메뉴 건너뛰기




Volumn 46, Issue 2, 2000, Pages 277-285

Specialization at the Z line of cardiac myocytes

Author keywords

Cell culture isolation; Developmental biology; Extracellular matrix; Myocytes

Indexed keywords

CADHERIN; COLLAGEN TYPE 1; DOCKING PROTEIN;

EID: 0034115115     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(99)00433-2     Document Type: Review
Times cited : (53)

References (72)
  • 1
    • 0342544999 scopus 로고    scopus 로고
    • The role of the extracellular matrix and its receptors in modulating cardiac development
    • R.B. Runyan, & R.J. Tomanek. Development of the cardiovascular system. New York: JAI Press. In press
    • Goldsmith E.C., Carver W. The role of the extracellular matrix and its receptors in modulating cardiac development. Runyan R.B., Tomanek R.J. Development of the cardiovascular system. Heart development. vol. I:2000;JAI Press, New York. In press.
    • (2000) Heart Development , vol.1
    • Goldsmith, E.C.1    Carver, W.2
  • 2
    • 0030995745 scopus 로고    scopus 로고
    • N-cadherin-catenin interaction: Necessary component of cardiac cell compartmentalization during early vertebrate heart development
    • Linask K.K., Knudsen K.A., Gui Y.H. N-cadherin-catenin interaction: necessary component of cardiac cell compartmentalization during early vertebrate heart development. Dev. Biol. (Orlando). 185:1997;148-164.
    • (1997) Dev. Biol. (Orlando) , vol.185 , pp. 148-164
    • Linask, K.K.1    Knudsen, K.A.2    Gui, Y.H.3
  • 3
    • 0030860779 scopus 로고    scopus 로고
    • Temporal and spatial patterns of phosphotyrosine immunolocalization during cardiac myofibrillogenesis of the chicken embryo
    • Shiraishi I., Takamatsu T., Price R.L., Fujita S. Temporal and spatial patterns of phosphotyrosine immunolocalization during cardiac myofibrillogenesis of the chicken embryo. Anat Embryol. 196:1997;81-89.
    • (1997) Anat Embryol , vol.196 , pp. 81-89
    • Shiraishi, I.1    Takamatsu, T.2    Price, R.L.3    Fujita, S.4
  • 4
    • 0028984922 scopus 로고
    • Three dimensional observation with a confocal scanning laser microscope of fibronectin immunolabeling during cardiac looping in the chick embryo
    • Shiraishi I., Takamatsu T., Fujita S. Three dimensional observation with a confocal scanning laser microscope of fibronectin immunolabeling during cardiac looping in the chick embryo. Anat Embryol. 191:1995;183-189.
    • (1995) Anat Embryol , vol.191 , pp. 183-189
    • Shiraishi, I.1    Takamatsu, T.2    Fujita, S.3
  • 5
    • 0031983145 scopus 로고    scopus 로고
    • N-cadherin is required for the differentiation and initial myofibrillogenesis of chick cardiomyocytes
    • Imanaka-Yoshida K., Knudsen K.A., Linask K.K. N-cadherin is required for the differentiation and initial myofibrillogenesis of chick cardiomyocytes. Cell Motil Cytoskelt. 39:1998;52-62.
    • (1998) Cell Motil Cytoskelt , vol.39 , pp. 52-62
    • Imanaka-Yoshida, K.1    Knudsen, K.A.2    Linask, K.K.3
  • 7
    • 0015835701 scopus 로고
    • Distribution and relationship of precursor Z material to organizing myofibrillar bundles in embryonic rat and hamster ventricular myocytes
    • Markwald R.R. Distribution and relationship of precursor Z material to organizing myofibrillar bundles in embryonic rat and hamster ventricular myocytes. J Mol Cell Cardiol. 5:1973;341-350.
    • (1973) J Mol Cell Cardiol , vol.5 , pp. 341-350
    • Markwald, R.R.1
  • 8
    • 0024532139 scopus 로고
    • Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. III Generation of fasciae adherentes and costameres
    • Tokuyasu K.T. Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. III Generation of fasciae adherentes and costameres. J Cell Biol. 108:1989;43-53.
    • (1989) J Cell Biol , vol.108 , pp. 43-53
    • Tokuyasu, K.T.1
  • 10
    • 0020444113 scopus 로고
    • Development of the connective tissue network in the neonatal hamster heart
    • Borg T.K. Development of the connective tissue network in the neonatal hamster heart. Am J Anat. 165:1982;435-445.
    • (1982) Am J Anat , vol.165 , pp. 435-445
    • Borg, T.K.1
  • 11
    • 0018427165 scopus 로고
    • The collagen network of the heart
    • Caulfield J.B., Borg T.K. The collagen network of the heart. Lab Invest. 40:1979;364-372.
    • (1979) Lab Invest , vol.40 , pp. 364-372
    • Caulfield, J.B.1    Borg, T.K.2
  • 13
    • 0026558556 scopus 로고
    • Urokinase activity in the developing avian heart: A spatial and temporal analysis
    • McQuire P.G., Orkin R.W. Urokinase activity in the developing avian heart: a spatial and temporal analysis. Dev Dyn. 193:1992;24-33.
    • (1992) Dev Dyn , vol.193 , pp. 24-33
    • McQuire, P.G.1    Orkin, R.W.2
  • 14
    • 0032969233 scopus 로고    scopus 로고
    • Interaction of metargidin (ADAM-15) with αvβ3 and α5βl integrins on different haemopoietic cells
    • Nath D., Slocombe P.M., Stephens P.E., et al. Interaction of metargidin (ADAM-15) with αvβ3 and α5βl integrins on different haemopoietic cells. J Cell Sci. 112:1999;579-587.
    • (1999) J Cell Sci , vol.112 , pp. 579-587
    • Nath, D.1    Slocombe, P.M.2    Stephens, P.E.3
  • 15
    • 0030589505 scopus 로고    scopus 로고
    • Adams in fertilization and development
    • Wolfsberg T.G., White J.M. Adams in fertilization and development. Dev Biol (Orlando). 180:1996;389-401.
    • (1996) Dev Biol (Orlando) , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 16
    • 0032515050 scopus 로고    scopus 로고
    • A cellular striptease act (comment)
    • Yan Y., Werb Z. A cellular striptease act (comment). Science (USA). 282:1998;1279-1280.
    • (1998) Science (USA) , vol.282 , pp. 1279-1280
    • Yan, Y.1    Werb, Z.2
  • 17
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan R., Primakoff P., Myles D.G. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J Cell Biol. 137:1997;105112.
    • (1997) J Cell Biol , vol.137 , pp. 105112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 18
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegin ADAM 10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip N.U., Dallas D.J., Wu E., Dale S., McKie N. The metallo-disintegin ADAM 10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem Biophys Res Commun. 245:1998;594-598.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 594-598
    • Millichip, N.U.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 19
    • 0032525330 scopus 로고    scopus 로고
    • β1 Integrins participate in the hypertrophic response of rat ventricular myocytes
    • Ross R.S., Pham C., Shai S.Y., et al. β1 Integrins participate in the hypertrophic response of rat ventricular myocytes. Circ Res. 82:(11):1998;1160-1172.
    • (1998) Circ Res , vol.82 , Issue.11 , pp. 1160-1172
    • Ross, R.S.1    Pham, C.2    Shai, S.Y.3
  • 21
    • 0032571395 scopus 로고    scopus 로고
    • The low molecular weight GTPase rho regulates myofibril formation and organization in neonatal rat ventricular myocytes: Involvement of rho kinase
    • Hoshijima M., Sah V.P., Wang V.P., Chien K.R., Heller Brown J. The low molecular weight GTPase rho regulates myofibril formation and organization in neonatal rat ventricular myocytes: involvement of rho kinase. J Biol Chem. 273:1998;7725-7730.
    • (1998) J Biol Chem , vol.273 , pp. 7725-7730
    • Hoshijima, M.1    Sah, V.P.2    Wang, V.P.3    Chien, K.R.4    Heller Brown, J.5
  • 22
    • 0029658495 scopus 로고    scopus 로고
    • Rho is required for Gαq and α1-adrenergic receptor signaling in cardiomyocytes: Dissociation of ras and rho pathways
    • Sah V.P., Hoshijima M., Chien K.R., Heller Brown J. Rho is required for Gαq and α1-adrenergic receptor signaling in cardiomyocytes: dissociation of ras and rho pathways. J Biol Chem. 271:1996;31185-31190.
    • (1996) J Biol Chem , vol.271 , pp. 31185-31190
    • Sah, V.P.1    Hoshijima, M.2    Chien, K.R.3    Heller Brown, J.4
  • 23
    • 0032489871 scopus 로고    scopus 로고
    • Angiotensin II activates RhoA in cardiac myocytes:a critical role of rhoA in angiotgensin II-induced premyofibril formation
    • Aoki H., Izumo S., Sadoshima J. Angiotensin II activates RhoA in cardiac myocytes:a critical role of rhoA in angiotgensin II-induced premyofibril formation. Circ Res. 82:1998;666-676.
    • (1998) Circ Res , vol.82 , pp. 666-676
    • Aoki, H.1    Izumo, S.2    Sadoshima, J.3
  • 24
    • 0032031590 scopus 로고    scopus 로고
    • Ras and Rho are required for Gαq-induced hypertrophic gene expression in neonatal rat cardiac myocytes
    • Hine W.A., Thorburn A. Ras and Rho are required for Gαq-induced hypertrophic gene expression in neonatal rat cardiac myocytes. J Mol Cell Cardiol. 30:1998;485-494.
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 485-494
    • Hine, W.A.1    Thorburn, A.2
  • 25
    • 0030790752 scopus 로고    scopus 로고
    • Studies on the function of Rho A protein in cardiac myofibrillogenesis
    • Wang S.-M., Tsai Y.-J., Tseng Y.Z. Studies on the function of Rho A protein in cardiac myofibrillogenesis. J Cell Biochem. 66:1997;43-53.
    • (1997) J Cell Biochem , vol.66 , pp. 43-53
    • Wang, S.-M.1    Tsai, Y.-J.2    Tseng, Y.Z.3
  • 26
    • 0032570809 scopus 로고    scopus 로고
    • Mechanical stressing of integrin receptors induces enhanced tyrosine phosphorylation of cytoskeletally anchored proteins
    • Schmidt C., Pommerenke H., Durr F., Nebe B., Rychly J. Mechanical stressing of integrin receptors induces enhanced tyrosine phosphorylation of cytoskeletally anchored proteins. J Biol Chem. 273:1998;5081-5085.
    • (1998) J Biol Chem , vol.273 , pp. 5081-5085
    • Schmidt, C.1    Pommerenke, H.2    Durr, F.3    Nebe, B.4    Rychly, J.5
  • 27
    • 0027722248 scopus 로고
    • Autocrine release of angiotensin II mediates stretch-induced hypertrophy of cardiac myocytes in vitro
    • Sadoshima J., Xu Y., Slater H.S., Izumo S. Autocrine release of angiotensin II mediates stretch-induced hypertrophy of cardiac myocytes in vitro. Cell. 75:1993;979-984.
    • (1993) Cell , vol.75 , pp. 979-984
    • Sadoshima, J.1    Xu, Y.2    Slater, H.S.3    Izumo, S.4
  • 28
    • 13344287048 scopus 로고    scopus 로고
    • Endothelin-1 is involved in mechanical stress-induced cardiomyocyte hypertrophy
    • Yamazaki T., Komuro I., Kudoh S. Endothelin-1 is involved in mechanical stress-induced cardiomyocyte hypertrophy. J Biol Chem. 271:1996;3221-3228.
    • (1996) J Biol Chem , vol.271 , pp. 3221-3228
    • Yamazaki, T.1    Komuro, I.2    Kudoh, S.3
  • 29
    • 0032486371 scopus 로고    scopus 로고
    • Autocrine/paracrine determinants of strain-activated brain natriuretic peptide gene expression in cultured cardiac myocytes
    • Liang F., Gardner D.G. Autocrine/paracrine determinants of strain-activated brain natriuretic peptide gene expression in cultured cardiac myocytes. J Biol Chem. 273:1998;14612-14619.
    • (1998) J Biol Chem , vol.273 , pp. 14612-14619
    • Liang, F.1    Gardner, D.G.2
  • 30
    • 0025064494 scopus 로고
    • Distribution of vinculin in the Z-disk of striated muscle: Analysis by laser scanning confocal microscopy
    • Terracio L., Simpson D.G., Hilenski L., et al. Distribution of vinculin in the Z-disk of striated muscle: Analysis by laser scanning confocal microscopy. J Cell Physiol. 145:1990;78-87.
    • (1990) J Cell Physiol , vol.145 , pp. 78-87
    • Terracio, L.1    Simpson, D.G.2    Hilenski, L.3
  • 32
    • 0029929689 scopus 로고    scopus 로고
    • Living adult rat cardiomyocytes in culture: Evidence for dissociation of costameric distribution of vinculin from costameric distributions of attachments
    • Imanaka-Yoshida K., Danowski B.A., Sanger J.M., Sanger J.W. Living adult rat cardiomyocytes in culture: evidence for dissociation of costameric distribution of vinculin from costameric distributions of attachments. Cell Motil Cytoskelt. 33:1996;263-275.
    • (1996) Cell Motil Cytoskelt , vol.33 , pp. 263-275
    • Imanaka-Yoshida, K.1    Danowski, B.A.2    Sanger, J.M.3    Sanger, J.W.4
  • 33
    • 0026026685 scopus 로고
    • Expression of collagen-binding integrins during cardiac development and hypertrophy
    • Terracio L., Rubin K., Gullberg D., et al. Expression of collagen-binding integrins during cardiac development and hypertrophy. Circ Res. 68:1991;734-744.
    • (1991) Circ Res , vol.68 , pp. 734-744
    • Terracio, L.1    Rubin, K.2    Gullberg, D.3
  • 34
    • 0026729525 scopus 로고
    • The vinculin/sarcomeric-α-actinin/α-actin nexus in cultured cardiac myocytes
    • Lu M.H., DiLullo C., Schultheiss T., et al. The vinculin/sarcomeric-α-actinin/α-actin nexus in cultured cardiac myocytes. J Cell Biol. 117:1992;1007-1022.
    • (1992) J Cell Biol , vol.117 , pp. 1007-1022
    • Lu, M.H.1    Dilullo, C.2    Schultheiss, T.3
  • 35
    • 0026683672 scopus 로고
    • The role of β1 integrin in spreading and myofibrillogenesis in neonatal rat cardiac myocytes in vitro
    • Hilenski K.K., Xuehui M.A., Vinson N., Terracio L., Borg T.K. The role of β1 integrin in spreading and myofibrillogenesis in neonatal rat cardiac myocytes in vitro. Cell Motil Cytoskelt. 21:1992;87-100.
    • (1992) Cell Motil Cytoskelt , vol.21 , pp. 87-100
    • Hilenski, K.K.1    Xuehui, M.A.2    Vinson, N.3    Terracio, L.4    Borg, T.K.5
  • 36
    • 0027424026 scopus 로고
    • Contractile activity and cell-cell contact regulate myofibrillar organization in cultured cardiac myocytes
    • Simpson D.G., Decker M.L., Clark W.A., Decker R.S. Contractile activity and cell-cell contact regulate myofibrillar organization in cultured cardiac myocytes. J Cell Biol. 123:1993;323-336.
    • (1993) J Cell Biol , vol.123 , pp. 323-336
    • Simpson, D.G.1    Decker, M.L.2    Clark, W.A.3    Decker, R.S.4
  • 37
    • 33751297308 scopus 로고    scopus 로고
    • Mechanical forces regulate focal adhesion and costamere assembly in cardiac myocytes
    • Sharp W.W., Simpson D.G., Borg T.K., Samarel A.M., Terracio L. Mechanical forces regulate focal adhesion and costamere assembly in cardiac myocytes. Am J Physiol. 273:1997;H546-H556.
    • (1997) Am J Physiol , vol.273 , pp. 546-H556
    • Sharp, W.W.1    Simpson, D.G.2    Borg, T.K.3    Samarel, A.M.4    Terracio, L.5
  • 38
    • 0022509093 scopus 로고
    • Load regulation of the properties of adult feline cardiocytes: The role of substrate adhesion
    • Cooper G., Mercer W.E., Hoober J.K., et al. Load regulation of the properties of adult feline cardiocytes: the role of substrate adhesion. Circ Res. 58:1986;692-705.
    • (1986) Circ Res , vol.58 , pp. 692-705
    • Cooper, G.1    Mercer, W.E.2    Hoober, J.K.3
  • 39
    • 0023607765 scopus 로고
    • Role of contraction in the structure and growth of neonatal rat cardiocytes
    • Marino T.A., Kuseryk L., Lauva I.K. Role of contraction in the structure and growth of neonatal rat cardiocytes. Am J Physiol. 253:1987;H391-H399.
    • (1987) Am J Physiol , vol.253 , pp. 391-H399
    • Marino, T.A.1    Kuseryk, L.2    Lauva, I.K.3
  • 40
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E.A., Brugge J.S. Integrins and signal transduction pathways: the road taken. Science. 268:1995;233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 41
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson A., Parsons J.T. Signal transduction through integrins: a central role for focal adhesion kinase? BioEssays. 17:1995;229-236.
    • (1995) BioEssays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 43
    • 0029154733 scopus 로고
    • 2+-induced regulation of ion channel and MAP kinase functions
    • 2+-induced regulation of ion channel and MAP kinase functions. Nature. 376:1995;737-745.
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno Hl Martinez, R.2
  • 44
    • 0031058040 scopus 로고    scopus 로고
    • Association of tyrosine-phosphorylated c-Src with the cytoskeleton of hypertrophying myocardium
    • Kuppuswamy D., Keff C., Narishige T., Kasi V., Menick D.R., Cooper G IV. 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    Keff, C.2    Narishige, T.3    Kasi, V.4    Menick, D.R.5    Cooper G. IV6
  • 45
    • 0342544995 scopus 로고    scopus 로고
    • Contraction-dependent hypertrophy of neonatal rat ventricular myocytes: Potential role for focal adhesion kinase
    • N. Takeda, & N.S. Dhalla. Boston: Kluwer. In press
    • Eble D.K., Qi M., Strait J., Samarel A.M. Contraction-dependent hypertrophy of neonatal rat ventricular myocytes: potential role for focal adhesion kinase. Takeda N., Dhalla N.S. The hypertrophied heart. 1999;Kluwer, Boston. In press.
    • (1999) The Hypertrophied Heart
    • Eble, D.K.1    Qi, M.2    Strait, J.3    Samarel, A.M.4
  • 46
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein
    • Guan J.L., Trevithick J.E., Hynes R.O. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein. Cell Regul. 2:1991;951-964.
    • (1991) Cell Regul , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 47
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, ppl25FAK, directs SH2-dependent binding of pp60Src
    • Schaller N.O., Hildebrand J.D., Shannon J.D., Fox J.W., Vines R.R., Parsons J.T. Autophosphorylation of the focal adhesion kinase, ppl25FAK, directs SH2-dependent binding of pp60Src. Mol Cell Biol. 14:1994;1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, N.O.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 48
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity
    • Calalb M.B., Polte T.R., Hanks S.K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity. Mol Cell Biol. 15:1995;954-963.
    • (1995) Mol Cell Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 49
    • 0030597218 scopus 로고    scopus 로고
    • Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src
    • Calalb N.O., Zhang X., Polte T.R., Hanks S.K. Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src. Biochem Biophys Res Commun. 228:1996;662-668.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 662-668
    • Calalb, N.O.1    Zhang, X.2    Polte, T.R.3    Hanks, S.K.4
  • 50
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein tyrosine kinases
    • Schlaepfer D.D., Hunter T. Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein tyrosine kinases. Mol Cell Biol. 16:1996;5623-5633.
    • (1996) Mol Cell Biol , vol.16 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 51
    • 0029925581 scopus 로고    scopus 로고
    • Thrombin stimulates association of Src homology domain containing adaptor protein Nck with ppl25FAK
    • Choudhury G.G., Marra F., Abboud B.E. Thrombin stimulates association of Src homology domain containing adaptor protein Nck with ppl25FAK. Am J Physiol. 270:1996;F295-F300.
    • (1996) Am J Physiol , vol.270 , pp. 295-F300
    • Choudhury, G.G.1    Marra, F.2    Abboud, B.E.3
  • 52
    • 0026726189 scopus 로고
    • Ultrastructural localization of laminin in in vivo embryonic, neonatal, and adult rat cardiac myocytes and early rat embryos raised in whole embryo culture
    • Price R.L., Nakagawa M., Terracio L., Borg T.K. Ultrastructural localization of laminin in in vivo embryonic, neonatal, and adult rat cardiac myocytes and early rat embryos raised in whole embryo culture. J Histochem Cytochem. 40:1992;1373-1381.
    • (1992) J Histochem Cytochem , vol.40 , pp. 1373-1381
    • Price, R.L.1    Nakagawa, M.2    Terracio, L.3    Borg, T.K.4
  • 53
    • 0022973240 scopus 로고
    • A-CAM: A 135 kD receptor of intercellular adherens junctions: Immunoelectron microscopic localization and biochemical studies
    • Volk T., Geiger B. A-CAM: a 135 kD receptor of intercellular adherens junctions: Immunoelectron microscopic localization and biochemical studies. J Cell Biol. 103:1986;1441-1450.
    • (1986) J Cell Biol , vol.103 , pp. 1441-1450
    • Volk, T.1    Geiger, B.2
  • 54
    • 0032926868 scopus 로고    scopus 로고
    • Localization and quantitation of cardiac annexin II, V, and VI in hypertensive guinea pigs
    • Trouve P., Legot S., Belikova I., et al. Localization and quantitation of cardiac annexin II, V, and VI in hypertensive guinea pigs. Am J Physiol. 276:1999;H1159-H1166.
    • (1999) Am J Physiol , vol.276 , pp. 1159-H1166
    • Trouve, P.1    Legot, S.2    Belikova, I.3
  • 55
    • 0031573943 scopus 로고    scopus 로고
    • The effects of angiotensin II and specific angiotensin receptor blockers on embryonic cardiac development
    • Price R.L., Carver W., Simpson D.G., et al. The effects of angiotensin II and specific angiotensin receptor blockers on embryonic cardiac development. Dev Biol. 192:1997;572-584.
    • (1997) Dev Biol , vol.192 , pp. 572-584
    • Price, R.L.1    Carver, W.2    Simpson, D.G.3
  • 57
    • 0029745535 scopus 로고    scopus 로고
    • A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function
    • Johnson J.A., Gray M.O., Chen C.H., Mochly-Rosen D. A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function. J Biol Chem. 271:1996;24962-24966.
    • (1996) J Biol Chem , vol.271 , pp. 24962-24966
    • Johnson, J.A.1    Gray, M.O.2    Chen, C.H.3    Mochly-Rosen, D.4
  • 58
    • 0027966390 scopus 로고
    • Paxillin: A cytoskeletal target for tryosine kinases
    • Turner C.E. Paxillin: a cytoskeletal target for tryosine kinases. Bioessays. 16:1994;47-52.
    • (1994) Bioessays , vol.16 , pp. 47-52
    • Turner, C.E.1
  • 59
    • 0032547857 scopus 로고    scopus 로고
    • Stretch-induced alkalinization of feline papillary muscle: An autocrine-paracrine system
    • Cingolani H.E., Alvarez B.V., Ennis I.L., Camilion de Hurtado M.C. Stretch-induced alkalinization of feline papillary muscle: an autocrine-paracrine system. Circ Res. 83:1998;775-780.
    • (1998) Circ Res , vol.83 , pp. 775-780
    • Cingolani, H.E.1    Alvarez, B.V.2    Ennis, I.L.3    Camilion De Hurtado, M.C.4
  • 60
    • 0343850654 scopus 로고    scopus 로고
    • The role of n-linked oligosaccharides on cell adhesion and phenotype in cardiac myocytes and fibroblasts
    • (submitted)
    • Reaves TA, Simpson DG, Terracio L, Borg TK. The role of n-linked oligosaccharides on cell adhesion and phenotype in cardiac myocytes and fibroblasts. J Mol Cell Cardiol 2000 (submitted).
    • (2000) J Mol Cell Cardiol
    • Reaves, T.A.1    Simpson, D.G.2    Terracio, L.3    Borg, T.K.4
  • 61
    • 0028785480 scopus 로고
    • The extracellular matrix during heart development
    • Little C.D., Rongish B.J. The extracellular matrix during heart development. Experimenta. 51:1995;873-882.
    • (1995) Experimenta , vol.51 , pp. 873-882
    • Little, C.D.1    Rongish, B.J.2
  • 63
    • 0034691295 scopus 로고    scopus 로고
    • Left ventricular hypertrophy in ascending aortic stenosis mice: anoikis and the progression to early failure
    • (in press)
    • Ding B, Price RL, Borg TK et al. Left ventricular hypertrophy in ascending aortic stenosis mice: anoikis and the progression to early failure. Circulation 2000 (in press).
    • (2000) Circulation
    • Ding, B.1    Price, R.L.2    Borg, T.K.3
  • 64
    • 0024822345 scopus 로고
    • Effects of extracellular matrix on cytoskeletal and myofibrillar organization in vitro
    • Hilenski L.L., Terracio L., Sawyer R., Borg T.K. Effects of extracellular matrix on cytoskeletal and myofibrillar organization in vitro. Scan Microsc. 3:1989;535-548.
    • (1989) Scan Microsc , vol.3 , pp. 535-548
    • Hilenski, L.L.1    Terracio, L.2    Sawyer, R.3    Borg, T.K.4
  • 65
    • 0030799487 scopus 로고    scopus 로고
    • Distribution and orientation of rhodamine-phalloidin bound to thin filaments in skeletal and cardiac myofibrils
    • Zhkarev V., Sanger J.M., Sanger J.W., Goldman Y.E., Shuman H. Distribution and orientation of rhodamine-phalloidin bound to thin filaments in skeletal and cardiac myofibrils. Cell Motil Cytoskelt. 37:1997;363-377.
    • (1997) Cell Motil Cytoskelt , vol.37 , pp. 363-377
    • Zhkarev, V.1    Sanger, J.M.2    Sanger, J.W.3    Goldman, Y.E.4    Shuman, H.5
  • 66
    • 0033013812 scopus 로고    scopus 로고
    • Myofibrillogenesis in the developing chicken heart: Assembly of Z-disk, M-line and the thick filaments
    • Ehler E., Rothen B.M., Hammerle S.P., Komiyama M., Perriard J.C. Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments. J Cell Sci. 112:1999;1529-1539.
    • (1999) J Cell Sci , vol.112 , pp. 1529-1539
    • Ehler, E.1    Rothen, B.M.2    Hammerle, S.P.3    Komiyama, M.4    Perriard, J.C.5
  • 67
    • 0028149868 scopus 로고
    • Modulation of cardiac myocyte phenotype in vitro by the composition and orientation of the extracellular matrix
    • Simpson D.G., Terracio L., Terracio M., Price R.L., Turner D.C., Borg T.K. Modulation of cardiac myocyte phenotype in vitro by the composition and orientation of the extracellular matrix. J Cell Physiol. 161:1994;89-105.
    • (1994) J Cell Physiol , vol.161 , pp. 89-105
    • Simpson, D.G.1    Terracio, L.2    Terracio, M.3    Price, R.L.4    Turner, D.C.5    Borg, T.K.6
  • 69
    • 0033550149 scopus 로고    scopus 로고
    • Regulation of cardiac myocyte protein turnover and myofibrillar structure in vitro by specific directions of stretch
    • (in press)
    • Simpson DG, Majeski K, Borg TK, Terracio L. Regulation of cardiac myocyte protein turnover and myofibrillar structure in vitro by specific directions of stretch. Circ Res 1999 (in press).
    • (1999) Circ Res
    • Simpson, D.G.1    Majeski, K.2    Borg, T.K.3    Terracio, L.4
  • 70
    • 0033105762 scopus 로고    scopus 로고
    • Dietrich C. Looking at lipid rafts?
    • Jacobson K. Dietrich C. Looking at lipid rafts? Trends Cell Biol. 9:1999;87-91.
    • (1999) Trends Cell Biol , vol.9 , pp. 87-91
    • Jacobson, K.1
  • 71
    • 0030724031 scopus 로고    scopus 로고
    • Compartmentalization of eukaryotic gene expression: Causes and effects
    • St. Johnson E. Compartmentalization of eukaryotic gene expression: causes and effects. Cell. 91:1997;291-294.
    • (1997) Cell , vol.91 , pp. 291-294
    • St. Johnson, E.1
  • 72
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchor proteins: A theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchor proteins: A theme in signal transduction. Science (USA). 268:1995;247-250.
    • (1995) Science (USA) , vol.268 , pp. 247-250
    • Mochly-Rosen, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.