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Volumn 104, Issue 7, 2013, Pages 1623-1633

Novel role for vinculin in ventricular myocyte mechanics and dysfunction

Author keywords

[No Author keywords available]

Indexed keywords

VINCULIN;

EID: 84875880400     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.02.021     Document Type: Article
Times cited : (28)

References (52)
  • 1
    • 0032503970 scopus 로고    scopus 로고
    • Differential actin organization by vinculin isoforms: Implications for cell type-specific microfilament anchorage
    • M. Rüdiger, and N. Korneeva B.M. Jockusch Differential actin organization by vinculin isoforms: implications for cell type-specific microfilament anchorage FEBS Lett. 431 1998 49 54
    • (1998) FEBS Lett. , vol.431 , pp. 49-54
    • Rüdiger, M.1    Korneeva, N.2    Jockusch, B.M.3
  • 2
    • 0030464110 scopus 로고    scopus 로고
    • Signal transduction from the extracellular matrix - A role for the focal adhesion protein-tyrosine kinase FAK
    • D.D. Schlaepfer, and T. Hunter Signal transduction from the extracellular matrix - a role for the focal adhesion protein-tyrosine kinase FAK Cell Struct. Funct. 21 1996 445 450
    • (1996) Cell Struct. Funct. , vol.21 , pp. 445-450
    • Schlaepfer, D.D.1    Hunter, T.2
  • 3
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
    • J.D. Hildebrand, M.D. Schaller, and J.T. Parsons Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions J. Cell Biol. 123 1993 993 1005
    • (1993) J. Cell Biol. , vol.123 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 4
    • 35648949369 scopus 로고    scopus 로고
    • Cardiac-myocyte-specific excision of the vinculin gene disrupts cellular junctions, causing sudden death or dilated cardiomyopathy
    • A.E. Zemljic-Harpf, and J.C. Miller R.S. Ross Cardiac-myocyte-specific excision of the vinculin gene disrupts cellular junctions, causing sudden death or dilated cardiomyopathy Mol. Cell. Biol. 27 2007 7522 7537
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7522-7537
    • Zemljic-Harpf, A.E.1    Miller, J.C.2    Ross, R.S.3
  • 5
    • 4344568148 scopus 로고    scopus 로고
    • Heterozygous inactivation of the vinculin gene predisposes to stress-induced cardiomyopathy
    • A.E. Zemljic-Harpf, and S. Ponrartana R.S. Ross Heterozygous inactivation of the vinculin gene predisposes to stress-induced cardiomyopathy Am. J. Pathol. 165 2004 1033 1044
    • (2004) Am. J. Pathol. , vol.165 , pp. 1033-1044
    • Zemljic-Harpf, A.E.1    Ponrartana, S.2    Ross, R.S.3
  • 6
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • S.M. Palmer, and M.P. Playford S.L. Campbell Lipid binding to the tail domain of vinculin: specificity and the role of the N and C termini J. Biol. Chem. 284 2009 7223 7231
    • (2009) J. Biol. Chem. , vol.284 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Campbell, S.L.3
  • 7
    • 0031817205 scopus 로고    scopus 로고
    • Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • W.H. Goldmann, and R. Galneder R.M. Ezzell Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy Exp. Cell Res. 239 1998 235 242
    • (1998) Exp. Cell Res. , vol.239 , pp. 235-242
    • Goldmann, W.H.1    Galneder, R.2    Ezzell, R.M.3
  • 9
    • 0031213728 scopus 로고    scopus 로고
    • Vinculin is an essential component for normal myofibrillar arrangement in fetal mouse cardiac myocytes
    • I. Shiraishi, and D.G. Simpson T.K. Borg Vinculin is an essential component for normal myofibrillar arrangement in fetal mouse cardiac myocytes J. Mol. Cell. Cardiol. 29 1997 2041 2052
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 2041-2052
    • Shiraishi, I.1    Simpson, D.G.2    Borg, T.K.3
  • 10
    • 0029151575 scopus 로고
    • Laminar structure of the heart: Ventricular myocyte arrangement and connective tissue architecture in the dog
    • I.J. LeGrice, and B.H. Smaill P.J. Hunter Laminar structure of the heart: ventricular myocyte arrangement and connective tissue architecture in the dog Am. J. Physiol. 269 1995 H571 H582
    • (1995) Am. J. Physiol. , vol.269
    • Legrice, I.J.1    Smaill, B.H.2    Hunter, P.J.3
  • 11
    • 28144435989 scopus 로고    scopus 로고
    • Costameres, focal adhesions, and cardiomyocyte mechanotransduction
    • A.M. Samarel Costameres, focal adhesions, and cardiomyocyte mechanotransduction Am. J. Physiol. Heart Circ. Physiol. 289 2005 H2291 H2301
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289
    • Samarel, A.M.1
  • 12
    • 78349298260 scopus 로고    scopus 로고
    • Determination of three-dimensional ventricular strain distributions in gene-targeted mice using tagged MRI
    • J.S. Chuang, and A. Zemljic-Harpf J.H. Omens Determination of three-dimensional ventricular strain distributions in gene-targeted mice using tagged MRI Magn. Reson. Med. 64 2010 1281 1288
    • (2010) Magn. Reson. Med. , vol.64 , pp. 1281-1288
    • Chuang, J.S.1    Zemljic-Harpf, A.2    Omens, J.H.3
  • 13
    • 33744930583 scopus 로고    scopus 로고
    • User-guided 3D active contour segmentation of anatomical structures: Significantly improved efficiency and reliability
    • P.A. Yushkevich, and J. Piven G. Gerig User-guided 3D active contour segmentation of anatomical structures: significantly improved efficiency and reliability Neuroimage 31 2006 1116 1128
    • (2006) Neuroimage , vol.31 , pp. 1116-1128
    • Yushkevich, P.A.1    Piven, J.2    Gerig, G.3
  • 14
    • 0032752454 scopus 로고    scopus 로고
    • Cardiac motion tracking using CINE harmonic phase (HARP) magnetic resonance imaging
    • N.F. Osman, and W.S. Kerwin J.L. Prince Cardiac motion tracking using CINE harmonic phase (HARP) magnetic resonance imaging Magn. Reson. Med. 42 1999 1048 1060
    • (1999) Magn. Reson. Med. , vol.42 , pp. 1048-1060
    • Osman, N.F.1    Kerwin, W.S.2    Prince, J.L.3
  • 15
    • 68649091265 scopus 로고    scopus 로고
    • Hypertrophic gene expression induced by chronic stretch of excised mouse heart muscle
    • A.M. Raskin, and M. Hoshijima J.H. Omens Hypertrophic gene expression induced by chronic stretch of excised mouse heart muscle Mol. Cell. Biomech. 6 2009 145 159
    • (2009) Mol. Cell. Biomech. , vol.6 , pp. 145-159
    • Raskin, A.M.1    Hoshijima, M.2    Omens, J.H.3
  • 16
    • 33750692762 scopus 로고    scopus 로고
    • Method for isolation of adult mouse cardiac myocytes for studies of contraction and microfluorimetry
    • B.M. Wolska, and R.J. Solaro Method for isolation of adult mouse cardiac myocytes for studies of contraction and microfluorimetry Am. J. Physiol. 271 1996 H1250 H1255
    • (1996) Am. J. Physiol. , vol.271
    • Wolska, B.M.1    Solaro, R.J.2
  • 17
    • 77952629071 scopus 로고    scopus 로고
    • Cardiomyocyte contractile status is associated with differences in fibronectin and integrin interactions
    • X. Wu, and Z. Sun M. Muthuchamy Cardiomyocyte contractile status is associated with differences in fibronectin and integrin interactions Am. J. Physiol. Heart Circ. Physiol. 298 2010 H2071 H2081
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.298
    • Wu, X.1    Sun, Z.2    Muthuchamy, M.3
  • 18
    • 78650850233 scopus 로고    scopus 로고
    • Fibronectin increases the force production of mouse papillary muscles via α5β1 integrin
    • X. Wu, and S. Chakraborty M. Muthuchamy Fibronectin increases the force production of mouse papillary muscles via α5β1 integrin J. Mol. Cell. Cardiol. 50 2011 203 213
    • (2011) J. Mol. Cell. Cardiol. , vol.50 , pp. 203-213
    • Wu, X.1    Chakraborty, S.2    Muthuchamy, M.3
  • 19
    • 0018877429 scopus 로고
    • Geometrical factors influencing muscle force development. I. The effect of filament spacing upon axial forces
    • M. Schoenberg Geometrical factors influencing muscle force development. I. The effect of filament spacing upon axial forces Biophys. J. 30 1980 51 67
    • (1980) Biophys. J. , vol.30 , pp. 51-67
    • Schoenberg, M.1
  • 20
    • 0017880528 scopus 로고
    • The mechanism for vertebrate striated muscle contraction
    • F.J. Julian, R.L. Moss, and M.R. Sollins The mechanism for vertebrate striated muscle contraction Circ. Res. 42 1978 2 14
    • (1978) Circ. Res. , vol.42 , pp. 2-14
    • Julian, F.J.1    Moss, R.L.2    Sollins, M.R.3
  • 21
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • I. Rayment, and H.M. Holden R.A. Milligan Structure of the actin-myosin complex and its implications for muscle contraction Science 261 1993 58 65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Milligan, R.A.3
  • 22
    • 0026534068 scopus 로고
    • Z-line/I-band and A-band lattices of intact frog Sartorius muscle at altered interfilament spacing
    • T.C. Irving, and B.M. Millman Z-line/I-band and A-band lattices of intact frog Sartorius muscle at altered interfilament spacing J. Muscle Res. Cell Motil. 13 1992 100 105
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 100-105
    • Irving, T.C.1    Millman, B.M.2
  • 23
    • 3042721428 scopus 로고    scopus 로고
    • Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C
    • B.M. Palmer, and B.K. McConnell D.W. Maughan Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C Mol. Cell. Biochem. 263 2004 73 80
    • (2004) Mol. Cell. Biochem. , vol.263 , pp. 73-80
    • Palmer, B.M.1    McConnell, B.K.2    Maughan, D.W.3
  • 24
    • 0031918744 scopus 로고    scopus 로고
    • The filament lattice of striated muscle
    • B.M. Millman The filament lattice of striated muscle Physiol. Rev. 78 1998 359 391
    • (1998) Physiol. Rev. , vol.78 , pp. 359-391
    • Millman, B.M.1
  • 25
    • 0027551854 scopus 로고
    • Mechanics of active contraction in cardiac muscle: Part i - Constitutive relations for fiber stress that describe deactivation
    • J.M. Guccione, and A.D. McCulloch Mechanics of active contraction in cardiac muscle: part I - constitutive relations for fiber stress that describe deactivation J. Biomech. Eng. 115 1993 72 81
    • (1993) J. Biomech. Eng. , vol.115 , pp. 72-81
    • Guccione, J.M.1    McCulloch, A.D.2
  • 26
    • 0036081583 scopus 로고    scopus 로고
    • Muscle LIM protein deficiency leads to alterations in passive ventricular mechanics
    • J.H. Omens, and T.P. Usyk A.D. McCulloch Muscle LIM protein deficiency leads to alterations in passive ventricular mechanics Am. J. Physiol. Heart Circ. Physiol. 282 2002 H680 H687
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282
    • Omens, J.H.1    Usyk, T.P.2    McCulloch, A.D.3
  • 28
    • 33846074303 scopus 로고    scopus 로고
    • Gender and strain variations in left ventricular cardiac function and mass determined with magnetic resonance imaging at 7 tesla in adult mice
    • P. Croisille, and C. Rotaru B. Hiba Gender and strain variations in left ventricular cardiac function and mass determined with magnetic resonance imaging at 7 tesla in adult mice Invest. Radiol. 42 2007 1 7
    • (2007) Invest. Radiol. , vol.42 , pp. 1-7
    • Croisille, P.1    Rotaru, C.2    Hiba, B.3
  • 29
    • 58249114882 scopus 로고    scopus 로고
    • Quantification of left ventricular volumes and ejection fraction in mice using PET, compared with MRI
    • L. Stegger, and E. Heijman G.J. Strijkers Quantification of left ventricular volumes and ejection fraction in mice using PET, compared with MRI J. Nucl. Med. 50 2009 132 138
    • (2009) J. Nucl. Med. , vol.50 , pp. 132-138
    • Stegger, L.1    Heijman, E.2    Strijkers, G.J.3
  • 30
    • 67049097592 scopus 로고    scopus 로고
    • Transmural myocardial strain in mouse: Quantification of high-resolution MR tagging using harmonic phase (HARP) analysis
    • J. Zhong, W. Liu, and X. Yu Transmural myocardial strain in mouse: quantification of high-resolution MR tagging using harmonic phase (HARP) analysis Magn. Reson. Med. 61 2009 1368 1373
    • (2009) Magn. Reson. Med. , vol.61 , pp. 1368-1373
    • Zhong, J.1    Liu, W.2    Yu, X.3
  • 31
    • 44449104211 scopus 로고    scopus 로고
    • Characterization of three-dimensional myocardial deformation in the mouse heart: An MR tagging study
    • J. Zhong, W. Liu, and X. Yu Characterization of three-dimensional myocardial deformation in the mouse heart: an MR tagging study J. Magn. Reson. Imaging 27 2008 1263 1270
    • (2008) J. Magn. Reson. Imaging , vol.27 , pp. 1263-1270
    • Zhong, J.1    Liu, W.2    Yu, X.3
  • 32
    • 33746879927 scopus 로고    scopus 로고
    • Reperfused myocardial infarction in mice: 3D mapping of late gadolinium enhancement and strain
    • A.A. Young, and B.A. French F.H. Epstein Reperfused myocardial infarction in mice: 3D mapping of late gadolinium enhancement and strain J. Cardiovasc. Magn. Reson. 8 2006 685 692
    • (2006) J. Cardiovasc. Magn. Reson. , vol.8 , pp. 685-692
    • Young, A.A.1    French, B.A.2    Epstein, F.H.3
  • 33
    • 0033049917 scopus 로고    scopus 로고
    • Laminar fiber architecture and three-dimensional systolic mechanics in canine ventricular myocardium
    • K.D. Costa, and Y. Takayama J.W. Covell Laminar fiber architecture and three-dimensional systolic mechanics in canine ventricular myocardium Am. J. Physiol. 276 1999 H595 H607
    • (1999) Am. J. Physiol. , vol.276
    • Costa, K.D.1    Takayama, Y.2    Covell, J.W.3
  • 34
    • 0036084083 scopus 로고    scopus 로고
    • Cell prestress. I. Stiffness and prestress are closely associated in adherent contractile cells
    • N. Wang, and I.M. Tolić-Nørrelykke D. Stamenović Cell prestress. I. Stiffness and prestress are closely associated in adherent contractile cells Am. J. Physiol. Cell Physiol. 282 2002 C606 C616
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Wang, N.1    Tolić-Nørrelykke, I.M.2    Stamenović, D.3
  • 35
    • 0033770910 scopus 로고    scopus 로고
    • Opposing views on tensegrity as a structural framework for understanding cell mechanics
    • D.E. Ingber, and S.R. Heidemann R.E. Buxbaum Opposing views on tensegrity as a structural framework for understanding cell mechanics J. Appl. Physiol. 89 2000 1663 1670
    • (2000) J. Appl. Physiol. , vol.89 , pp. 1663-1670
    • Ingber, D.E.1    Heidemann, S.R.2    Buxbaum, R.E.3
  • 36
    • 0033668412 scopus 로고    scopus 로고
    • Myofilament lattice spacing as a function of sarcomere length in isolated rat myocardium
    • T.C. Irving, and J. Konhilas P.P. de Tombe Myofilament lattice spacing as a function of sarcomere length in isolated rat myocardium Am. J. Physiol. Heart Circ. Physiol. 279 2000 H2568 H2573
    • (2000) Am. J. Physiol. Heart Circ. Physiol. , vol.279
    • Irving, T.C.1    Konhilas, J.2    De Tombe, P.P.3
  • 37
    • 78651233102 scopus 로고    scopus 로고
    • Axial and radial forces of cross-bridges depend on lattice spacing
    • C.D. Williams, M. Regnier, and T.L. Daniel Axial and radial forces of cross-bridges depend on lattice spacing PLOS Comput. Biol. 6 2010 e1001018
    • (2010) PLOS Comput. Biol. , vol.6 , pp. 1001018
    • Williams, C.D.1    Regnier, M.2    Daniel, T.L.3
  • 38
    • 0024318208 scopus 로고
    • MR imaging of motion with spatial modulation of magnetization
    • L. Axel, and L. Dougherty MR imaging of motion with spatial modulation of magnetization Radiology 171 1989 841 845
    • (1989) Radiology , vol.171 , pp. 841-845
    • Axel, L.1    Dougherty, L.2
  • 40
    • 27144507337 scopus 로고    scopus 로고
    • Regional ventricular wall thickening reflects changes in cardiac fiber and sheet structure during contraction: Quantification with diffusion tensor MRI
    • J. Chen, and W. Liu X. Yu Regional ventricular wall thickening reflects changes in cardiac fiber and sheet structure during contraction: quantification with diffusion tensor MRI Am. J. Physiol. Heart Circ. Physiol. 289 2005 H1898 H1907
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289
    • Chen, J.1    Liu, W.2    Yu, X.3
  • 43
    • 0024506533 scopus 로고
    • Electron microscopic studies on the stretch-induced disordering of the myofilament lattice in tetanized frog skeletal muscle fibers
    • S. Suzuki, and T. Tsuchiya H. Sugi Electron microscopic studies on the stretch-induced disordering of the myofilament lattice in tetanized frog skeletal muscle fibers J. Electron Microsc. (Tokyo) 38 1989 60 63
    • (1989) J. Electron Microsc. (Tokyo) , vol.38 , pp. 60-63
    • Suzuki, S.1    Tsuchiya, T.2    Sugi, H.3
  • 44
    • 41149127332 scopus 로고    scopus 로고
    • + (BK) channels by α5β1 integrin activation in arteriolar smooth muscle
    • + (BK) channels by α5β1 integrin activation in arteriolar smooth muscle J. Physiol. 586 2008 1699 1713
    • (2008) J. Physiol. , vol.586 , pp. 1699-1713
    • Wu, X.1    Yang, Y.2    Davis, M.J.3
  • 45
    • 28144436067 scopus 로고    scopus 로고
    • Mechanical properties of the interaction between fibronectin and α5β1-integrin on vascular smooth muscle cells studied using atomic force microscopy
    • Z. Sun, and L.A. Martinez-Lemus G.A. Meininger Mechanical properties of the interaction between fibronectin and α5β1-integrin on vascular smooth muscle cells studied using atomic force microscopy Am. J. Physiol. Heart Circ. Physiol. 289 2005 H2526 H2535
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289
    • Sun, Z.1    Martinez-Lemus, L.A.2    Meininger, G.A.3
  • 46
    • 0033575007 scopus 로고    scopus 로고
    • Single integrin molecule adhesion forces in intact cells measured by atomic force microscopy
    • P.P. Lehenkari, and M.A. Horton Single integrin molecule adhesion forces in intact cells measured by atomic force microscopy Biochem. Biophys. Res. Commun. 259 1999 645 650
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 645-650
    • Lehenkari, P.P.1    Horton, M.A.2
  • 47
    • 33845409769 scopus 로고    scopus 로고
    • Role of diastolic properties in the transition to failure in a mouse model of the cardiac dilatation
    • P.N. Costandi, and L.R. Frank J.H. Omens Role of diastolic properties in the transition to failure in a mouse model of the cardiac dilatation Am. J. Physiol. Heart Circ. Physiol. 291 2006 H2971 H2979
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.291
    • Costandi, P.N.1    Frank, L.R.2    Omens, J.H.3
  • 48
    • 0034156395 scopus 로고    scopus 로고
    • On the development of volumetric strain energy functions
    • S. Doll, and K. Schweizerhof On the development of volumetric strain energy functions J. Appl. Mech. 67 2000 17 21
    • (2000) J. Appl. Mech. , vol.67 , pp. 17-21
    • Doll, S.1    Schweizerhof, K.2
  • 49
    • 0026112935 scopus 로고
    • Passive material properties of intact ventricular myocardium determined from a cylindrical model
    • J.M. Guccione, A.D. McCulloch, and L.K. Waldman Passive material properties of intact ventricular myocardium determined from a cylindrical model J. Biomech. Eng. 113 1991 42 55
    • (1991) J. Biomech. Eng. , vol.113 , pp. 42-55
    • Guccione, J.M.1    McCulloch, A.D.2    Waldman, L.K.3
  • 50
    • 33845501360 scopus 로고    scopus 로고
    • Coupling of a 3D finite element model of cardiac ventricular mechanics to lumped systems models of the systemic and pulmonic circulation
    • R.C. Kerckhoffs, and M.L. Neal A.D. McCulloch Coupling of a 3D finite element model of cardiac ventricular mechanics to lumped systems models of the systemic and pulmonic circulation Ann. Biomed. Eng. 35 2007 1 18
    • (2007) Ann. Biomed. Eng. , vol.35 , pp. 1-18
    • Kerckhoffs, R.C.1    Neal, M.L.2    McCulloch, A.D.3
  • 51
    • 0016262954 scopus 로고
    • Reconsideration of the ultrastructural basis of cardiac length-tension relations
    • E.H. Sonnenblick, and C.L. Skelton Reconsideration of the ultrastructural basis of cardiac length-tension relations Circ. Res. 35 1974 517 526
    • (1974) Circ. Res. , vol.35 , pp. 517-526
    • Sonnenblick, E.H.1    Skelton, C.L.2
  • 52
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • R. Craig, and J.L. Woodhead Structure and function of myosin filaments Curr. Opin. Struct. Biol. 16 2006 204 212
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2


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