메뉴 건너뛰기




Volumn 23, Issue 2, 2009, Pages 149-159

Dystrophin-glycoprotein complex and vinculin-talin-integrin system in human adult cardiac muscle

Author keywords

Atrium; Cardiac muscle; Costameres; Immunohistochemistry; Intercalated disk; T tubules

Indexed keywords

ACTIN; ALPHA SARCOGLYCAN; ALPHA7 INTEGRIN; BETA1 INTEGRIN; DELTA SARCOGLYCAN; DYSTROPHIN; EPSILON SARCOGLYCAN; GAMMA SARCOGLYCAN; GLYCOPROTEIN; INTEGRIN; TALIN; VINCULIN;

EID: 64749115627     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm_00000112     Document Type: Article
Times cited : (33)

References (47)
  • 1
    • 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, D'Angelo Siliciano J and 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 USA 80: 1008-1012, 1983.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    D'Angelo Siliciano, J.2    Craig, S.W.3
  • 2
    • 0020506125 scopus 로고
    • Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers
    • Pardo JV, D'Angelo Siliciano J and Craig SW: Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers. J Cell Biol 97: 1081-1088, 1983.
    • (1983) J Cell Biol , vol.97 , pp. 1081-1088
    • Pardo, J.V.1    D'Angelo Siliciano, J.2    Craig, S.W.3
  • 4
    • 0017798263 scopus 로고
    • The distribution of desmin (100 Å) filaments in primary cultures of embryonic chick cardiac cells
    • Lazarides E: The distribution of desmin (100 Å) filaments in primary cultures of embryonic chick cardiac cells. Exp Cell Res 112: 265-273, 1978.
    • (1978) Exp Cell Res , vol.112 , pp. 265-273
    • Lazarides, E.1
  • 5
    • 0020156264 scopus 로고
    • Widespread occurrence of avian spectrin in non-erythroid cells
    • Repasky EA, Granger BL and Lazarides E: Widespread occurrence of avian spectrin in non-erythroid cells. Cell 29: 821-833, 1982.
    • (1982) Cell , vol.29 , pp. 821-833
    • Repasky, E.A.1    Granger, B.L.2    Lazarides, E.3
  • 6
    • 0021009545 scopus 로고
    • Gamma-actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemmal attachment sites
    • Craig SW and Pardo V: Gamma-actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemmal attachment sites. Cell Motil 3: 449-462, 1983.
    • (1983) Cell Motil , vol.3 , pp. 449-462
    • Craig, S.W.1    Pardo, V.2
  • 7
    • 0022458171 scopus 로고
    • Localization of talin in skeletal and cardiac muscle
    • Belkin AM, Zhidkova NI and Koteliansky VE: Localization of talin in skeletal and cardiac muscle. FEBS Lett 200: 32-36, 1986.
    • (1986) FEBS Lett , vol.200 , pp. 32-36
    • Belkin, A.M.1    Zhidkova, N.I.2    Koteliansky, V.E.3
  • 8
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowsky BA, Imanaka-Yoshida K, Sanger JM and Sanger JW: Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J Cell Biol 118: 1411-1420, 1992.
    • (1992) J Cell Biol , vol.118 , pp. 1411-1420
    • Danowsky, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 9
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM and Campbell KP: A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 809-823, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 10
    • 0029990461 scopus 로고    scopus 로고
    • Immunolocalization of the costameres in human skeletal muscle fibers: Confocal scanning laser microscope investigations
    • Mondello MR, Bramanti P, Cutroneo G, Santoro G, Di Mauro D and Anastasi G: Immunolocalization of the costameres in human skeletal muscle fibers: confocal scanning laser microscope investigations. Anat Rec 245: 481-487, 1996.
    • (1996) Anat Rec , vol.245 , pp. 481-487
    • Mondello, M.R.1    Bramanti, P.2    Cutroneo, G.3    Santoro, G.4    Di Mauro, D.5    Anastasi, G.6
  • 11
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M and Ozawa E: Glycoprotein complex anchoring dystrophin to sarcolemma. J Biochem 108: 748-752, 1990.
    • (1990) J Biochem , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 12
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti JM and Campbell KP: Membrane organization of the dystrophin-glycoprotein complex. Cell 66: 1121-1131, 1991.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 14
    • 0032006681 scopus 로고    scopus 로고
    • The role of cytoskeletal proteins in cardiomyopathies
    • Towbin JA: The role of cytoskeletal proteins in cardiomyopathies. Curr Opin Cell Biol 10: 131-139, 1998.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 131-139
    • Towbin, J.A.1
  • 16
    • 0036714792 scopus 로고    scopus 로고
    • Z-sarcoglycan, a novel component of the sarcoglycan complex, is reduced in muscular dystrophy
    • Wheeler MT, Zarnegar S and McNally EM: Z-sarcoglycan, a novel component of the sarcoglycan complex, is reduced in muscular dystrophy. Hum Mol Genet 11: 2147-2154, 2002.
    • (2002) Hum Mol Genet , vol.11 , pp. 2147-2154
    • Wheeler, M.T.1    Zarnegar, S.2    McNally, E.M.3
  • 17
    • 0041559837 scopus 로고    scopus 로고
    • Sarcoglycans in vascular smooth and striated muscle
    • Wheeler MT and McNally EM: Sarcoglycans in vascular smooth and striated muscle. Trends Cardiovasc Med 13: 238-243, 2003.
    • (2003) Trends Cardiovasc Med , vol.13 , pp. 238-243
    • Wheeler, M.T.1    McNally, E.M.2
  • 18
    • 25644444579 scopus 로고    scopus 로고
    • Sarcoglycan subcomplex in normal human smooth muscle: An immunohistochemical and molecular study
    • Anastasi G, Cutroneo G, Sidoti A, et al: Sarcoglycan subcomplex in normal human smooth muscle: an immunohistochemical and molecular study. Int J Mol Med 16: 367-374, 2005.
    • (2005) Int J Mol Med , vol.16 , pp. 367-374
    • Anastasi, G.1    Cutroneo, G.2    Sidoti, A.3
  • 19
    • 34447519221 scopus 로고    scopus 로고
    • Sarcoglycan subcomplex expression in normal human smooth muscle
    • Anastasi G, Cutroneo G, Sidoti A, et al: Sarcoglycan subcomplex expression in normal human smooth muscle. J Histochem Cytochem 55: 831-843, 2007.
    • (2007) J Histochem Cytochem , vol.55 , pp. 831-843
    • Anastasi, G.1    Cutroneo, G.2    Sidoti, A.3
  • 20
    • 0026674188 scopus 로고
    • Transmembrane signaling by integrins
    • Schwartz MA: Transmembrane signaling by integrins. Trends Cell Biol 2: 304-308, 1992.
    • (1992) Trends Cell Biol , vol.2 , pp. 304-308
    • Schwartz, M.A.1
  • 21
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO: Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 23
    • 0029671374 scopus 로고    scopus 로고
    • β1D integrin displaces the β1A isoform in striated muscle: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin AM, Zhidkova NI, Balzac F, et al: β1D integrin displaces the β1A isoform in striated muscle: localization at junctional structures and signaling potential in nonmuscle cells. J Cell Biol 132: 211-226, 1996.
    • (1996) J Cell Biol , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3
  • 24
    • 0031283019 scopus 로고    scopus 로고
    • Muscle β1D integrin reinforces the cytoskeleton-matrix link: Modulation of integrin adhesive function by alternative splicing
    • Belkin AM, Retta SF, Pletjushkina OY, et al: Muscle β1D integrin reinforces the cytoskeleton-matrix link: modulation of integrin adhesive function by alternative splicing. J Cell Biol 139: 1583-1595, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 1583-1595
    • Belkin, A.M.1    Retta, S.F.2    Pletjushkina, O.Y.3
  • 25
    • 0025931224 scopus 로고
    • The subcellular distribution of dystrophin in mouse skeletal, cardiac and smooth muscle
    • Byers TJ, Kunkel LM and Watkins SC: The subcellular distribution of dystrophin in mouse skeletal, cardiac and smooth muscle. J Cell Biol 115: 411-421, 1991.
    • (1991) J Cell Biol , vol.115 , pp. 411-421
    • Byers, T.J.1    Kunkel, L.M.2    Watkins, S.C.3
  • 26
    • 17544379921 scopus 로고    scopus 로고
    • The association of cardiac dystrophin with myofibrils/Z-disc regions in cardiac muscle suggests a novel role in the contractile apparatus
    • Meng H, Leddy JJ, Franki J, Holland P and Tuana BS: The association of cardiac dystrophin with myofibrils/Z-disc regions in cardiac muscle suggests a novel role in the contractile apparatus. J Biol Chem 271: 12364-12371, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 12364-12371
    • Meng, H.1    Leddy, J.J.2    Franki, J.3    Holland, P.4    Tuana, B.S.5
  • 27
    • 0031035219 scopus 로고    scopus 로고
    • Dystrophin is not a specific component of the cardiac costamere
    • Stevenson S, Rothery S, Cullen MJ and Severs NJ: Dystrophin is not a specific component of the cardiac costamere. Circ Res 80: 269-280, 1997.
    • (1997) Circ Res , vol.80 , pp. 269-280
    • Stevenson, S.1    Rothery, S.2    Cullen, M.J.3    Severs, N.J.4
  • 28
    • 0033680710 scopus 로고    scopus 로고
    • Dystrophin and the cardiomyocyte membrane cytoskeleton in the healthy and failing heart
    • Kaprielian RR and Severs NJ: Dystrophin and the cardiomyocyte membrane cytoskeleton in the healthy and failing heart. Heart Fail Rev 5: 221-238, 2000.
    • (2000) Heart Fail Rev , vol.5 , pp. 221-238
    • Kaprielian, R.R.1    Severs, N.J.2
  • 29
    • 0027533969 scopus 로고
    • Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle
    • Klietsch R, Ervasti JM, Arnold W, Campbell KP and Jorgensen AO: Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle. Circ Res 72: 349-360, 1993.
    • (1993) Circ Res , vol.72 , pp. 349-360
    • Klietsch, R.1    Ervasti, J.M.2    Arnold, W.3    Campbell, K.P.4    Jorgensen, A.O.5
  • 30
    • 0028883973 scopus 로고
    • Mutations in the dystrophin-associated protein γ-sarcoglycan in chromosome 13 muscular dystrophy
    • Noguchi S, McNally EM, Ben K, et al: Mutations in the dystrophin-associated protein γ-sarcoglycan in chromosome 13 muscular dystrophy. Science 270: 819-822, 1995.
    • (1995) Science , vol.270 , pp. 819-822
    • Noguchi, S.1    McNally, E.M.2    Ben, K.3
  • 31
    • 0028971221 scopus 로고
    • γ-sarcoglycan: Characterization and role in limb-girdle muscular dystrophy linked to 4q12
    • Lim LE, Duclos F, Broux O, et al: γ-sarcoglycan: characterization and role in limb-girdle muscular dystrophy linked to 4q12. Nat Genet 11: 257-265, 1995.
    • (1995) Nat Genet , vol.11 , pp. 257-265
    • Lim, L.E.1    Duclos, F.2    Broux, O.3
  • 32
    • 34547573673 scopus 로고    scopus 로고
    • Impact of delta-sarcoglycan gene polymorphism on the occurrence of coronary spastic angina in Japanese patients with hypertrophic cardiomyopathy
    • Honda T, Sugiyama S, Sakamoto T, Kaikita K and Ogawa H: Impact of delta-sarcoglycan gene polymorphism on the occurrence of coronary spastic angina in Japanese patients with hypertrophic cardiomyopathy. Circ J 71: 1263-1267, 2007.
    • (2007) Circ J , vol.71 , pp. 1263-1267
    • Honda, T.1    Sugiyama, S.2    Sakamoto, T.3    Kaikita, K.4    Ogawa, H.5
  • 33
    • 10744225733 scopus 로고    scopus 로고
    • Distribution and localization of vinculin-talin-integrin system and dystrophin-glycoprotein complex in human skeletal muscle
    • Anastasi G, Amato A, Tarone G, et al: Distribution and localization of vinculin-talin-integrin system and dystrophin-glycoprotein complex in human skeletal muscle. Cells Tissues Organs 175: 151-164, 2003.
    • (2003) Cells Tissues Organs , vol.175 , pp. 151-164
    • Anastasi, G.1    Amato, A.2    Tarone, G.3
  • 34
    • 0037265833 scopus 로고    scopus 로고
    • Sarcoglycans in human skeletal muscle and human cardiac muscle: A confocal laser scanning microscope study
    • Anastasi G, Cutroneo G, Trimarchi F, et al: Sarcoglycans in human skeletal muscle and human cardiac muscle: a confocal laser scanning microscope study. Cells Tissues Organs 173: 54-63, 2003.
    • (2003) Cells Tissues Organs , vol.173 , pp. 54-63
    • Anastasi, G.1    Cutroneo, G.2    Trimarchi, F.3
  • 35
    • 0026666069 scopus 로고
    • Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers
    • Masuda T, Fujimaki N, Ozawa E and Ishikawa H: Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers. J Cell Biol 119: 543-548, 1992.
    • (1992) J Cell Biol , vol.119 , pp. 543-548
    • Masuda, T.1    Fujimaki, N.2    Ozawa, E.3    Ishikawa, H.4
  • 36
    • 0026785988 scopus 로고
    • Dystrophin at the plasma membrane of human fibres shows a costameric localisation
    • Minetti C, Beltrame F, Marcenaro G and Bonilla E: Dystrophin at the plasma membrane of human fibres shows a costameric localisation. Neuromuscul Disord 2: 99-109, 1992.
    • (1992) Neuromuscul Disord , vol.2 , pp. 99-109
    • Minetti, C.1    Beltrame, F.2    Marcenaro, G.3    Bonilla, E.4
  • 37
    • 0026711133 scopus 로고
    • Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle
    • Porter GA, Dmytrenko GM, Winkelmann JC and Bloch RJ: Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J Cell Biol 117: 997-1005, 1992.
    • (1992) J Cell Biol , vol.117 , pp. 997-1005
    • Porter, G.A.1    Dmytrenko, G.M.2    Winkelmann, J.C.3    Bloch, R.J.4
  • 38
    • 0026453372 scopus 로고
    • Direct visualization of the dystrophin network on skeletal muscle fiber membrane
    • Straub V, Bittner RE, Léger JJ and Voit T: Direct visualization of the dystrophin network on skeletal muscle fiber membrane. J Cell Biol 119: 1183-1191, 1992.
    • (1992) J Cell Biol , vol.119 , pp. 1183-1191
    • Straub, V.1    Bittner, R.E.2    Léger, J.J.3    Voit, T.4
  • 39
    • 0037112402 scopus 로고    scopus 로고
    • Dance band on the Titanic: Biomechanical signaling in cardiac hypertrophy
    • Sussman MA, McCulloch A and Borg TK: Dance band on the Titanic: biomechanical signaling in cardiac hypertrophy. Circ Res 91: 888-898, 2002.
    • (2002) Circ Res , vol.91 , pp. 888-898
    • Sussman, M.A.1    McCulloch, A.2    Borg, T.K.3
  • 40
    • 28144435989 scopus 로고    scopus 로고
    • Costameres, focal adhesions, and cardiomyocyte mechanotransduction
    • Samarel AM: Costameres, focal adhesions, and cardiomyocyte mechanotransduction. Am J Physiol Heart Circ Physiol 289: H2291-H2301, 2005.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Samarel, A.M.1
  • 41
    • 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
    • Imanaka-Yoshida K, Enomoto-Iwamoto M, Yoshida T and 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 421: 1-11, 1999.
    • (1999) Cell Motil Cytoskeleton , vol.421 , pp. 1-11
    • Imanaka-Yoshida, K.1    Enomoto-Iwamoto, M.2    Yoshida, T.3    Sakakura, T.4
  • 42
    • 0030905955 scopus 로고    scopus 로고
    • Myofibrillogenesis in precardiac mesoderm explant culture
    • Imanaka-Yoshida K: Myofibrillogenesis in precardiac mesoderm explant culture. Cell Struct Funct 22: 45-49, 1997.
    • (1997) Cell Struct Funct , vol.22 , pp. 45-49
    • Imanaka-Yoshida, K.1
  • 43
    • 0029843697 scopus 로고    scopus 로고
    • Single channel evidence for a cytoskeletal defect involving acetylcholine receptors and calcium influx in cultured dystrophic (mdx) myotubes
    • Carlson CG and Officer T: Single channel evidence for a cytoskeletal defect involving acetylcholine receptors and calcium influx in cultured dystrophic (mdx) myotubes. Muscle Nerve 19: 1116-1126, 1996.
    • (1996) Muscle Nerve , vol.19 , pp. 1116-1126
    • Carlson, C.G.1    Officer, T.2
  • 44
    • 8044254229 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy
    • Chang WJ, Iannaccone ST, Lau KS, et al: Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy. Proc Natl Acad Sci USA 93: 9142-9147, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9142-9147
    • Chang, W.J.1    Iannaccone, S.T.2    Lau, K.S.3
  • 45
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal cardiac and smooth muscle cells: Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin associated glycoproteins
    • Song KS, Scherer PE, Tang Z, et al: Expression of caveolin-3 in skeletal cardiac and smooth muscle cells: Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin associated glycoproteins. J Biol Chem 271: 15150-15165, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 15150-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3
  • 46
    • 33646127782 scopus 로고    scopus 로고
    • Quantification of calcium entry at the T-tubules and surface membrane in rat ventricular myocytes
    • Brette F, Sallè L and Orchard H: Quantification of calcium entry at the T-tubules and surface membrane in rat ventricular myocytes. Biophys J 90: 381-389, 2006.
    • (2006) Biophys J , vol.90 , pp. 381-389
    • Brette, F.1    Sallè, L.2    Orchard, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.