메뉴 건너뛰기




Volumn 70, Issue 3, 2006, Pages 422-433

Corrigendum to: Integrin signalling: The tug-of-war in heart hypertrophy [Cardiovascular Research 70 (2006) 422-433] (DOI:10.1016/j.cardiores.2005.12.015);Integrin signalling: The tug-of-war in heart hypertrophy

Author keywords

Cardiac hypertrophy; Integrins; Mechano transduction; Signal transduction

Indexed keywords

BETA INTEGRIN; FILAMIN; FOCAL ADHESION KINASE; INTEGRIN; ISOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE B; RAS PROTEIN; SCLEROPROTEIN; TALIN; VASODILATOR STIMULATED PHOSPHOPROTEIN; VINCULIN; ZYXIN;

EID: 33646529418     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2006.09.002     Document Type: Erratum
Times cited : (148)

References (84)
  • 1
    • 0141793051 scopus 로고    scopus 로고
    • Molecular interplay between mechanical and humoral signalling in cardiac hypertrophy
    • Tarone G., and Lembo G. Molecular interplay between mechanical and humoral signalling in cardiac hypertrophy. Trends Mol Med 9 (2003) 376-382
    • (2003) Trends Mol Med , vol.9 , pp. 376-382
    • Tarone, G.1    Lembo, G.2
  • 2
    • 0002537440 scopus 로고    scopus 로고
    • Cardiac hypertrophy: the good, the bad, and the ugly
    • Frey N., and Olson E.N. Cardiac hypertrophy: the good, the bad, and the ugly. Annu Rev Physiol 65 (2003) 45-79
    • (2003) Annu Rev Physiol , vol.65 , pp. 45-79
    • Frey, N.1    Olson, E.N.2
  • 3
    • 23644446462 scopus 로고    scopus 로고
    • Akt1 in the cardiovascular system: friend or foe?
    • O'Neill B.T., and Abel E.D. Akt1 in the cardiovascular system: friend or foe?. J Clin Invest 115 (2005) 2059-2064
    • (2005) J Clin Invest , vol.115 , pp. 2059-2064
    • O'Neill, B.T.1    Abel, E.D.2
  • 4
    • 27144536566 scopus 로고    scopus 로고
    • Class IA phosphoinositide 3-kinase regulates heart size and physiological cardiac hypertrophy
    • Luo J., McMullen J.R., Sobkiw C.L., Zhang L., Dorfman A.L., Sherwood M.C., et al. Class IA phosphoinositide 3-kinase regulates heart size and physiological cardiac hypertrophy. Mol Cell Biol 25 (2005) 9491-9502
    • (2005) Mol Cell Biol , vol.25 , pp. 9491-9502
    • Luo, J.1    McMullen, J.R.2    Sobkiw, C.L.3    Zhang, L.4    Dorfman, A.L.5    Sherwood, M.C.6
  • 5
    • 4344714889 scopus 로고    scopus 로고
    • PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects
    • Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A., Brancaccio M., et al. PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects. Cell 118 (2004) 375-387
    • (2004) Cell , vol.118 , pp. 375-387
    • Patrucco, E.1    Notte, A.2    Barberis, L.3    Selvetella, G.4    Maffei, A.5    Brancaccio, M.6
  • 6
    • 0030969371 scopus 로고    scopus 로고
    • The cellular and molecular response of cardiac myocytes to mechanical stress
    • Sadoshima J., and Izumo S. The cellular and molecular response of cardiac myocytes to mechanical stress. Annu Rev Physiol 59 (1997) 551-571
    • (1997) Annu Rev Physiol , vol.59 , pp. 551-571
    • Sadoshima, J.1    Izumo, S.2
  • 7
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • Pardo J.V., Siliciano J.D., and Craig S.W. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc Natl Acad Sci U S A 80 (1983) 1008-1012
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 8
    • 0036947050 scopus 로고    scopus 로고
    • The extracellular connections: the role of integrins in myocardial remodeling
    • Ross R.S. The extracellular connections: the role of integrins in myocardial remodeling. J Card Fail 8 (2002) S326-S331
    • (2002) J Card Fail , vol.8
    • Ross, R.S.1
  • 9
    • 0035827723 scopus 로고    scopus 로고
    • Integrins and the myocardium
    • Ross R.S., and Borg T.K. Integrins and the myocardium. Circ Res 88 (2001) 1112-1119
    • (2001) Circ Res , vol.88 , pp. 1112-1119
    • Ross, R.S.1    Borg, T.K.2
  • 10
    • 0034123657 scopus 로고    scopus 로고
    • Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways
    • Ruwhof C., and van der Laarse A. Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways. Cardiovasc Res 47 (2000) 23-37
    • (2000) Cardiovasc Res , vol.47 , pp. 23-37
    • Ruwhof, C.1    van der Laarse, A.2
  • 11
    • 0347381135 scopus 로고    scopus 로고
    • Ras, Akt, and mechanotransduction in the cardiac myocyte
    • Sugden P.H. Ras, Akt, and mechanotransduction in the cardiac myocyte. Circ Res 93 (2003) 1179-1192
    • (2003) Circ Res , vol.93 , pp. 1179-1192
    • Sugden, P.H.1
  • 12
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: a historical perspective on integrin signal transduction
    • Miranti C.K., and Brugge J.S. Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol 4 (2002) E83-E90
    • (2002) Nat Cell Biol , vol.4
    • Miranti, C.K.1    Brugge, J.S.2
  • 13
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti F.G., and Tarone G. Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu Rev Cell Dev Biol 19 (2003) 173-206
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 14
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: are changes in affinity and conformation underemphasized?
    • Carman C.V., and Springer T.A. Integrin avidity regulation: are changes in affinity and conformation underemphasized?. Curr Opin Cell Biol 15 (2003) 547-556
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 15
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 16
    • 0031856588 scopus 로고    scopus 로고
    • Differential onset of expression of alpha 7 and beta 1D integrins during mouse heart and skeletal muscle development
    • Brancaccio M., Cabodi S., Belkin A.M., Collo G., Koteliansky V.E., Tomatis D., et al. Differential onset of expression of alpha 7 and beta 1D integrins during mouse heart and skeletal muscle development. Cell Adhes Commun 5 (1998) 193-205
    • (1998) Cell Adhes Commun , vol.5 , pp. 193-205
    • Brancaccio, M.1    Cabodi, S.2    Belkin, A.M.3    Collo, G.4    Koteliansky, V.E.5    Tomatis, D.6
  • 18
    • 0031283019 scopus 로고    scopus 로고
    • Muscle beta1D integrin reinforces the cytoskeleton-matrix link: modulation of integrin adhesive function by alternative splicing
    • Belkin A.M., Retta S.F., Pletjushkina O.Y., Balzac F., Silengo L., Fassler R., et al. Muscle beta1D integrin reinforces the cytoskeleton-matrix link: modulation of integrin adhesive function by alternative splicing. J Cell Biol 139 (1997) 1583-1595
    • (1997) J Cell Biol , vol.139 , pp. 1583-1595
    • Belkin, A.M.1    Retta, S.F.2    Pletjushkina, O.Y.3    Balzac, F.4    Silengo, L.5    Fassler, R.6
  • 19
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - the cytoskeletal connection
    • Critchley D.R. Focal adhesions - the cytoskeletal connection. Curr Opin Cell Biol 12 (2000) 133-139
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 133-139
    • Critchley, D.R.1
  • 20
    • 0035969233 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu C., and Dedhar S. Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol 155 (2001) 505-510
    • (2001) J Cell Biol , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 21
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., and Williams B.D. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol 12 (2002) 787-797
    • (2002) Curr Biol , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 22
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas C.G., Gregory S.L., and Brown N.H. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J Cell Biol 152 (2001) 1007-1018
    • (2001) J Cell Biol , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 23
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai T., Li S., Docheva D., Grashoff C., Sakai K., Kostka G., et al. Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev 17 (2003) 926-940
    • (2003) Genes Dev , vol.17 , pp. 926-940
    • Sakai, T.1    Li, S.2    Docheva, D.3    Grashoff, C.4    Sakai, K.5    Kostka, G.6
  • 24
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C., and Fassler R. The integrin-actin connection, an eternal love affair. EMBO J 22 (2003) 2324-2333
    • (2003) EMBO J , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 25
    • 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 85 (2005) 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
  • 26
    • 0347993703 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch
    • Ling K., Doughman R.L., Iyer V.V., Firestone A.J., Bairstow S.F., Mosher D.F., et al. Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch. J Cell Biol 163 (2003) 1339-1349
    • (2003) J Cell Biol , vol.163 , pp. 1339-1349
    • Ling, K.1    Doughman, R.L.2    Iyer, V.V.3    Firestone, A.J.4    Bairstow, S.F.5    Mosher, D.F.6
  • 27
    • 0037038412 scopus 로고    scopus 로고
    • Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K., Doughman R.L., Firestone A.J., Bunce M.W., and Anderson R.A. Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420 (2002) 89-93
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 28
    • 18644371169 scopus 로고    scopus 로고
    • Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin
    • Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R., Voronov S., et al. Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin. Nature 420 (2002) 85-89
    • (2002) Nature , vol.420 , pp. 85-89
    • Di Paolo, G.1    Pellegrini, L.2    Letinic, K.3    Cestra, G.4    Zoncu, R.5    Voronov, S.6
  • 29
    • 0037040839 scopus 로고    scopus 로고
    • Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure
    • Shai S.Y., Harpf A.E., Babbitt C.J., Jordan M.C., Fishbein M.C., Chen J., et al. Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure. Circ Res 90 (2002) 458-464
    • (2002) Circ Res , vol.90 , pp. 458-464
    • Shai, S.Y.1    Harpf, A.E.2    Babbitt, C.J.3    Jordan, M.C.4    Fishbein, M.C.5    Chen, J.6
  • 30
    • 0035108354 scopus 로고    scopus 로고
    • Disruption of integrin function in the murine myocardium leads to perinatal lethality, fibrosis, and abnormal cardiac performance
    • Keller R.S., Shai S.Y., Babbitt C.J., Pham C.G., Solaro R.J., Valencik M.L., et al. Disruption of integrin function in the murine myocardium leads to perinatal lethality, fibrosis, and abnormal cardiac performance. Am J Pathol 158 (2001) 1079-1090
    • (2001) Am J Pathol , vol.158 , pp. 1079-1090
    • Keller, R.S.1    Shai, S.Y.2    Babbitt, C.J.3    Pham, C.G.4    Solaro, R.J.5    Valencik, M.L.6
  • 31
    • 0032513019 scopus 로고    scopus 로고
    • Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins
    • Pfaff M., Liu S., Erle D.J., and Ginsberg M.H. Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins. J Biol Chem 273 (1998) 6104-6109
    • (1998) J Biol Chem , vol.273 , pp. 6104-6109
    • Pfaff, M.1    Liu, S.2    Erle, D.J.3    Ginsberg, M.H.4
  • 32
    • 0032521681 scopus 로고    scopus 로고
    • Knockout and knocking of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development
    • Baudoin C., Goumans M.J., Mummery C., and Sonnenberg A. Knockout and knocking of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development. Genes Dev 12 (1998) 1202-1216
    • (1998) Genes Dev , vol.12 , pp. 1202-1216
    • Baudoin, C.1    Goumans, M.J.2    Mummery, C.3    Sonnenberg, A.4
  • 33
    • 0031058040 scopus 로고    scopus 로고
    • Association of tyrosine-phosphorylated c-Src with the cytoskeleton of hypertrophying myocardium
    • Kuppuswamy D., Kerr C., Narishige T., Kasi V.S., Menick D.R., and Cooper G.T. Association of tyrosine-phosphorylated c-Src with the cytoskeleton of hypertrophying myocardium. J Biol Chem 272 (1997) 4500-4508
    • (1997) J Biol Chem , vol.272 , pp. 4500-4508
    • Kuppuswamy, D.1    Kerr, C.2    Narishige, T.3    Kasi, V.S.4    Menick, D.R.5    Cooper, G.T.6
  • 34
    • 0037604598 scopus 로고    scopus 로고
    • Focal complex formation in adult cardiomyocytes is accompanied by the activation of beta3 integrin and c-Src
    • Willey C.D., Balasubramanian S., Rodriguez Rosas M.C., Ross R.S., and Kuppuswamy D. Focal complex formation in adult cardiomyocytes is accompanied by the activation of beta3 integrin and c-Src. J Mol Cell Cardiol 35 (2003) 671-683
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 671-683
    • Willey, C.D.1    Balasubramanian, S.2    Rodriguez Rosas, M.C.3    Ross, R.S.4    Kuppuswamy, D.5
  • 35
    • 0142211247 scopus 로고    scopus 로고
    • RGD-containing peptides activate S6K1 through beta3 integrin in adult cardiac muscle cells
    • Balasubramanian S., and Kuppuswamy D. RGD-containing peptides activate S6K1 through beta3 integrin in adult cardiac muscle cells. J Biol Chem 278 (2003) 42214-42224
    • (2003) J Biol Chem , vol.278 , pp. 42214-42224
    • Balasubramanian, S.1    Kuppuswamy, D.2
  • 36
    • 0037465435 scopus 로고    scopus 로고
    • Temporal response and localization of integrins beta1 and beta3 in the heart after myocardial infarction: regulation by cytokines
    • Sun M., Opavsky M.A., Stewart D.J., Rabinovitch M., Dawood F., Wen W.H., et al. Temporal response and localization of integrins beta1 and beta3 in the heart after myocardial infarction: regulation by cytokines. Circulation 107 (2003) 1046-1052
    • (2003) Circulation , vol.107 , pp. 1046-1052
    • Sun, M.1    Opavsky, M.A.2    Stewart, D.J.3    Rabinovitch, M.4    Dawood, F.5    Wen, W.H.6
  • 37
    • 0037200708 scopus 로고    scopus 로고
    • Spironolactone increases integrin beta3 gene expression in kidney and heart muscle cells
    • Chun T.Y., Bloem L., and Pratt J.H. Spironolactone increases integrin beta3 gene expression in kidney and heart muscle cells. Mol Cell Endocrinol 194 (2002) 175-182
    • (2002) Mol Cell Endocrinol , vol.194 , pp. 175-182
    • Chun, T.Y.1    Bloem, L.2    Pratt, J.H.3
  • 38
    • 0034634653 scopus 로고    scopus 로고
    • Integrin activation and focal complex formation in cardiac hypertrophy
    • Laser M., Willey C.D., Jiang W., Cooper G.t., Menick D.R., Zile M.R., et al. Integrin activation and focal complex formation in cardiac hypertrophy. J Biol Chem 275 (2000) 35624-35630
    • (2000) J Biol Chem , vol.275 , pp. 35624-35630
    • Laser, M.1    Willey, C.D.2    Jiang, W.3    Cooper, G.t.4    Menick, D.R.5    Zile, M.R.6
  • 39
    • 9644254078 scopus 로고    scopus 로고
    • Osteopontin: a protective mediator of cardiac fibrosis?
    • Graf K., and Stawowy P. Osteopontin: a protective mediator of cardiac fibrosis?. Hypertension 44 (2004) 809-810
    • (2004) Hypertension , vol.44 , pp. 809-810
    • Graf, K.1    Stawowy, P.2
  • 40
    • 18244385727 scopus 로고    scopus 로고
    • Distinct upregulation of extracellular matrix genes in transition from hypertrophy to hypertensive heart failure
    • Rysa J., Leskinen H., Ilves M., and Ruskoaho H. Distinct upregulation of extracellular matrix genes in transition from hypertrophy to hypertensive heart failure. Hypertension 45 (2005) 927-933
    • (2005) Hypertension , vol.45 , pp. 927-933
    • Rysa, J.1    Leskinen, H.2    Ilves, M.3    Ruskoaho, H.4
  • 41
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: in command and control of cell motility
    • Mitra S.K., Hanson D.A., and Schlaepfer D.D. Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6 (2005) 56-68
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 42
    • 0034730790 scopus 로고    scopus 로고
    • Early activation of the multicomponent signaling complex associated with focal adhesion kinase induced by pressure overload in the rat heart
    • Franchini K.G., Torsoni A.S., Soares P.H., and Saad M.J. Early activation of the multicomponent signaling complex associated with focal adhesion kinase induced by pressure overload in the rat heart. Circ Res 87 (2000) 558-565
    • (2000) Circ Res , vol.87 , pp. 558-565
    • Franchini, K.G.1    Torsoni, A.S.2    Soares, P.H.3    Saad, M.J.4
  • 43
    • 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 Jr. W., and Franchini K.G. Load-induced focal adhesion kinase activation in the myocardium: role of stretch and contractile activity. Am J Physiol Heart Circ Physiol 282 (2002) H556-H564
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • Domingos, P.P.1    Fonseca, P.M.2    Nadruz Jr., W.3    Franchini, K.G.4
  • 44
    • 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 Jr. W., Hanks S.K., and Franchini K.G. Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes. Circ Res 93 (2003) 140-147
    • (2003) Circ Res , vol.93 , pp. 140-147
    • Torsoni, A.S.1    Constancio, S.S.2    Nadruz Jr., W.3    Hanks, S.K.4    Franchini, K.G.5
  • 45
    • 0037188927 scopus 로고    scopus 로고
    • GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes
    • Heidkamp M.C., Bayer A.L., Kalina J.A., Eble D.M., and Samarel A.M. GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes. Circ Res 90 (2002) 1282-1289
    • (2002) Circ Res , vol.90 , pp. 1282-1289
    • Heidkamp, M.C.1    Bayer, A.L.2    Kalina, J.A.3    Eble, D.M.4    Samarel, A.M.5
  • 46
    • 0034533580 scopus 로고    scopus 로고
    • Striated muscle-specific beta(1D)-integrin and FAK are involved in cardiac myocyte hypertrophic response pathway
    • Pham C.G., Harpf A.E., Keller R.S., Vu H.T., Shai S.Y., Loftus J.C., et al. Striated muscle-specific beta(1D)-integrin and FAK are involved in cardiac myocyte hypertrophic response pathway. Am J Physiol Heart Circ Physiol 279 (2000) H2916-H2926
    • (2000) Am J Physiol Heart Circ Physiol , vol.279
    • Pham, C.G.1    Harpf, A.E.2    Keller, R.S.3    Vu, H.T.4    Shai, S.Y.5    Loftus, J.C.6
  • 47
    • 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., and Parsons J.T. A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes. J Biol Chem 275 (2000) 19250-19257
    • (2000) J Biol Chem , vol.275 , pp. 19250-19257
    • Taylor, J.M.1    Rovin, J.D.2    Parsons, J.T.3
  • 48
    • 0034644612 scopus 로고    scopus 로고
    • Focal adhesion kinase is involved in angiotensin II-mediated protein synthesis in cultured vascular smooth muscle cells
    • Govindarajan G., Eble D.M., Lucchesi P.A., and Samarel A.M. Focal adhesion kinase is involved in angiotensin II-mediated protein synthesis in cultured vascular smooth muscle cells. Circ Res 87 (2000) 710-716
    • (2000) Circ Res , vol.87 , pp. 710-716
    • Govindarajan, G.1    Eble, D.M.2    Lucchesi, P.A.3    Samarel, A.M.4
  • 50
    • 0035158546 scopus 로고    scopus 로고
    • Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy
    • Kovacic-Milivojevic B., Roediger F., Almeida E.A., Damsky C.H., Gardner D.G., and Ilic D. Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy. Mol Biol Cell 12 (2001) 2290-2307
    • (2001) Mol Biol Cell , vol.12 , pp. 2290-2307
    • Kovacic-Milivojevic, B.1    Roediger, F.2    Almeida, E.A.3    Damsky, C.H.4    Gardner, D.G.5    Ilic, D.6
  • 51
    • 0032525330 scopus 로고    scopus 로고
    • Beta1 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. Beta1 integrins participate in the hypertrophic response of rat ventricular myocytes. Circ Res 82 (1998) 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
  • 53
    • 0037160062 scopus 로고    scopus 로고
    • Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling
    • Melendez J., Welch S., Schaefer E., Moravec C.S., Avraham S., Avraham H., et al. Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling. J Biol Chem 277 (2002) 45203-45210
    • (2002) J Biol Chem , vol.277 , pp. 45203-45210
    • Melendez, J.1    Welch, S.2    Schaefer, E.3    Moravec, C.S.4    Avraham, S.5    Avraham, H.6
  • 55
    • 0032879692 scopus 로고    scopus 로고
    • Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain
    • Brancaccio M., Guazzone S., Menini N., Sibona E., Hirsch E., De Andrea M., et al. Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain. J Biol Chem 274 (1999) 29282-29288
    • (1999) J Biol Chem , vol.274 , pp. 29282-29288
    • Brancaccio, M.1    Guazzone, S.2    Menini, N.3    Sibona, E.4    Hirsch, E.5    De Andrea, M.6
  • 57
    • 0037236642 scopus 로고    scopus 로고
    • Melusin, a muscle-specific integrin beta1-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 beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload. Nat Med 9 (2003) 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
  • 58
    • 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 96 (2005) 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
  • 59
    • 14644414790 scopus 로고    scopus 로고
    • Protein kinase cascades in the regulation of cardiac hypertrophy
    • Dorn II G.W., and Force T. Protein kinase cascades in the regulation of cardiac hypertrophy. J Clin Invest 115 (2005) 527-537
    • (2005) J Clin Invest , vol.115 , pp. 527-537
    • Dorn II, G.W.1    Force, T.2
  • 61
    • 0034213075 scopus 로고    scopus 로고
    • The conserved phosphoinositide 3-kinase pathway determines heart size in mice
    • Shioi T., Kang P.M., Douglas P.S., Hampe J., Yballe C.M., Lawitts J., et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J 19 (2000) 2537-2548
    • (2000) EMBO J , vol.19 , pp. 2537-2548
    • Shioi, T.1    Kang, P.M.2    Douglas, P.S.3    Hampe, J.4    Yballe, C.M.5    Lawitts, J.6
  • 62
    • 0037151104 scopus 로고    scopus 로고
    • Phenotypic spectrum caused by transgenic overexpression of activated Akt in the heart
    • Matsui T., Li L., Wu J.C., Cook S.A., Nagoshi T., Picard M.H., et al. Phenotypic spectrum caused by transgenic overexpression of activated Akt in the heart. J Biol Chem 277 (2002) 22896-22901
    • (2002) J Biol Chem , vol.277 , pp. 22896-22901
    • Matsui, T.1    Li, L.2    Wu, J.C.3    Cook, S.A.4    Nagoshi, T.5    Picard, M.H.6
  • 63
    • 7444264785 scopus 로고    scopus 로고
    • Molecular determinants of the physiological adaptation to stress in the cardiomyocyte: a focus on AKT
    • Ceci M., Ross Jr. J., and Condorelli G. Molecular determinants of the physiological adaptation to stress in the cardiomyocyte: a focus on AKT. J Mol Cell Cardiol 37 (2004) 905-912
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 905-912
    • Ceci, M.1    Ross Jr., J.2    Condorelli, G.3
  • 64
    • 0036100436 scopus 로고    scopus 로고
    • Modifier genes for hypertrophic cardiomyopathy
    • Marian A.J. Modifier genes for hypertrophic cardiomyopathy. Curr Opin Cardiol 17 (2002) 242-252
    • (2002) Curr Opin Cardiol , vol.17 , pp. 242-252
    • Marian, A.J.1
  • 65
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., and Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125 (1998) 327-337
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 66
  • 67
    • 0027529373 scopus 로고
    • Organization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter
    • Moiseyeva E.P., Weller P.A., Zhidkova N.I., Corben E.B., Patel B., Jasinska I., et al. Organization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter. J Biol Chem 268 (1993) 4318-4325
    • (1993) J Biol Chem , vol.268 , pp. 4318-4325
    • Moiseyeva, E.P.1    Weller, P.A.2    Zhidkova, N.I.3    Corben, E.B.4    Patel, B.5    Jasinska, I.6
  • 69
    • 0031034388 scopus 로고    scopus 로고
    • Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin
    • Maeda M., Holder E., Lowes B., Valent S., and Bies R.D. Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin. Circulation 95 (1997) 17-20
    • (1997) Circulation , vol.95 , pp. 17-20
    • Maeda, M.1    Holder, E.2    Lowes, B.3    Valent, S.4    Bies, R.D.5
  • 70
    • 32044458438 scopus 로고    scopus 로고
    • Vasile VC, Will ML, Ommen SR, Edwards WD, Olson TM, Ackerman MJ. Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy. Mol Genet Metab in press (Available online 19 October 2005, doi:10.1016/j.ymgme.2005.08.06).
  • 71
    • 0031281898 scopus 로고    scopus 로고
    • Zyxin: zinc fingers at sites of cell adhesion
    • Beckerle M.C. Zyxin: zinc fingers at sites of cell adhesion. Bioessays 19 (1997) 949-957
    • (1997) Bioessays , vol.19 , pp. 949-957
    • Beckerle, M.C.1
  • 75
    • 0033529302 scopus 로고    scopus 로고
    • Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice
    • Hauser W., Knobeloch K.P., Eigenthaler M., Gambaryan S., Krenn V., Geiger J., et al. Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice. Proc Natl Acad Sci U S A 96 (1999) 8120-8125
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8120-8125
    • Hauser, W.1    Knobeloch, K.P.2    Eigenthaler, M.3    Gambaryan, S.4    Krenn, V.5    Geiger, J.6
  • 77
    • 0036153139 scopus 로고    scopus 로고
    • Gene transfer of cGMP-dependent protein kinase I enhances the antihypertrophic effects of nitric oxide in cardiomyocytes
    • Wollert K.C., Fiedler B., Gambaryan S., Smolenski A., Heineke J., Butt E., et al. Gene transfer of cGMP-dependent protein kinase I enhances the antihypertrophic effects of nitric oxide in cardiomyocytes. Hypertension 39 (2002) 87-92
    • (2002) Hypertension , vol.39 , pp. 87-92
    • Wollert, K.C.1    Fiedler, B.2    Gambaryan, S.3    Smolenski, A.4    Heineke, J.5    Butt, E.6
  • 78
    • 14944370105 scopus 로고    scopus 로고
    • Migfilin and its binding partners: from cell biology to human diseases
    • Wu C. Migfilin and its binding partners: from cell biology to human diseases. J Cell Sci 118 (2005) 659-664
    • (2005) J Cell Sci , vol.118 , pp. 659-664
    • Wu, C.1
  • 79
    • 0842288224 scopus 로고    scopus 로고
    • A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5
    • Akazawa H., Kudoh S., Mochizuki N., Takekoshi N., Takano H., Nagai T., et al. A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5. J Cell Biol 164 (2004) 395-405
    • (2004) J Cell Biol , vol.164 , pp. 395-405
    • Akazawa, H.1    Kudoh, S.2    Mochizuki, N.3    Takekoshi, N.4    Takano, H.5    Nagai, T.6
  • 80
    • 0033912859 scopus 로고    scopus 로고
    • Loss of function and inhibitory effects of human CSX/NKX2.5 homeoprotein mutations associated with congenital heart disease
    • Kasahara H., Lee B., Schott J.J., Benson D.W., Seidman J.G., Seidman C.E., et al. Loss of function and inhibitory effects of human CSX/NKX2.5 homeoprotein mutations associated with congenital heart disease. J Clin Invest 106 (2000) 299-308
    • (2000) J Clin Invest , vol.106 , pp. 299-308
    • Kasahara, H.1    Lee, B.2    Schott, J.J.3    Benson, D.W.4    Seidman, J.G.5    Seidman, C.E.6
  • 81
    • 0031861927 scopus 로고    scopus 로고
    • Upregulation of the cardiac homeobox gene Nkx2-5 (CSX) in feline right ventricular pressure overload
    • Thompson J.T., Rackley M.S., and O'Brien T.X. Upregulation of the cardiac homeobox gene Nkx2-5 (CSX) in feline right ventricular pressure overload. Am J Physiol 274 (1998) H1569-H1573
    • (1998) Am J Physiol , vol.274
    • Thompson, J.T.1    Rackley, M.S.2    O'Brien, T.X.3
  • 82
    • 0032809986 scopus 로고    scopus 로고
    • Expression of immediate early genes, GATA-4, and Nkx-2.5 in adrenergic-induced cardiac hypertrophy and during regression in adult mice
    • Saadane N., Alpert L., and Chalifour L.E. Expression of immediate early genes, GATA-4, and Nkx-2.5 in adrenergic-induced cardiac hypertrophy and during regression in adult mice. Br J Pharmacol 127 (1999) 1165-1176
    • (1999) Br J Pharmacol , vol.127 , pp. 1165-1176
    • Saadane, N.1    Alpert, L.2    Chalifour, L.E.3
  • 83
    • 0035853070 scopus 로고    scopus 로고
    • Regulation of cardiomyocyte mechanotransduction by the cardiac cycle
    • Yamamoto K., Dang Q.N., Maeda Y., Huang H., Kelly R.A., and Lee R.T. Regulation of cardiomyocyte mechanotransduction by the cardiac cycle. Circulation 103 (2001) 1459-1464
    • (2001) Circulation , vol.103 , pp. 1459-1464
    • Yamamoto, K.1    Dang, Q.N.2    Maeda, Y.3    Huang, H.4    Kelly, R.A.5    Lee, R.T.6
  • 84
    • 4544384693 scopus 로고    scopus 로고
    • Activation of distinct signal transduction pathways in hypertrophied hearts by pressure and volume overload
    • Miyamoto T., Takeishi Y., Takahashi H., Shishido T., Arimoto T., Tomoike H., et al. Activation of distinct signal transduction pathways in hypertrophied hearts by pressure and volume overload. Basic Res Cardiol 99 (2004) 328-337
    • (2004) Basic Res Cardiol , vol.99 , pp. 328-337
    • Miyamoto, T.1    Takeishi, Y.2    Takahashi, H.3    Shishido, T.4    Arimoto, T.5    Tomoike, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.