메뉴 건너뛰기




Volumn 5 JUL, Issue , 2014, Pages

Tenascin-C and mechanotransduction in the development and diseases of cardiovascular system

Author keywords

Aortic dissection; Coronary artery; Extracellular matrix; Heart; Matricellular protein; Mechanotrasduction; Tenascin C

Indexed keywords

TENASCIN;

EID: 84904338703     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00283     Document Type: Article
Times cited : (59)

References (136)
  • 1
    • 67650875881 scopus 로고    scopus 로고
    • Vascular extracellular matrix and arterial mechanics
    • doi: 10.1152/physrev.00041.2008
    • Wagenseil JE, Mecham RP. Vascular extracellular matrix and arterial mechanics. Physiol Rev. 2009;89:957-89. doi: 10.1152/physrev.00041.2008.
    • (2009) Physiol Rev , vol.89 , pp. 957-989
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 2
    • 0018427165 scopus 로고
    • The collagen network of the heart
    • Caulfield JB, Borg TK. The collagen network of the heart. Lab Invest. 1979;40:364-72.
    • (1979) Lab Invest , vol.40 , pp. 364-372
    • Caulfield, J.B.1    Borg, T.K.2
  • 3
    • 0019830784 scopus 로고
    • The collagen matrix of the heart
    • Borg TK, Caulfield JB. The collagen matrix of the heart. Fed Proc. 1981;40:2037-41.
    • (1981) Fed Proc , vol.40 , pp. 2037-2041
    • Borg, T.K.1    Caulfield, J.B.2
  • 4
    • 79951785577 scopus 로고    scopus 로고
    • Heart valve structure and function in development and disease
    • doi: 10.1146/annurev-physiol-012110-142145
    • Hinton RB, Yutzey KE. Heart valve structure and function in development and disease. Annu Rev Physiol. 2011;73:29-46. doi: 10.1146/annurev-physiol-012110-142145.
    • (2011) Annu Rev Physiol , vol.73 , pp. 29-46
    • Hinton, R.B.1    Yutzey, K.E.2
  • 5
    • 0037112402 scopus 로고    scopus 로고
    • Dance band on the Titanic: biomechanical signaling in cardiac hypertrophy
    • Sussman MA, McCulloch A, Borg TK. Dance band on the Titanic: biomechanical signaling in cardiac hypertrophy. Circ Res. 2002;91:888-98.
    • (2002) Circ Res , vol.91 , pp. 888-898
    • Sussman, M.A.1    McCulloch, A.2    Borg, T.K.3
  • 6
    • 77649270920 scopus 로고    scopus 로고
    • The extracellular matrix: at the center of it all
    • doi: 10.1016/j.yjmcc.2009.08.024
    • Bowers SL, Banerjee I, Baudino TA. The extracellular matrix: at the center of it all. J Mol Cell Cardiol. 2010;48:474-82. doi: 10.1016/j.yjmcc.2009.08.024.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 474-482
    • Bowers, S.L.1    Banerjee, I.2    Baudino, T.A.3
  • 7
    • 79958807720 scopus 로고    scopus 로고
    • Dynamic interactions between the cellular components of the heart and the extracellular matrix
    • doi: 10.1007/s00424-011-0940-7
    • Borg TK, Baudino TA. Dynamic interactions between the cellular components of the heart and the extracellular matrix. Pflugers Arch. 2011;462:69-74. doi: 10.1007/s00424-011-0940-7.
    • (2011) Pflugers Arch , vol.462 , pp. 69-74
    • Borg, T.K.1    Baudino, T.A.2
  • 8
    • 72449177328 scopus 로고    scopus 로고
    • Matricellular proteins: an overview
    • doi: 10.1007/s12079-009-0069-z
    • Bornstein P. Matricellular proteins: an overview. J Cell Commun Signal. 2009;3:163-5. doi: 10.1007/s12079-009-0069-z.
    • (2009) J Cell Commun Signal , vol.3 , pp. 163-165
    • Bornstein, P.1
  • 9
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
    • Sage EH, Bornstein P. Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J Biol Chem. 1991;266:14831-4.
    • (1991) J Biol Chem , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 10
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: extracellular modulators of cell function
    • Bornstein P, Sage EH. Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol. 2002;14:608-16.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 11
    • 65949102766 scopus 로고    scopus 로고
    • Periostin as a heterofunctional regulator of cardiac development and disease
    • doi: 10.2174/138920208786847917
    • Conway SJ, Molkentin JD. Periostin as a heterofunctional regulator of cardiac development and disease. Curr Genomics. 2008;9:548-55. doi: 10.2174/138920208786847917.
    • (2008) Curr Genomics , vol.9 , pp. 548-555
    • Conway, S.J.1    Molkentin, J.D.2
  • 12
    • 39949083939 scopus 로고    scopus 로고
    • BMP-2 induces cell migration and periostin expression during atrioventricular valvulogenesis
    • doi: 10.1016/j.ydbio.2007.12.028
    • Inai K, Norris RA, Hoffman S, Markwald RR, Sugi Y. BMP-2 induces cell migration and periostin expression during atrioventricular valvulogenesis. Dev Biol. 2008;315:383-96. doi: 10.1016/j.ydbio.2007.12.028.
    • (2008) Dev Biol , vol.315 , pp. 383-396
    • Inai, K.1    Norris, R.A.2    Hoffman, S.3    Markwald, R.R.4    Sugi, Y.5
  • 15
    • 84896937123 scopus 로고    scopus 로고
    • Periostin Induces Intracellular Cross-talk between Kinases and Hyaluronan in Atrioventricular Valvulogenesis
    • doi: 10.1074/jbc.M113.539882
    • Ghatak S, Misra S, Norris RA, Moreno-Rodriguez RA, Hoffman S, Levine RA, Hascall VC, Markwald RR. Periostin Induces Intracellular Cross-talk between Kinases and Hyaluronan in Atrioventricular Valvulogenesis. J Biol Chem. 2014;289:8545-61. doi: 10.1074/jbc.M113.539882.
    • (2014) J Biol Chem , vol.289 , pp. 8545-8561
    • Ghatak, S.1    Misra, S.2    Norris, R.A.3    Moreno-Rodriguez, R.A.4    Hoffman, S.5    Levine, R.A.6    Hascall, V.C.7    Markwald, R.R.8
  • 16
    • 33749142748 scopus 로고    scopus 로고
    • Phylogenetic analysis of the tenascin gene family: evidence of origin early in the chordate lineage
    • doi: 10.1186/1471-2148-6-60
    • Tucker RP, Drabikowski K, Hess JF, Ferralli J, Chiquet-Ehrismann R, Adams JC. Phylogenetic analysis of the tenascin gene family: evidence of origin early in the chordate lineage. BMC Evol Biol. 2006;6:60. doi: 10.1186/1471-2148-6-60.
    • (2006) BMC Evol Biol , vol.6 , pp. 60
    • Tucker, R.P.1    Drabikowski, K.2    Hess, J.F.3    Ferralli, J.4    Chiquet-Ehrismann, R.5    Adams, J.C.6
  • 17
    • 67349268473 scopus 로고    scopus 로고
    • The regulation of tenascin expression by tissue microenvironments
    • doi: 10.1016/j.bbamcr.2008.12.012
    • Tucker RP, Chiquet-Ehrismann R. The regulation of tenascin expression by tissue microenvironments. Biochim Biophys Acta. 2009;1793:888-92. doi: 10.1016/j.bbamcr.2008.12.012.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 888-892
    • Tucker, R.P.1    Chiquet-Ehrismann, R.2
  • 18
    • 0022972814 scopus 로고
    • Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis
    • Chiquet-Ehrismann R, Mackie EJ, Pearson CA, Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell. 1986;47:131-9.
    • (1986) Cell , vol.47 , pp. 131-139
    • Chiquet-Ehrismann, R.1    Mackie, E.J.2    Pearson, C.A.3    Sakakura, T.4
  • 19
    • 84855165117 scopus 로고    scopus 로고
    • Tenascins and the importance of adhesion modulation
    • doi: 10.1101/cshperspect.a004960
    • Chiquet-Ehrismann R, Tucker RP. Tenascins and the importance of adhesion modulation. Cold Spring Harb Perspect Biol. 2011;3. doi: 10.1101/cshperspect.a004960.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Chiquet-Ehrismann, R.1    Tucker, R.P.2
  • 20
    • 0025744729 scopus 로고
    • Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11
    • Rathjen FG, Wolff JM, Chiquet-Ehrismann R. Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11. Development. 1991;113:151-64.
    • (1991) Development , vol.113 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 21
    • 0026606265 scopus 로고
    • Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin
    • Matsumoto K, Arai M, Ishihara N, Ando A, Inoko H, Ikemura T. Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin. Genomics. 1992;12:485-91.
    • (1992) Genomics , vol.12 , pp. 485-491
    • Matsumoto, K.1    Arai, M.2    Ishihara, N.3    Ando, A.4    Inoko, H.5    Ikemura, T.6
  • 22
    • 0027231385 scopus 로고
    • Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow J, Tee MK, Gitelman SE, Mellon SH, Miller WL. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J Cell Biol. 1993;122:265-78.
    • (1993) J Cell Biol , vol.122 , pp. 265-278
    • Bristow, J.1    Tee, M.K.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 23
    • 28444462887 scopus 로고    scopus 로고
    • Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome
    • doi: 10.1002/ajmg.c.30071
    • Bristow J, Carey W, Egging D, Schalkwijk J. Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome. Am J Med Genet C Semin Med Genet. 2005;139C:24-30. doi: 10.1002/ajmg.c.30071.
    • (2005) Am J Med Genet C Semin Med Genet , vol.139 C , pp. 24-30
    • Bristow, J.1    Carey, W.2    Egging, D.3    Schalkwijk, J.4
  • 24
    • 0029822205 scopus 로고    scopus 로고
    • Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue
    • Hagios C, Koch M, Spring J, Chiquet M, Chiquet-Ehrismann R. Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue. J Cell Biol. 1996;134:1499-512.
    • (1996) J Cell Biol , vol.134 , pp. 1499-1512
    • Hagios, C.1    Koch, M.2    Spring, J.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 25
  • 26
    • 0038383036 scopus 로고    scopus 로고
    • Tenascin-N: characterization of a novel member of the tenascin family that mediates neurite repulsion from hippocampal explants
    • Neidhardt J, Fehr S, Kutsche M, Lohler J, Schachner M. Tenascin-N: characterization of a novel member of the tenascin family that mediates neurite repulsion from hippocampal explants. Mol Cell Neurosci. 2003;23:193-209.
    • (2003) Mol Cell Neurosci , vol.23 , pp. 193-209
    • Neidhardt, J.1    Fehr, S.2    Kutsche, M.3    Lohler, J.4    Schachner, M.5
  • 28
    • 84855181728 scopus 로고    scopus 로고
    • How do tenascins influence the birth and life of a malignant cell?
    • doi 10.1111/j.1582-4934.2011.01360.x
    • Brellier F, Chiquet-Ehrismann R. How do tenascins influence the birth and life of a malignant cell? J Cell Mol Med. 2012;16:32-40. doi 10.1111/j.1582-4934.2011.01360.x.
    • (2012) J Cell Mol Med , vol.16 , pp. 32-40
    • Brellier, F.1    Chiquet-Ehrismann, R.2
  • 30
    • 80052942375 scopus 로고    scopus 로고
    • Advances in tenascin-C biology
    • doi: 10.1007/s00018-011-0783-6
    • Midwood KS, Hussenet T, Langlois B, Orend G. Advances in tenascin-C biology. Cell Mol Life Sci. 2011;68:3175-99. doi: 10.1007/s00018-011-0783-6.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3175-3199
    • Midwood, K.S.1    Hussenet, T.2    Langlois, B.3    Orend, G.4
  • 31
    • 72449127497 scopus 로고    scopus 로고
    • The role of tenascin-C in tissue injury and tumorigenesis
    • doi: 10.1007/s12079-009-0075-1
    • Midwood KS, Orend G. The role of tenascin-C in tissue injury and tumorigenesis. J Cell Commun Signal. 2009;3:287-310. doi: 10.1007/s12079-009-0075-1.
    • (2009) J Cell Commun Signal , vol.3 , pp. 287-310
    • Midwood, K.S.1    Orend, G.2
  • 32
    • 33749452709 scopus 로고    scopus 로고
    • Tenascin-C induced signaling in cancer
    • doi: 10.1016/j.canlet.2006.02.017
    • Orend G, Chiquet-Ehrismann R. Tenascin-C induced signaling in cancer. Cancer Lett. 2006;244:143-63. doi: 10.1016/j.canlet.2006.02.017.
    • (2006) Cancer Lett , vol.244 , pp. 143-163
    • Orend, G.1    Chiquet-Ehrismann, R.2
  • 35
    • 84869129525 scopus 로고    scopus 로고
    • Tenascin-C in cardiovascular tissue remodeling
    • Imanaka-Yoshida K. Tenascin-C in cardiovascular tissue remodeling. Circ J. 2012;76:2513-20.
    • (2012) Circ J , vol.76 , pp. 2513-2520
    • Imanaka-Yoshida, K.1
  • 36
    • 1642403894 scopus 로고    scopus 로고
    • Tenascin-C upregulation by transforming growth factor-beta in human dermal fibroblasts involves Smad3, Sp1, and Ets1
    • doi: 10.1038/sj.onc.1207064
    • Jinnin M, Ihn H, Asano Y, Yamane K, Trojanowska M, Tamaki K. Tenascin-C upregulation by transforming growth factor-beta in human dermal fibroblasts involves Smad3, Sp1, and Ets1. Oncogene. 2004;23:1656-67. doi: 10.1038/sj.onc.1207064.
    • (2004) Oncogene , vol.23 , pp. 1656-1667
    • Jinnin, M.1    Ihn, H.2    Asano, Y.3    Yamane, K.4    Trojanowska, M.5    Tamaki, K.6
  • 37
    • 77951887486 scopus 로고    scopus 로고
    • Transcriptional regulation of the endogenous danger signal tenascin-C: a novel autocrine loop in inflammation
    • doi: 10.4049/jimmunol.0903359
    • Goh FG, Piccinini AM, Krausgruber T, Udalova IA, Midwood KS. Transcriptional regulation of the endogenous danger signal tenascin-C: a novel autocrine loop in inflammation. J Immunol. 2010;184:2655-62. doi: 10.4049/jimmunol.0903359.
    • (2010) J Immunol , vol.184 , pp. 2655-2662
    • Goh, F.G.1    Piccinini, A.M.2    Krausgruber, T.3    Udalova, I.A.4    Midwood, K.S.5
  • 40
    • 58349101326 scopus 로고    scopus 로고
    • Genome-wide promoter analysis of the SOX4 transcriptional network in prostate cancer cells
    • doi: 10.1158/0008-5472.can-08-3415
    • Scharer CD, McCabe CD, Ali-Seyed M, Berger MF, Bulyk ML, Moreno CS. Genome-wide promoter analysis of the SOX4 transcriptional network in prostate cancer cells. Cancer Res. 2009;69:709-17. doi: 10.1158/0008-5472.can-08-3415.
    • (2009) Cancer Res , vol.69 , pp. 709-717
    • Scharer, C.D.1    McCabe, C.D.2    Ali-Seyed, M.3    Berger, M.F.4    Bulyk, M.L.5    Moreno, C.S.6
  • 41
    • 31944443343 scopus 로고    scopus 로고
    • Platelet derived growth factor induced tenascin-C transcription is phosphoinositide 3-kinase/Akt-dependent and mediated by Ets family transcription factors
    • doi: 10.1002/jcp.20527
    • Jinnin M, Ihn H, Asano Y, Yamane K, Trojanowska M, Tamaki K. Platelet derived growth factor induced tenascin-C transcription is phosphoinositide 3-kinase/Akt-dependent and mediated by Ets family transcription factors. J Cell Physiol. 2006;206:718-27. doi: 10.1002/jcp.20527.
    • (2006) J Cell Physiol , vol.206 , pp. 718-727
    • Jinnin, M.1    Ihn, H.2    Asano, Y.3    Yamane, K.4    Trojanowska, M.5    Tamaki, K.6
  • 42
    • 63349093919 scopus 로고    scopus 로고
    • The Xenopus MEF2 gene family: evidence of a role for XMEF2C in larval tendon development
    • doi: 10.1016/j.ydbio.2009.01.039
    • della Gaspera B, Armand AS, Sequeira I, Lecolle S, Gallien CL, Charbonnier F, Chanoine C. The Xenopus MEF2 gene family: evidence of a role for XMEF2C in larval tendon development. Dev Biol. 2009;328:392-402. doi: 10.1016/j.ydbio.2009.01.039.
    • (2009) Dev Biol , vol.328 , pp. 392-402
    • della Gaspera, B.1    Armand, A.S.2    Sequeira, I.3    Lecolle, S.4    Gallien, C.L.5    Charbonnier, F.6    Chanoine, C.7
  • 43
    • 4444314614 scopus 로고    scopus 로고
    • Induction of tenascin-C by cyclic tensile strain versus growth factors: distinct contributions by Rho/ROCK and MAPK signaling pathways
    • doi: 10.1016/j.bbamcr.2004.08.001
    • Chiquet M, Sarasa-Renedo A, Tunc-Civelek V. Induction of tenascin-C by cyclic tensile strain versus growth factors: distinct contributions by Rho/ROCK and MAPK signaling pathways. Biochim Biophys Acta. 2004;1693:193-204. doi: 10.1016/j.bbamcr.2004.08.001.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 193-204
    • Chiquet, M.1    Sarasa-Renedo, A.2    Tunc-Civelek, V.3
  • 44
    • 79960675151 scopus 로고    scopus 로고
    • Tenascin-C enhances crosstalk signaling of integrin alphavbeta3/PDGFR-beta complex by SRC recruitment promoting PDGF-induced proliferation and migration in smooth muscle cells
    • doi: 10.1002/jcp.22614
    • Ishigaki T, Imanaka-Yoshida K, Shimojo N, Matsushima S, Taki W, Yoshida T. Tenascin-C enhances crosstalk signaling of integrin alphavbeta3/PDGFR-beta complex by SRC recruitment promoting PDGF-induced proliferation and migration in smooth muscle cells. J Cell Physiol. 2011;226:2617-24. doi: 10.1002/jcp.22614.
    • (2011) J Cell Physiol , vol.226 , pp. 2617-2624
    • Ishigaki, T.1    Imanaka-Yoshida, K.2    Shimojo, N.3    Matsushima, S.4    Taki, W.5    Yoshida, T.6
  • 45
    • 0037348805 scopus 로고    scopus 로고
    • Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle
    • Jarvinen TA, Jozsa L, Kannus P, Jarvinen TL, Hurme T, Kvist M, Pelto-Huikko M, Kalimo H, Jarvinen M. Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle. J Cell Sci. 2003;116:857-66.
    • (2003) J Cell Sci , vol.116 , pp. 857-866
    • Jarvinen, T.A.1    Jozsa, L.2    Kannus, P.3    Jarvinen, T.L.4    Hurme, T.5    Kvist, M.6    Pelto-Huikko, M.7    Kalimo, H.8    Jarvinen, M.9
  • 48
    • 0026702532 scopus 로고
    • Expression of tenascin by vascular smooth muscle cells. Alterations in hypertensive rats and stimulation by angiotensin II
    • Mackie EJ, Scott-Burden T, Hahn AW, Kern F, Bernhardt J, Regenass S, Weller A, Buhler FR. Expression of tenascin by vascular smooth muscle cells. Alterations in hypertensive rats and stimulation by angiotensin II. Am J Pathol. 1992;141:377-88.
    • (1992) Am J Pathol , vol.141 , pp. 377-388
    • Mackie, E.J.1    Scott-Burden, T.2    Hahn, A.W.3    Kern, F.4    Bernhardt, J.5    Regenass, S.6    Weller, A.7    Buhler, F.R.8
  • 49
    • 0033740717 scopus 로고    scopus 로고
    • Rapid and reciprocal regulation of tenascin-C and tenascin-Y expression by loading of skeletal muscle
    • Fluck M, Tunc-Civelek V, Chiquet M. Rapid and reciprocal regulation of tenascin-C and tenascin-Y expression by loading of skeletal muscle. J Cell Sci. 2000;113:3583-91.
    • (2000) J Cell Sci , vol.113 , pp. 3583-3591
    • Fluck, M.1    Tunc-Civelek, V.2    Chiquet, M.3
  • 50
    • 79957901408 scopus 로고    scopus 로고
    • Sequenced response of extracellular matrix deadhesion and fibrotic regulators after muscle damage is involved in protection against future injury in human skeletal muscle
    • doi: 10.1096/fj.10-176487
    • Mackey AL, Brandstetter S, Schjerling P, Bojsen-Moller J, Qvortrup K, Pedersen MM, Doessing S, Kjaer M, Magnusson SP, Langberg H. Sequenced response of extracellular matrix deadhesion and fibrotic regulators after muscle damage is involved in protection against future injury in human skeletal muscle. FASEB J. 2011;25:1943-59. doi: 10.1096/fj.10-176487.
    • (2011) FASEB J , vol.25 , pp. 1943-1959
    • Mackey, A.L.1    Brandstetter, S.2    Schjerling, P.3    Bojsen-Moller, J.4    Qvortrup, K.5    Pedersen, M.M.6    Doessing, S.7    Kjaer, M.8    Magnusson, S.P.9    Langberg, H.10
  • 51
    • 0034190288 scopus 로고    scopus 로고
    • Mechanical modulation of tenascin-C and collagen-XII expression during avian synovial joint formation
    • doi: 10.1002/jor.1100180312
    • Mikic B, Wong M, Chiquet M, Hunziker EB. Mechanical modulation of tenascin-C and collagen-XII expression during avian synovial joint formation. J Orthop Res. 2000;18:406-15. doi: 10.1002/jor.1100180312.
    • (2000) J Orthop Res , vol.18 , pp. 406-415
    • Mikic, B.1    Wong, M.2    Chiquet, M.3    Hunziker, E.B.4
  • 52
  • 53
    • 44649117332 scopus 로고    scopus 로고
    • Influence of perfusion and cyclic compression on proliferation and differentiation of bone marrow stromal cells in 3-dimensional culture
    • doi: 10.1016/j.jbiomech.2008.04.001
    • Jagodzinski M, Breitbart A, Wehmeier M, Hesse E, Haasper C, Krettek C, Zeichen J, Hankemeier S. Influence of perfusion and cyclic compression on proliferation and differentiation of bone marrow stromal cells in 3-dimensional culture. J Biomech. 2008;41:1885-91. doi: 10.1016/j.jbiomech.2008.04.001.
    • (2008) J Biomech , vol.41 , pp. 1885-1891
    • Jagodzinski, M.1    Breitbart, A.2    Wehmeier, M.3    Hesse, E.4    Haasper, C.5    Krettek, C.6    Zeichen, J.7    Hankemeier, S.8
  • 54
    • 84872947606 scopus 로고    scopus 로고
    • Fluid flow forces and rhoA regulate fibrous development of the atrioventricular valves
    • doi: 10.1016/j.ydbio.2012.11.023
    • Tan H, Biechler S, Junor L, Yost MJ, Dean D, Li J, Potts JD, Goodwin RL. Fluid flow forces and rhoA regulate fibrous development of the atrioventricular valves. Dev Biol. 2013;374:345-56. doi: 10.1016/j.ydbio.2012.11.023.
    • (2013) Dev Biol , vol.374 , pp. 345-356
    • Tan, H.1    Biechler, S.2    Junor, L.3    Yost, M.J.4    Dean, D.5    Li, J.6    Potts, J.D.7    Goodwin, R.L.8
  • 55
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • doi: 10.1038/nature03896
    • Kung C. A possible unifying principle for mechanosensation. Nature. 2005;436:647-54. doi: 10.1038/nature03896.
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 56
    • 58049211966 scopus 로고    scopus 로고
    • Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus
    • doi: 10.1038/nrm2594
    • Wang N, Tytell JD, Ingber DE. Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Nat Rev Mol Cell Biol. 2009;10:75-82. doi: 10.1038/nrm2594.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 75-82
    • Wang, N.1    Tytell, J.D.2    Ingber, D.E.3
  • 57
    • 80053900363 scopus 로고    scopus 로고
    • The transcriptional regulator megakaryoblastic leukemia-1 mediates serum response factor-independent activation of tenascin-C transcription by mechanical stress
    • doi: 10.1096/fj.11-187310
    • Asparuhova MB, Ferralli J, Chiquet M, Chiquet-Ehrismann R. The transcriptional regulator megakaryoblastic leukemia-1 mediates serum response factor-independent activation of tenascin-C transcription by mechanical stress. FASEB J. 2011;25:3477-88. doi: 10.1096/fj.11-187310.
    • (2011) FASEB J , vol.25 , pp. 3477-3488
    • Asparuhova, M.B.1    Ferralli, J.2    Chiquet, M.3    Chiquet-Ehrismann, R.4
  • 58
    • 77956187161 scopus 로고    scopus 로고
    • Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis
    • doi: 10.1016/j.biocel.2010.07.001
    • 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;42:1717-28. doi: 10.1016/j.biocel.2010.07.001.
    • (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
  • 59
    • 67349089040 scopus 로고    scopus 로고
    • From mechanotransduction to extracellular matrix gene expression in fibroblasts
    • doi: 10.1016/j.bbamcr.2009.01.012
    • Chiquet M, Gelman L, Lutz R, Maier S. From mechanotransduction to extracellular matrix gene expression in fibroblasts. Biochim Biophys Acta. 2009;1793:911-20. doi: 10.1016/j.bbamcr.2009.01.012.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 911-920
    • Chiquet, M.1    Gelman, L.2    Lutz, R.3    Maier, S.4
  • 60
    • 69149102112 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in tuning cellular responses to external mechanical stress
    • doi: 10.1111/j.1600-0838.2009.00928.x
    • Asparuhova MB, Gelman L, Chiquet M. Role of the actin cytoskeleton in tuning cellular responses to external mechanical stress. Scand J Med Sci Sports. 2009;19:490-9. doi: 10.1111/j.1600-0838.2009.00928.x.
    • (2009) Scand J Med Sci Sports , vol.19 , pp. 490-499
    • Asparuhova, M.B.1    Gelman, L.2    Chiquet, M.3
  • 61
    • 36148950528 scopus 로고    scopus 로고
    • Gene regulation by mechanotransduction in fibroblasts
    • doi: 10.1139/h07-053
    • Chiquet M, Tunc-Civelek V, Sarasa-Renedo A. Gene regulation by mechanotransduction in fibroblasts. Appl Physiol Nutr Metab. 2007;32:967-73. doi: 10.1139/h07-053.
    • (2007) Appl Physiol Nutr Metab , vol.32 , pp. 967-973
    • Chiquet, M.1    Tunc-Civelek, V.2    Sarasa-Renedo, A.3
  • 62
    • 33646058254 scopus 로고    scopus 로고
    • Role of RhoA/ROCK-dependent actin contractility in the induction of tenascin-C by cyclic tensile strain
    • doi: 10.1016/j.yexcr.2005.12.025
    • Sarasa-Renedo A, Tunc-Civelek V, Chiquet M. Role of RhoA/ROCK-dependent actin contractility in the induction of tenascin-C by cyclic tensile strain. Exp Cell Res. 2006;312:1361-70. doi: 10.1016/j.yexcr.2005.12.025.
    • (2006) Exp Cell Res , vol.312 , pp. 1361-1370
    • Sarasa-Renedo, A.1    Tunc-Civelek, V.2    Chiquet, M.3
  • 64
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 1992;70:389-99.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 65
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles F, Posern G, Zaromytidou AI, Treisman R. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell. 2003;113:329-42.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 66
    • 37849015440 scopus 로고    scopus 로고
    • RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding
    • doi: 10.1128/mcb.01623-07
    • Guettler S, Vartiainen MK, Miralles F, Larijani B, Treisman R. RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding. Mol Cell Biol. 2008;28:732-42. doi: 10.1128/mcb.01623-07.
    • (2008) Mol Cell Biol , vol.28 , pp. 732-742
    • Guettler, S.1    Vartiainen, M.K.2    Miralles, F.3    Larijani, B.4    Treisman, R.5
  • 67
    • 77951728146 scopus 로고    scopus 로고
    • Pericellular fibronectin is required for RhoA-dependent responses to cyclic strain in fibroblasts
    • doi: 10.1242/jcs.060905
    • Lutz R, Sakai T, Chiquet M. Pericellular fibronectin is required for RhoA-dependent responses to cyclic strain in fibroblasts. J Cell Sci. 2010;123:1511-21. doi: 10.1242/jcs.060905.
    • (2010) J Cell Sci , vol.123 , pp. 1511-1521
    • Lutz, R.1    Sakai, T.2    Chiquet, M.3
  • 68
    • 52049090807 scopus 로고    scopus 로고
    • Combined lysophosphatidic acid/platelet-derived growth factor signaling triggers glioma cell migration in a tenascin-C microenvironment
    • doi: 10.1158/0008-5472.can-08-0347
    • Lange K, Kammerer M, Saupe F, Hegi ME, Grotegut S, Fluri E, Orend G. Combined lysophosphatidic acid/platelet-derived growth factor signaling triggers glioma cell migration in a tenascin-C microenvironment. Cancer Res. 2008;68:6942-52. doi: 10.1158/0008-5472.can-08-0347.
    • (2008) Cancer Res , vol.68 , pp. 6942-6952
    • Lange, K.1    Kammerer, M.2    Saupe, F.3    Hegi, M.E.4    Grotegut, S.5    Fluri, E.6    Orend, G.7
  • 70
    • 79960993177 scopus 로고    scopus 로고
    • Fibronectin and tenascin-C: accomplices in vascular morphogenesis during development and tumor growth
    • doi: 10.1387/ijdb.103243eo
    • Van Obberghen-Schilling E, Tucker RP, Saupe F, Gasser I, Cseh B, Orend G. Fibronectin and tenascin-C: accomplices in vascular morphogenesis during development and tumor growth. Int J Dev Biol. 2011;55:511-25. doi: 10.1387/ijdb.103243eo.
    • (2011) Int J Dev Biol , vol.55 , pp. 511-525
    • Van Obberghen-Schilling, E.1    Tucker, R.P.2    Saupe, F.3    Gasser, I.4    Cseh, B.5    Orend, G.6
  • 71
    • 19244385785 scopus 로고    scopus 로고
    • Folding-unfolding of FN-III domains in tenascin: an elastically coupled two-state system
    • Marin JL, Muniz J, Huerta M, Trujillo X. Folding-unfolding of FN-III domains in tenascin: an elastically coupled two-state system. J Biomech. 2003;36:1733-7.
    • (2003) J Biomech , vol.36 , pp. 1733-1737
    • Marin, J.L.1    Muniz, J.2    Huerta, M.3    Trujillo, X.4
  • 72
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • doi: 10.1038/30270
    • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 1998;393:181-5. doi: 10.1038/30270.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 74
    • 0037672165 scopus 로고    scopus 로고
    • The dynamic expression of tenascin-C and tenascin-X during early heart development in the mouse
    • Imanaka-Yoshida K, Matsumoto K, Hara M, Sakakura T, Yoshida T. The dynamic expression of tenascin-C and tenascin-X during early heart development in the mouse. Differentiation. 2003;71:291-8.
    • (2003) Differentiation , vol.71 , pp. 291-298
    • Imanaka-Yoshida, K.1    Matsumoto, K.2    Hara, M.3    Sakakura, T.4    Yoshida, T.5
  • 75
    • 0029061401 scopus 로고
    • Molecular regulation of atrioventricular valvuloseptal morphogenesis
    • Eisenberg LM, Markwald RR. Molecular regulation of atrioventricular valvuloseptal morphogenesis. Circ Res. 1995;77:1-6.
    • (1995) Circ Res , vol.77 , pp. 1-6
    • Eisenberg, L.M.1    Markwald, R.R.2
  • 76
    • 16844380290 scopus 로고    scopus 로고
    • Cell biology of cardiac cushion development
    • doi: 10.1016/s0074-7696(05)43005-3
    • Person AD, Klewer SE, Runyan RB. Cell biology of cardiac cushion development. Int Rev Cytol. 2005;243:287-335. doi: 10.1016/s0074-7696(05)43005-3.
    • (2005) Int Rev Cytol , vol.243 , pp. 287-335
    • Person, A.D.1    Klewer, S.E.2    Runyan, R.B.3
  • 77
    • 0032953451 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transformation in the embryonic heart is mediated through distinct pertussis toxin-sensitive and TGFbeta signal transduction mechanisms
    • doi: 10.1002/(sici)1097-0177(199901)214:1<81::aid-dvdy8>3.0.co;2-3
    • Boyer AS, Erickson CP, Runyan RB. Epithelial-mesenchymal transformation in the embryonic heart is mediated through distinct pertussis toxin-sensitive and TGFbeta signal transduction mechanisms. Dev Dyn. 1999;214:81-91. doi: 10.1002/(sici)1097-0177(199901)214:1<81::aid-dvdy8>3.0.co;2-3.
    • (1999) Dev Dyn , vol.214 , pp. 81-91
    • Boyer, A.S.1    Erickson, C.P.2    Runyan, R.B.3
  • 78
    • 0025734106 scopus 로고
    • Expression of adhesion molecules during the formation and differentiation of the avian endocardial cushion tissue
    • Crossin KL, Hoffman S. Expression of adhesion molecules during the formation and differentiation of the avian endocardial cushion tissue. Dev Biol. 1991;145:277-86.
    • (1991) Dev Biol , vol.145 , pp. 277-286
    • Crossin, K.L.1    Hoffman, S.2
  • 79
    • 0027461522 scopus 로고
    • The extracellular matrix glycoproteins BM-90 and tenascin are expressed in the mesenchyme at sites of endothelial-mesenchymal conversion in the embryonic mouse heart
    • Zhang HY, Kluge M, Timpl R, Chu ML, Ekblom P. The extracellular matrix glycoproteins BM-90 and tenascin are expressed in the mesenchyme at sites of endothelial-mesenchymal conversion in the embryonic mouse heart. Differentiation. 1993;52:211-20.
    • (1993) Differentiation , vol.52 , pp. 211-220
    • Zhang, H.Y.1    Kluge, M.2    Timpl, R.3    Chu, M.L.4    Ekblom, P.5
  • 80
    • 0029873444 scopus 로고    scopus 로고
    • Formation and early morphogenesis of endocardial endothelial precursor cells and the role of endoderm
    • doi: 10.1006/dbio.1996.0096
    • Sugi Y, Markwald RR. Formation and early morphogenesis of endocardial endothelial precursor cells and the role of endoderm. Dev Biol. 1996;175:66-83. doi: 10.1006/dbio.1996.0096.
    • (1996) Dev Biol , vol.175 , pp. 66-83
    • Sugi, Y.1    Markwald, R.R.2
  • 81
    • 0025231707 scopus 로고
    • Immunofluorescent localization of tenascin during the morphogenesis of the outflow tract of the chick embryo heart
    • Hurle JM, Garcia-Martinez V, Ros MA. Immunofluorescent localization of tenascin during the morphogenesis of the outflow tract of the chick embryo heart. Anat Embryol (Berl). 1990;181:149-55.
    • (1990) Anat Embryol (Berl) , vol.181 , pp. 149-155
    • Hurle, J.M.1    Garcia-Martinez, V.2    Ros, M.A.3
  • 82
    • 0030051077 scopus 로고    scopus 로고
    • Morphogenetic alterations during endocardial cushion development in the trisomy 16 (Down syndrome) mouse
    • Hiltgen GG, Markwald RR, Litke LL. Morphogenetic alterations during endocardial cushion development in the trisomy 16 (Down syndrome) mouse. Pediatr Cardiol. 1996;17:21-30.
    • (1996) Pediatr Cardiol , vol.17 , pp. 21-30
    • Hiltgen, G.G.1    Markwald, R.R.2    Litke, L.L.3
  • 83
    • 84883188295 scopus 로고    scopus 로고
    • Binding of alphavbeta1 and alphavbeta6 integrins to tenascin-C induces epithelial-mesenchymal transition-like change of breast cancer cells
    • doi: 10.1038/oncsis.2013.27
    • Katoh D, Nagaharu K, Shimojo N, Hanamura N, Yamashita M, Kozuka Y, Imanaka-Yoshida K, Yoshida T. Binding of alphavbeta1 and alphavbeta6 integrins to tenascin-C induces epithelial-mesenchymal transition-like change of breast cancer cells. Oncogenesis. 2013;2:e65. doi: 10.1038/oncsis.2013.27.
    • (2013) Oncogenesis , vol.2
    • Katoh, D.1    Nagaharu, K.2    Shimojo, N.3    Hanamura, N.4    Yamashita, M.5    Kozuka, Y.6    Imanaka-Yoshida, K.7    Yoshida, T.8
  • 84
    • 79951841887 scopus 로고    scopus 로고
    • Tenascin C induces epithelial-mesenchymal transition-like change accompanied by SRC activation and focal adhesion kinase phosphorylation in human breast cancer cells
    • doi: 10.1016/j.ajpath.2010.10.015
    • Nagaharu K, Zhang X, Yoshida T, Katoh D, Hanamura N, Kozuka Y, Ogawa T, Shiraishi T, Imanaka-Yoshida K. Tenascin C induces epithelial-mesenchymal transition-like change accompanied by SRC activation and focal adhesion kinase phosphorylation in human breast cancer cells. Am J Pathol. 2011;178:754-63. doi: 10.1016/j.ajpath.2010.10.015.
    • (2011) Am J Pathol , vol.178 , pp. 754-763
    • Nagaharu, K.1    Zhang, X.2    Yoshida, T.3    Katoh, D.4    Hanamura, N.5    Kozuka, Y.6    Ogawa, T.7    Shiraishi, T.8    Imanaka-Yoshida, K.9
  • 86
    • 2442639010 scopus 로고    scopus 로고
    • Development of heart valve leaflets and supporting apparatus in chicken and mouse embryos
    • doi: 10.1002/dvdy.20051
    • Lincoln J, Alfieri CM, Yutzey KE. Development of heart valve leaflets and supporting apparatus in chicken and mouse embryos. Dev Dyn. 2004;230:239-50. doi: 10.1002/dvdy.20051.
    • (2004) Dev Dyn , vol.230 , pp. 239-250
    • Lincoln, J.1    Alfieri, C.M.2    Yutzey, K.E.3
  • 87
    • 33646924001 scopus 로고    scopus 로고
    • BMP and FGF regulatory pathways control cell lineage diversification of heart valve precursor cells
    • doi: 10.1016/j.ydbio.2005.12.042
    • Lincoln J, Alfieri CM, Yutzey KE. BMP and FGF regulatory pathways control cell lineage diversification of heart valve precursor cells. Dev Biol. 2006;292:290-302. doi: 10.1016/j.ydbio.2005.12.042.
    • (2006) Dev Biol , vol.292 , pp. 290-302
    • Lincoln, J.1    Alfieri, C.M.2    Yutzey, K.E.3
  • 88
    • 33745400942 scopus 로고    scopus 로고
    • Extracellular matrix remodeling and organization in developing and diseased aortic valves
    • doi: 10.1161/01.RES.0000224114.65109.4e
    • Hinton RB, Jr., Lincoln J, Deutsch GH, Osinska H, Manning PB, Benson DW, Yutzey KE. Extracellular matrix remodeling and organization in developing and diseased aortic valves. Circ Res. 2006;98:1431-8. doi: 10.1161/01.RES.0000224114.65109.4e.
    • (2006) Circ Res , vol.98 , pp. 1431-1438
    • Hinton Jr., R.B.1    Lincoln, J.2    Deutsch, G.H.3    Osinska, H.4    Manning, P.B.5    Benson, D.W.6    Yutzey, K.E.7
  • 89
    • 34247376587 scopus 로고    scopus 로고
    • BMP and FGF regulatory pathways in semilunar valve precursor cells
    • doi: 10.1002/dvdy.21097
    • Zhao B, Etter L, Hinton RB, Jr., Benson DW. BMP and FGF regulatory pathways in semilunar valve precursor cells. Dev Dyn. 2007;236:971-80. doi: 10.1002/dvdy.21097.
    • (2007) Dev Dyn , vol.236 , pp. 971-980
    • Zhao, B.1    Etter, L.2    Hinton Jr., R.B.3    Benson, D.W.4
  • 90
    • 33745102721 scopus 로고    scopus 로고
    • Hearts and bones: shared regulatory mechanisms in heart valve, cartilage, tendon, and bone development
    • doi: 10.1016/j.ydbio.2006.03.027
    • Lincoln J, Lange AW, Yutzey KE. Hearts and bones: shared regulatory mechanisms in heart valve, cartilage, tendon, and bone development. Dev Biol. 2006;294:292-302. doi: 10.1016/j.ydbio.2006.03.027.
    • (2006) Dev Biol , vol.294 , pp. 292-302
    • Lincoln, J.1    Lange, A.W.2    Yutzey, K.E.3
  • 91
    • 1542348472 scopus 로고    scopus 로고
    • Signals regulating tendon formation during chick embryonic development
    • doi: 10.1002/dvdy.10481
    • Edom-Vovard F, Duprez D. Signals regulating tendon formation during chick embryonic development. Dev Dyn. 2004;229:449-57. doi: 10.1002/dvdy.10481.
    • (2004) Dev Dyn , vol.229 , pp. 449-457
    • Edom-Vovard, F.1    Duprez, D.2
  • 92
    • 0036308681 scopus 로고    scopus 로고
    • Fgf4 positively regulates scleraxis and tenascin expression in chick limb tendons
    • Edom-Vovard F, Schuler B, Bonnin MA, Teillet MA, Duprez D. Fgf4 positively regulates scleraxis and tenascin expression in chick limb tendons. Dev Biol. 2002;247:351-66.
    • (2002) Dev Biol , vol.247 , pp. 351-366
    • Edom-Vovard, F.1    Schuler, B.2    Bonnin, M.A.3    Teillet, M.A.4    Duprez, D.5
  • 93
    • 70149088960 scopus 로고    scopus 로고
    • Heart valve development: regulatory networks in development and disease
    • doi: 10.1161/circresaha.109.201566
    • Combs MD, Yutzey KE. Heart valve development: regulatory networks in development and disease. Circ Res. 2009;105:408-21. doi: 10.1161/circresaha.109.201566.
    • (2009) Circ Res , vol.105 , pp. 408-421
    • Combs, M.D.1    Yutzey, K.E.2
  • 94
    • 84874236612 scopus 로고    scopus 로고
    • New insights into the developmental mechanisms of coronary vessels and epicardium
    • doi: 10.1016/b978-0-12-407697-6.00007-6
    • Nakajima Y, Imanaka-Yoshida K. New insights into the developmental mechanisms of coronary vessels and epicardium. Int Rev Cell Mol Biol. 2013;303:263-317. doi: 10.1016/b978-0-12-407697-6.00007-6.
    • (2013) Int Rev Cell Mol Biol , vol.303 , pp. 263-317
    • Nakajima, Y.1    Imanaka-Yoshida, K.2
  • 95
    • 79958134271 scopus 로고    scopus 로고
    • Tenascin C may regulate the recruitment of smooth muscle cells during coronary artery development
    • doi: 10.1016/j.diff.2011.03.002
    • Ando K, Takahashi M, Yamagishi T, Miyagawa-Tomita S, Imanaka-Yoshida K, Yoshida T, Nakajima Y. Tenascin C may regulate the recruitment of smooth muscle cells during coronary artery development. Differentiation. 2011;81:299-306. doi: 10.1016/j.diff.2011.03.002.
    • (2011) Differentiation , vol.81 , pp. 299-306
    • Ando, K.1    Takahashi, M.2    Yamagishi, T.3    Miyagawa-Tomita, S.4    Imanaka-Yoshida, K.5    Yoshida, T.6    Nakajima, Y.7
  • 97
    • 85027956045 scopus 로고    scopus 로고
    • Mechanotransduction: the role of mechanical stress, myocyte shape, and cytoskeletal architecture on cardiac function
    • doi: 10.1007/s00424-011-0951-4
    • McCain ML, Parker KK. Mechanotransduction: the role of mechanical stress, myocyte shape, and cytoskeletal architecture on cardiac function. Pflugers Arch. 2011;462:89-104. doi: 10.1007/s00424-011-0951-4.
    • (2011) Pflugers Arch , vol.462 , pp. 89-104
    • McCain, M.L.1    Parker, K.K.2
  • 98
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ('costameres') mark sites of attachment between myofibrils and sarcolemma
    • Pardo JV, Siliciano JD, Craig SW. 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. 1983;80:1008-12.
    • (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
  • 99
    • 0020506125 scopus 로고
    • Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers
    • Pardo JV, Siliciano JD, Craig SW. Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers. J Cell Biol. 1983;97:1081-8.
    • (1983) J Cell Biol , vol.97 , pp. 1081-1088
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 100
    • 77951620985 scopus 로고    scopus 로고
    • Mechanical stress-induced sarcomere assembly for cardiac muscle growth in length and width
    • doi: 10.1016/j.yjmcc.2010.02.016
    • Russell B, Curtis MW, Koshman YE, Samarel AM. Mechanical stress-induced sarcomere assembly for cardiac muscle growth in length and width. J Mol Cell Cardiol. 2010;48:817-23. doi: 10.1016/j.yjmcc.2010.02.016.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 817-823
    • Russell, B.1    Curtis, M.W.2    Koshman, Y.E.3    Samarel, A.M.4
  • 101
    • 28144435989 scopus 로고    scopus 로고
    • Costameres, focal adhesions, and cardiomyocyte mechanotransduction
    • H2291-H301
    • Samarel AM. Costameres, focal adhesions, and cardiomyocyte mechanotransduction. Am J Physiol Heart Circ Physiol 2005;289:H2291-H301.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Samarel, A.M.1
  • 102
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • doi: 0.1152/ajpheart.00749.2005
    • Danowski BA, Imanaka-Yoshida K, Sanger JM, Sanger JW. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J Cell Biol. 1992;118:1411-20. doi: 0.1152/ajpheart.00749.2005.
    • (1992) J Cell Biol , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 103
    • 0029929689 scopus 로고    scopus 로고
    • Living adult rat cardiomyocytes in culture: evidence for dissociation of costameric distribution of vinculin from costameric distributions of attachments
    • doi:10.1002/(sici)1097-0169(1996)33:4<263::aid-cm3>3.0.co;2-a
    • Imanaka-Yoshida K, Danowski BA, Sanger JM, Sanger JW. Living adult rat cardiomyocytes in culture: evidence for dissociation of costameric distribution of vinculin from costameric distributions of attachments. Cell Motil Cytoskeleton. 1996;33:263-75. doi:10.1002/(sici)1097-0169(1996)33:4<263::aid-cm3>3.0.co;2-a.
    • (1996) Cell Motil Cytoskeleton , vol.33 , pp. 263-275
    • Imanaka-Yoshida, K.1    Danowski, B.A.2    Sanger, J.M.3    Sanger, J.W.4
  • 104
    • 0033040088 scopus 로고    scopus 로고
    • Vinculin, Talin, Integrin alpha6beta1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix
    • doi: 10.1002/(sici)1097-0169(1999)42:1<1::aid-cm1>3.0.co;2-0
    • Imanaka-Yoshida K, Enomoto-Iwamoto M, Yoshida T, Sakakura T. Vinculin, Talin, Integrin alpha6beta1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix. Cell Motil Cytoskeleton. 1999;42:1-11. doi: 10.1002/(sici)1097-0169(1999)42:1<1::aid-cm1>3.0.co;2-0.
    • (1999) Cell Motil Cytoskeleton , vol.42 , pp. 1-11
    • Imanaka-Yoshida, K.1    Enomoto-Iwamoto, M.2    Yoshida, T.3    Sakakura, T.4
  • 105
    • 1842454323 scopus 로고    scopus 로고
    • Interaction between cell and extracellular matrix in heart disease: multiple roles of tenascin-C in tissue remodeling
    • Imanaka-Yoshida K, Hiroe M, Yoshida T. Interaction between cell and extracellular matrix in heart disease: multiple roles of tenascin-C in tissue remodeling. Histol Histopathol. 2004;19:517-25.
    • (2004) Histol Histopathol , vol.19 , pp. 517-525
    • Imanaka-Yoshida, K.1    Hiroe, M.2    Yoshida, T.3
  • 106
    • 84856750390 scopus 로고    scopus 로고
    • Matricellular proteins: new molecular targets to prevent heart failure
    • doi: 10.1111/j.1755-5922.2011.00276.x
    • Okamoto H, Imanaka-Yoshida K. Matricellular proteins: new molecular targets to prevent heart failure. Cardiovasc Ther. 2012;30:e198-209. doi: 10.1111/j.1755-5922.2011.00276.x.
    • (2012) Cardiovasc Ther , vol.30
    • Okamoto, H.1    Imanaka-Yoshida, K.2
  • 107
    • 0034939862 scopus 로고    scopus 로고
    • Tenascin-C modulates adhesion of cardiomyocytes to extracellular matrix during tissue remodeling after myocardial infarction
    • Imanaka-Yoshida K, Hiroe M, Nishikawa T, Ishiyama S, Shimojo T, Ohta Y, Sakakura T, Yoshida T. Tenascin-C modulates adhesion of cardiomyocytes to extracellular matrix during tissue remodeling after myocardial infarction. Lab Invest. 2001;81:1015-24.
    • (2001) Lab Invest , vol.81 , pp. 1015-1024
    • Imanaka-Yoshida, K.1    Hiroe, M.2    Nishikawa, T.3    Ishiyama, S.4    Shimojo, T.5    Ohta, Y.6    Sakakura, T.7    Yoshida, T.8
  • 113
    • 0038704997 scopus 로고    scopus 로고
    • Combinatorial control of smooth muscle-specific gene expression
    • doi: 10.1161/01.ATV.0000065197.07635.BA
    • Kumar MS, Owens GK. Combinatorial control of smooth muscle-specific gene expression. Arteriosclerosis, thrombosis, and vascular biology. 2003;23:737-47. doi: 10.1161/01.ATV.0000065197.07635.BA.
    • (2003) Arteriosclerosis, thrombosis, and vascular biology , vol.23 , pp. 737-747
    • Kumar, M.S.1    Owens, G.K.2
  • 114
    • 33746829275 scopus 로고    scopus 로고
    • Transforming growth factor-betas and vascular disorders
    • doi: 10.1161/01.ATV.0000225287.20034.2c
    • Bobik A. Transforming growth factor-betas and vascular disorders. Arteriosclerosis, thrombosis, and vascular biology. 2006;26:1712-20. doi: 10.1161/01.ATV.0000225287.20034.2c.
    • (2006) Arteriosclerosis, thrombosis, and vascular biology , vol.26 , pp. 1712-1720
    • Bobik, A.1
  • 116
    • 23844546577 scopus 로고    scopus 로고
    • Overexpression of transforming growth factor-beta1 stabilizes already-formed aortic aneurysms: a first approach to induction of functional healing by endovascular gene therapy
    • doi: 10.1161/CIRCULATIONAHA.104.523357
    • Dai J, Losy F, Guinault AM, Pages C, Anegon I, Desgranges P, Becquemin JP, Allaire E. Overexpression of transforming growth factor-beta1 stabilizes already-formed aortic aneurysms: a first approach to induction of functional healing by endovascular gene therapy. Circulation. 2005;112:1008-15. doi: 10.1161/CIRCULATIONAHA.104.523357.
    • (2005) Circulation , vol.112 , pp. 1008-1015
    • Dai, J.1    Losy, F.2    Guinault, A.M.3    Pages, C.4    Anegon, I.5    Desgranges, P.6    Becquemin, J.P.7    Allaire, E.8
  • 117
    • 76649100088 scopus 로고    scopus 로고
    • TGF-beta in the pathogenesis and prevention of disease: a matter of aneurysmic proportions
    • doi: 10.1172/jci42014
    • Dietz HC. TGF-beta in the pathogenesis and prevention of disease: a matter of aneurysmic proportions. J Clin Invest. 2010;120:403-7. doi: 10.1172/jci42014.
    • (2010) J Clin Invest , vol.120 , pp. 403-407
    • Dietz, H.C.1
  • 120
    • 57149118835 scopus 로고    scopus 로고
    • Mechanobiology of adult and stem cells
    • doi: 10.1016/s1937-6448(08)01207-0
    • Wang JH, Thampatty BP. Mechanobiology of adult and stem cells. Int Rev Cell Mol Biol. 2008;271:301-46. doi: 10.1016/s1937-6448(08)01207-0.
    • (2008) Int Rev Cell Mol Biol , vol.271 , pp. 301-346
    • Wang, J.H.1    Thampatty, B.P.2
  • 121
    • 57749179515 scopus 로고    scopus 로고
    • Mechanical strain activates a program of genes functionally involved in paracrine signaling of angiogenesis
    • doi: 10.1152/physiolgenomics.90291.2008
    • Yang R, Amir J, Liu H, Chaqour B. Mechanical strain activates a program of genes functionally involved in paracrine signaling of angiogenesis. Physiol Genomics. 2008;36:1-14. doi: 10.1152/physiolgenomics.90291.2008.
    • (2008) Physiol Genomics , vol.36 , pp. 1-14
    • Yang, R.1    Amir, J.2    Liu, H.3    Chaqour, B.4
  • 123
    • 69249107729 scopus 로고    scopus 로고
    • Mechanical regulation of the proangiogenic factor CCN1/CYR61 gene requires the combined activities of MRTF-A and CREB-binding protein histone acetyltransferase
    • doi: 10.1074/jbc.M109.019059
    • Hanna M, Liu H, Amir J, Sun Y, Morris SW, Siddiqui MA, Lau LF, Chaqour B. Mechanical regulation of the proangiogenic factor CCN1/CYR61 gene requires the combined activities of MRTF-A and CREB-binding protein histone acetyltransferase. J Biol Chem. 2009;284:23125-36. doi: 10.1074/jbc.M109.019059.
    • (2009) J Biol Chem , vol.284 , pp. 23125-23136
    • Hanna, M.1    Liu, H.2    Amir, J.3    Sun, Y.4    Morris, S.W.5    Siddiqui, M.A.6    Lau, L.F.7    Chaqour, B.8
  • 124
    • 1642587806 scopus 로고    scopus 로고
    • Three members of the connective tissue growth factor family CCN are differentially regulated by mechanical stress
    • doi: 10.1016/j.bbamcr.2003.12.001
    • Schild C, Trueb B. Three members of the connective tissue growth factor family CCN are differentially regulated by mechanical stress. Biochim Biophys Acta. 2004;1691:33-40. doi: 10.1016/j.bbamcr.2003.12.001.
    • (2004) Biochim Biophys Acta , vol.1691 , pp. 33-40
    • Schild, C.1    Trueb, B.2
  • 125
    • 33746010588 scopus 로고    scopus 로고
    • Mechanical stretch modulates the promoter activity of the profibrotic factor CCN2 through increased actin polymerization and NF-kappaB activation
    • doi: 10.1074/jbc.M600214200
    • Chaqour B, Yang R, Sha Q. Mechanical stretch modulates the promoter activity of the profibrotic factor CCN2 through increased actin polymerization and NF-kappaB activation. J Biol Chem. 2006;281:20608-22. doi: 10.1074/jbc.M600214200.
    • (2006) J Biol Chem , vol.281 , pp. 20608-20622
    • Chaqour, B.1    Yang, R.2    Sha, Q.3
  • 126
    • 84874105864 scopus 로고    scopus 로고
    • Promotion of Ccn2 expression and osteoblastic differentiation by actin polymerization, which is induced by laminar fluid flow stress
    • doi: 10.1007/s12079-012-0177-z
    • Honjo T, Kubota S, Kamioka H, Sugawara Y, Ishihara Y, Yamashiro T, Takigawa M, Takano-Yamamoto T. Promotion of Ccn2 expression and osteoblastic differentiation by actin polymerization, which is induced by laminar fluid flow stress. J Cell Commun Signal. 2012;6:225-32. doi: 10.1007/s12079-012-0177-z.
    • (2012) J Cell Commun Signal , vol.6 , pp. 225-232
    • Honjo, T.1    Kubota, S.2    Kamioka, H.3    Sugawara, Y.4    Ishihara, Y.5    Yamashiro, T.6    Takigawa, M.7    Takano-Yamamoto, T.8
  • 127
    • 0036831230 scopus 로고    scopus 로고
    • Analysis of differential gene expression in stretched podocytes: osteopontin enhances adaptation of podocytes to mechanical stress
    • doi: 10.1096/fj.02-0125fje
    • Endlich N, Sunohara M, Nietfeld W, Wolski EW, Schiwek D, Kranzlin B, Gretz N, Kriz W, Eickhoff H, Endlich K. Analysis of differential gene expression in stretched podocytes: osteopontin enhances adaptation of podocytes to mechanical stress. FASEB J. 2002;16:1850-2. doi: 10.1096/fj.02-0125fje.
    • (2002) FASEB J , vol.16 , pp. 1850-1852
    • Endlich, N.1    Sunohara, M.2    Nietfeld, W.3    Wolski, E.W.4    Schiwek, D.5    Kranzlin, B.6    Gretz, N.7    Kriz, W.8    Eickhoff, H.9    Endlich, K.10
  • 128
    • 68049136011 scopus 로고    scopus 로고
    • Insulin stimulated cardiac glucose oxidation is increased in high-fat diet-induced obese mice lacking malonyl CoA decarboxylase
    • Ussher JR, Koves TR, Jaswal JS, Zhang L, Ilkayeva O, Dyck JR, Muoio DM, Lopaschuk GD. (2009). Insulin stimulated cardiac glucose oxidation is increased in high-fat diet-induced obese mice lacking malonyl CoA decarboxylase. Diabetes 58, 1766-75.
    • (2009) Diabetes , vol.58 , pp. 1766-1775
    • Ussher, J.R.1    Koves, T.R.2    Jaswal, J.S.3    Zhang, L.4    Ilkayeva, O.5    Dyck, J.R.6    Muoio, D.M.7    Lopaschuk, G.D.8
  • 130
    • 0348133545 scopus 로고    scopus 로고
    • Intramyocellular lipids form an important substrate source during moderate intensity exercise in endurance-trained males in a fasted state
    • van Loon LJ, Koopman R, Stegen JH, Wagenmakers AJ, Keizer HA, Saris WH. (2003). Intramyocellular lipids form an important substrate source during moderate intensity exercise in endurance-trained males in a fasted state. J Physiol 553:611-25.
    • (2003) J Physiol , vol.553 , pp. 611-625
    • van Loon, L.J.1    Koopman, R.2    Stegen, J.H.3    Wagenmakers, A.J.4    Keizer, H.A.5    Saris, W.H.6
  • 131
    • 84866665390 scopus 로고    scopus 로고
    • Mitochondria and cancer
    • Wallace DC. (2012). Mitochondria and cancer. Nat Rev Cancer 12:685-98.
    • (2012) Nat Rev Cancer , vol.12 , pp. 685-698
    • Wallace, D.C.1
  • 133
    • 23944486879 scopus 로고    scopus 로고
    • Mechanical strain increases SPARC levels in podocytes: implications for glomerulosclerosis
    • doi: 10.1152/ajprenal.00393.2004
    • Durvasula RV, Shankland SJ. Mechanical strain increases SPARC levels in podocytes: implications for glomerulosclerosis. Am J Physiol Renal Physiol. 2005;289:F577-84. doi: 10.1152/ajprenal.00393.2004.
    • (2005) Am J Physiol Renal Physiol , vol.289
    • Durvasula, R.V.1    Shankland, S.J.2
  • 134
    • 84896698858 scopus 로고    scopus 로고
    • Periostin links mechanical strain to inflammation in abdominal aortic aneurysm
    • e79753. doi: 10.1371/journal.pone.0079753
    • Yamashita O, Yoshimura K, Nagasawa A, Ueda K, Morikage N, Ikeda Y, Hamano K. Periostin links mechanical strain to inflammation in abdominal aortic aneurysm. PLoS One. 2013;8:e79753. doi: 10.1371/journal.pone.0079753.
    • (2013) PLoS One , vol.8
    • Yamashita, O.1    Yoshimura, K.2    Nagasawa, A.3    Ueda, K.4    Morikage, N.5    Ikeda, Y.6    Hamano, K.7
  • 136
    • 76249097588 scopus 로고    scopus 로고
    • Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture
    • doi: 10.1074/jbc.M109.051961
    • Kii I, Nishiyama T, Li M, Matsumoto K, Saito M, Amizuka N, Kudo A. Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture. J Biol Chem. 2010;285:2028-39. doi: 10.1074/jbc.M109.051961.
    • (2010) J Biol Chem , vol.285 , pp. 2028-2039
    • Kii, I.1    Nishiyama, T.2    Li, M.3    Matsumoto, K.4    Saito, M.5    Amizuka, N.6    Kudo, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.