp. 2355-2360
    • White, D.E.1    Coutu, P.2    Shi, Y.-F.3    Tardif, J.-C.4    Nattel, S.5    Arnaud, R.6
  • 93
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • Ahn A.H., Kunkel L.M. The structural and functional diversity of dystrophin. Nat Genet 1993, 3:283-291.
    • (1993) Nat Genet , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 95
    • 2342621479 scopus 로고    scopus 로고
    • The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma
    • Lapidos K.A., Kakkar R., McNally E.M. The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma. Circ Res 2004, 94:1023-1031.
    • (2004) Circ Res , vol.94 , pp. 1023-1031
    • Lapidos, K.A.1    Kakkar, R.2    McNally, E.M.3
  • 97
    • 0037236642 scopus 로고    scopus 로고
    • Melusin, a muscle-specific integrin ?1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload
    • Brancaccio M., Fratta L., Notte A., Hirsch E., Poulet R., Guazzone S., et al. Melusin, a muscle-specific integrin ?1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload. Nat Med 2003, 9:68-75.
    • (2003) Nat Med , vol.9 , pp. 68-75
    • Brancaccio, M.1    Fratta, L.2    Notte, A.3    Hirsch, E.4    Poulet, R.5    Guazzone, S.6
  • 98
    • 20344399430 scopus 로고    scopus 로고
    • Cardiac overexpression of melusin protects from dilated cardiomyopathy due to long-standing pressure overload
    • De Acetis M., Notte A., Accornero F., Selvetella G., Brancaccio M., Vecchione C., et al. Cardiac overexpression of melusin protects from dilated cardiomyopathy due to long-standing pressure overload. Circ Res 2005, 96:1087-1094.
    • (2005) Circ Res , vol.96 , pp. 1087-1094
    • de Acetis, M.1    Notte, A.2    Accornero, F.3    Selvetella, G.4    Brancaccio, M.5    Vecchione, C.6
  • 99
    • 77957976010 scopus 로고    scopus 로고
    • Nebulette mutations in cardiac remodeling: big effects from a small mechanosensor
    • Ram R., Blaxall B.C. Nebulette mutations in cardiac remodeling: big effects from a small mechanosensor. J Am Coll Cardiol 2010, 56:1503-1505.
    • (2010) J Am Coll Cardiol , vol.56 , pp. 1503-1505
    • Ram, R.1    Blaxall, B.C.2
  • 100
    • 77958011915 scopus 로고    scopus 로고
    • Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis
    • Purevjav E., Varela J., Morgado M., Kearney D.L., Li H., Taylor M.D., et al. Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis. J Am Coll Cardiol 2010, 56:1493-1502.
    • (2010) J Am Coll Cardiol , vol.56 , pp. 1493-1502
    • Purevjav, E.1    Varela, J.2    Morgado, M.3    Kearney, D.L.4    Li, H.5    Taylor, M.D.6
  • 101
    • 79953172201 scopus 로고    scopus 로고
    • Cardiac Z-disc signaling network
    • Frank D., Frey N. Cardiac Z-disc signaling network. J Biol Chem. 2011, 286:9897-9904.
    • (2011) J Biol Chem , vol.286 , pp. 9897-9904
    • Frank, D.1    Frey, N.2
  • 102
    • 1642458404 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes
    • Purcell N.H., Darwis D., Bueno O.F., Muller J.M., Schule R., Molkentin J.D. Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes. Mol Cell Biol 2004, 24:1081-1095.
    • (2004) Mol Cell Biol , vol.24 , pp. 1081-1095
    • Purcell, N.H.1    Darwis, D.2    Bueno, O.F.3    Muller, J.M.4    Schule, R.5    Molkentin, J.D.6
  • 103
    • 37549065527 scopus 로고    scopus 로고
    • Role of the sarcomeric Z-disc in the pathogenesis of cardiomyopathy
    • Frank D., Kuhn C., Katus H.A., Frey N. Role of the sarcomeric Z-disc in the pathogenesis of cardiomyopathy. Future Cardiol 2007, 3:611-622.
    • (2007) Future Cardiol , vol.3 , pp. 611-622
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 104
    • 33846218274 scopus 로고    scopus 로고
    • Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein
    • Boateng S.Y., Belin R.J., Geenen D.L., Margulies K.B., Martin J.L., Hoshijima M., et al. Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein. Am J Physiol Heart Circ Physiol 2007, 292:H259-H269.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292 , pp. H259-H269
    • Boateng, S.Y.1    Belin, R.J.2    Geenen, D.L.3    Margulies, K.B.4    Martin, J.L.5    Hoshijima, M.6
  • 105
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • Knoll R., Hoshijima M., Hoffman H.M., Person V., Lorenzen-Schmidt I., Bang M.L., et al. The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 2002, 111:943-955.
    • (2002) Cell , vol.111 , pp. 943-955
    • Knoll, R.1    Hoshijima, M.2    Hoffman, H.M.3    Person, V.4    Lorenzen-Schmidt, I.5    Bang, M.L.6
  • 106
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin J.D., Lu J.R., Antos C.L., Markham B., Richardson J., Robbins J., et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 1998, 93:215-228.
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1    Lu, J.R.2    Antos, C.L.3    Markham, B.4    Richardson, J.5    Robbins, J.6
  • 107
    • 84924091885 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
    • Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol 2001, 155:393-404.
    • (2001) J Cell Biol , vol.155 , pp. 393-404
    • Weins, A.1    Schwarz, K.2    Faul, C.3    Barisoni, L.4    Linke, W.A.5    Mundel, P.6
  • 108
    • 36849051314 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes
    • 2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes. Mol Cell Biol 2007, 27:8215-8227.
    • (2007) Mol Cell Biol , vol.27 , pp. 8215-8227
    • Faul, C.1    Dhume, A.2    Schecter, A.D.3    Mundel, P.4
  • 109
    • 79958838357 scopus 로고    scopus 로고
    • Conformation-regulated mechanosensory control via titin domains in cardiac muscle
    • Voelkel T., Linke W. Conformation-regulated mechanosensory control via titin domains in cardiac muscle. Pflügers Arch 2011, 462(1):143-154.
    • (2011) Pflügers Arch , vol.462 , Issue.1 , pp. 143-154
    • Voelkel, T.1    Linke, W.2
  • 110
    • 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 W.A., Rudy D.E., Centner T., Gautel M., Witt C., Labeit S., et al. 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
  • 111
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • Lange S., Auerbach D., McLoughlin P., Perriard E., Schafer B.W., Perriard J.-C., et al. Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2. J Cell Sci 2002, 115:4925-4936.
    • (2002) J Cell Sci , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    McLoughlin, P.3    Perriard, E.4    Schafer, B.W.5    Perriard, J.-C.6
  • 112
    • 57449117141 scopus 로고    scopus 로고
    • An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice
    • Sheikh F., Raskin A., Chu P.-H., Lange S., Domenighetti A.A., Zheng M., et al. An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice. J Clin Invest 2008, 118:3870-3880.
    • (2008) J Clin Invest , vol.118 , pp. 3870-3880
    • Sheikh, F.1    Raskin, A.2    Chu, P.-H.3    Lange, S.4    Domenighetti, A.A.5    Zheng, M.6
  • 113
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., et al. Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 1998, 395:863-869.
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    van der Ven, P.F.M.2    Wilm, M.3    Mues, A.4    Young, P.5    Furst, D.O.6
  • 114
    • 76249114882 scopus 로고    scopus 로고
    • Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules
    • Puchner E.M., Gaub H.E. Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules. Angew Chem Int Ed 2010, 49:1147-1150.
    • (2010) Angew Chem Int Ed , vol.49 , pp. 1147-1150
    • Puchner, E.M.1    Gaub, H.E.2
  • 115
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005, 308:1599-1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 116
    • 77449109551 scopus 로고    scopus 로고
    • Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes
    • Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., et al. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J Biol Chem 2009, 285:3487-3498.
    • (2009) J Biol Chem , vol.285 , pp. 3487-3498
    • Haque, F.1    Mazzeo, D.2    Patel, J.T.3    Smallwood, D.T.4    Ellis, J.A.5    Shanahan, C.M.6
  • 117
    • 0030272704 scopus 로고    scopus 로고
    • Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes
    • Bloom S., Lockard V.G., Bloom M. Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes. J Mol Cell Cardiol 1996, 28:2123-2127.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 2123-2127
    • Bloom, S.1    Lockard, V.G.2    Bloom, M.3
  • 118
    • 77956187161 scopus 로고    scopus 로고
    • Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis
    • Brosig M., Ferralli J., Gelman L., Chiquet M., Chiquet-Ehrismann R. Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis. Int J Biochem Cell Biol 2010, 42:1717-1728.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1717-1728
    • Brosig, M.1    Ferralli, J.2    Gelman, L.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 119
    • 67651056405 scopus 로고    scopus 로고
    • Lamin A/C deficiency as a cause of familial dilated cardiomyopathy
    • 10.1097/HCO.0b013e32832a11c6
    • Malhotra R., Mason P.K. Lamin A/C deficiency as a cause of familial dilated cardiomyopathy. Curr Opin Cardiol 2009, 24:203-208. 10.1097/HCO.0b013e32832a11c6.
    • (2009) Curr Opin Cardiol , vol.24 , pp. 203-208
    • Malhotra, R.1    Mason, P.K.2
  • 120
    • 24144481867 scopus 로고    scopus 로고
    • Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
    • Lammerding J., Hsiao J., Schulze P.C., Kozlov S., Stewart C.L., Lee R.T. Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. J Cell Biol 2005, 170:781-791.
    • (2005) J Cell Biol , vol.170 , pp. 781-791
    • Lammerding, J.1    Hsiao, J.2    Schulze, P.C.3    Kozlov, S.4    Stewart, C.L.5    Lee, R.T.6
  • 121
    • 66149137505 scopus 로고    scopus 로고
    • Modulation of actin isoform expression before the transition from experimental compensated pressure-overload cardiac hypertrophy to decompensation
    • Berni R., Savi M., Bocchi L., Delucchi F., Musso E., Chaponnier C., et al. Modulation of actin isoform expression before the transition from experimental compensated pressure-overload cardiac hypertrophy to decompensation. Am J Physiol Heart Circ Physiol 2009, 296:H1625-H1632.
    • (2009) Am J Physiol Heart Circ Physiol , vol.296 , pp. H1625-H1632
    • Berni, R.1    Savi, M.2    Bocchi, L.3    Delucchi, F.4    Musso, E.5    Chaponnier, C.6
  • 122
    • 0033550149 scopus 로고    scopus 로고
    • Regulation of cardiac myocyte protein turnover and myofibrillar structure in vitro by specific directions of stretch
    • Simpson D.G., Majeski M., Borg T.K., Terracio L. Regulation of cardiac myocyte protein turnover and myofibrillar structure in vitro by specific directions of stretch. Circ Res 1999, 85:e59-e69.
    • (1999) Circ Res , vol.85 , pp. e59-e69
    • Simpson, D.G.1    Majeski, M.2    Borg, T.K.3    Terracio, L.4
  • 123
    • 27544435992 scopus 로고    scopus 로고
    • Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement
    • Yoshigi M., Hoffman L.M., Jensen C.C., Yost H.J., Beckerle M.C. Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement. J Cell Biol 2005, 171:209-215.
    • (2005) J Cell Biol , vol.171 , pp. 209-215
    • Yoshigi, M.1    Hoffman, L.M.2    Jensen, C.C.3    Yost, H.J.4    Beckerle, M.C.5
  • 125
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multifunctional actin regulatory protein
    • Sun H.Q., Yamamoto M., Mejillano M., Yin H.L. Gelsolin, a multifunctional actin regulatory protein. J Biol Chem 1999, 274:33179-33182.
    • (1999) J Biol Chem , vol.274 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 126
    • 0035861686 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin
    • Chellaiah M.A., Biswas R.S., Yuen D., Alvarez U.M., Hruska K.A. Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin. J Biol Chem 2001, 276:47434-47444.
    • (2001) J Biol Chem , vol.276 , pp. 47434-47444
    • Chellaiah, M.A.1    Biswas, R.S.2    Yuen, D.3    Alvarez, U.M.4    Hruska, K.A.5
  • 127
    • 0034687593 scopus 로고    scopus 로고
    • Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays
    • Yang J., Moravec C.S., Sussman M.A., DiPaola N.R., Fu D., Hawthorn L., et al. Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays. Circulation 2000, 102:3046-3052.
    • (2000) Circulation , vol.102 , pp. 3046-3052
    • Yang, J.1    Moravec, C.S.2    Sussman, M.A.3    DiPaola, N.R.4    Fu, D.5    Hawthorn, L.6
  • 129
    • 1842507518 scopus 로고    scopus 로고
    • Fibroblast network in rabbit sinoatrial node: structural and functional identification of homogeneous and heterogeneous cell coupling
    • Camelliti P., Green C.R., LeGrice I., Kohl P. Fibroblast network in rabbit sinoatrial node: structural and functional identification of homogeneous and heterogeneous cell coupling. Circ Res 2004, 94:828-835.
    • (2004) Circ Res , vol.94 , pp. 828-835
    • Camelliti, P.1    Green, C.R.2    LeGrice, I.3    Kohl, P.4
  • 130
    • 34547852342 scopus 로고    scopus 로고
    • Evidence of intercellular coupling between co-cultured adult rabbit ventricular myocytes and myofibroblasts
    • Chilton L., Giles W.R., Smith G.L. Evidence of intercellular coupling between co-cultured adult rabbit ventricular myocytes and myofibroblasts. J Physiol 2007, 583:225-236.
    • (2007) J Physiol , vol.583 , pp. 225-236
    • Chilton, L.1    Giles, W.R.2    Smith, G.L.3
  • 131
    • 0032518286 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase and c-Jun NH2-terminal kinase activation by mechanical stretch is integrin-dependent and matrix-specific in rat cardiac fibroblasts
    • MacKenna D.A., Dolfi F., Vuori K., Ruoslahti E. Extracellular signal-regulated kinase and c-Jun NH2-terminal kinase activation by mechanical stretch is integrin-dependent and matrix-specific in rat cardiac fibroblasts. J Clin Invest 1998, 101:301-310.
    • (1998) J Clin Invest , vol.101 , pp. 301-310
    • MacKenna, D.A.1    Dolfi, F.2    Vuori, K.3    Ruoslahti, E.4
  • 132
    • 0033002207 scopus 로고    scopus 로고
    • Angiotensin II and mechanical stretch induce production of tumor necrosis factor in cardiac fibroblasts
    • Yokoyama T., Sekiguchi K., Tanaka T., Tomaru K., Arai M., Suzuki T., et al. Angiotensin II and mechanical stretch induce production of tumor necrosis factor in cardiac fibroblasts. Am J Physiol 1999, 276:H1968-H1976.
    • (1999) Am J Physiol , vol.276 , pp. H1968-H1976
    • Yokoyama, T.1    Sekiguchi, K.2    Tanaka, T.3    Tomaru, K.4    Arai, M.5    Suzuki, T.6
  • 133
    • 0033921695 scopus 로고    scopus 로고
    • Cyclic stretch induces the release of growth promoting factors from cultured neonatal cardiomyocytes and cardiac fibroblasts
    • Ruwhof C., van Wamel A.E., Egas J.M., van der Laarse A. Cyclic stretch induces the release of growth promoting factors from cultured neonatal cardiomyocytes and cardiac fibroblasts. Mol Cell Biochem 2000, 208:89-98.
    • (2000) Mol Cell Biochem , vol.208 , pp. 89-98
    • Ruwhof, C.1    van Wamel, A.E.2    Egas, J.M.3    van der Laarse, A.4
  • 134
    • 0032871262 scopus 로고    scopus 로고
    • Differential responses of adult cardiac fibroblasts to in vitro biaxial strain patterns
    • Lee A.A., Delhaas T., McCulloch A.D., Villarreal F.J. Differential responses of adult cardiac fibroblasts to in vitro biaxial strain patterns. J Mol Cell Cardiol 1999, 31:1833-1843.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1833-1843
    • Lee, A.A.1    Delhaas, T.2    McCulloch, A.D.3    Villarreal, F.J.4
  • 135
    • 33744815900 scopus 로고    scopus 로고
    • Inverse regulation of preproendothelin-1 and endothelin-converting enzyme-1beta genes in cardiac cells by mechanical load
    • Pikkarainen S., Tokola H., Kerkela R., Ilves M., Makinen M., Orzechowski H.D., et al. Inverse regulation of preproendothelin-1 and endothelin-converting enzyme-1beta genes in cardiac cells by mechanical load. Am J Physiol Regul Integr Comp Physiol 2006, 290:R1639-R1645.
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.290 , pp. R1639-R1645
    • Pikkarainen, S.1    Tokola, H.2    Kerkela, R.3    Ilves, M.4    Makinen, M.5    Orzechowski, H.D.6
  • 136
    • 0032213728 scopus 로고    scopus 로고
    • Angiotensin II stimulates cardiac myocyte hypertrophy via paracrine release of TGF-beta 1 and endothelin-1 from fibroblasts
    • Gray M.O., Long C.S., Kalinyak J.E., Li H.T., Karliner J.S. Angiotensin II stimulates cardiac myocyte hypertrophy via paracrine release of TGF-beta 1 and endothelin-1 from fibroblasts. Cardiovasc Res 1998, 40:352-363.
    • (1998) Cardiovasc Res , vol.40 , pp. 352-363
    • Gray, M.O.1    Long, C.S.2    Kalinyak, J.E.3    Li, H.T.4    Karliner, J.S.5
  • 137
    • 33845647351 scopus 로고    scopus 로고
    • High- but not low-molecular weight FGF-2 causes cardiac hypertrophy in vivo; possible involvement of cardiotrophin-1
    • Jiang Z.S., Jeyaraman M., Wen G.B., Fandrich R.R., Dixon I.M., Cattini P.A., et al. High- but not low-molecular weight FGF-2 causes cardiac hypertrophy in vivo; possible involvement of cardiotrophin-1. J Mol Cell Cardiol 2007, 42:222-233.
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 222-233
    • Jiang, Z.S.1    Jeyaraman, M.2    Wen, G.B.3    Fandrich, R.R.4    Dixon, I.M.5    Cattini, P.A.6
  • 138
    • 34249882513 scopus 로고    scopus 로고
    • IL-33 and ST2 comprise a critical biomechanically induced and cardioprotective signaling system
    • Sanada S., Hakuno D., Higgins L.J., Schreiter E.R., McKenzie A.N., Lee R.T. IL-33 and ST2 comprise a critical biomechanically induced and cardioprotective signaling system. J Clin Invest 2007, 117:1538-1549.
    • (2007) J Clin Invest , vol.117 , pp. 1538-1549
    • Sanada, S.1    Hakuno, D.2    Higgins, L.J.3    Schreiter, E.R.4    McKenzie, A.N.5    Lee, R.T.6
  • 139
    • 33845391520 scopus 로고    scopus 로고
    • Cardiac myofibroblasts differentiated in 3D culture exhibit distinct changes in collagen I production, processing, and matrix deposition
    • Poobalarahi F., Baicu C.F., Bradshaw A.D. Cardiac myofibroblasts differentiated in 3D culture exhibit distinct changes in collagen I production, processing, and matrix deposition. Am J Physiol Heart Circ Physiol 2006, 291:H2924-H2932.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291 , pp. H2924-H2932
    • Poobalarahi, F.1    Baicu, C.F.2    Bradshaw, A.D.3
  • 140
  • 141
    • 36749014945 scopus 로고    scopus 로고
    • HSP90 and eNOS partially co-localize and change cellular localization in relation to different ECM components in 2D and 3D cultures of adult rat cardiomyocytes
    • Di Felice V., Cappello F., Montalbano A., Ardizzone N.M., De Luca A., Macaluso F., et al. HSP90 and eNOS partially co-localize and change cellular localization in relation to different ECM components in 2D and 3D cultures of adult rat cardiomyocytes. Biol Cell 2007, 99:689-699.
    • (2007) Biol Cell , vol.99 , pp. 689-699
    • di Felice, V.1    Cappello, F.2    Montalbano, A.3    Ardizzone, N.M.4    de Luca, A.5    Macaluso, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.