메뉴 건너뛰기




Volumn 22, Issue 1, 1997, Pages 191-195

Models of thin filament assembly in cardiac and skeletal muscle

Author keywords

Actin filament; Capping proteins; Cardiac muscle; Myofibril assembly; Skeletal muscle; Tropomodulin

Indexed keywords

ALPHA ACTIN;

EID: 0030994919     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.191     Document Type: Conference Paper
Times cited : (18)

References (37)
  • 1
    • 0028116302 scopus 로고
    • Isoform specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins
    • BABCOCK, G.G. and FOWLER, V.M. 1994. Isoform specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins. J. Biol. Chem., 269: 27510-27518.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27510-27518
    • Babcock, G.G.1    Fowler, V.M.2
  • 2
  • 3
    • 0028453839 scopus 로고
    • Actin assembly in response to extracellular signals: Role of capping proteins, thymosin β-4, and profilin
    • CARLIER, M.F. and PANTALONI, D. 1994. Actin assembly in response to extracellular signals: role of capping proteins, thymosin β-4, and profilin. Semin. Cell Biol., 5: 183-191.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 183-191
    • Carlier, M.F.1    Pantaloni, D.2
  • 4
    • 0023034626 scopus 로고
    • Purification and initial characterization of a protein from skeletal muscle that caps tbe barbed ends of actin filaments
    • CASELLA, J.F., MAACK, D.J., and LIN, S. 1986. Purification and initial characterization of a protein from skeletal muscle that caps tbe barbed ends of actin filaments. J. Biol. Chem., 261: 10915-10921.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10915-10921
    • Casella, J.F.1    Maack, D.J.2    Lin, S.3
  • 5
    • 0023372284 scopus 로고
    • (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J. Cell Biol., 105: 371-379.
    • (1987) J. Cell Biol. , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 6
    • 0025782315 scopus 로고
    • Molecular analysis of protein assembly in muscle development
    • EPSTEIN, H.F. and FISCHMAM, D.A. 1991. Molecular analysis of protein assembly in muscle development. Science, 251: 1039-1044.
    • (1991) Science , vol.251 , pp. 1039-1044
    • Epstein, H.F.1    Fischmam, D.A.2
  • 7
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • FOWLER, V.M. 1996. Regulation of actin filament length in erythrocytes and striated muscle. Curr. Opin. Cell Biol., 8: 86-96.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 8
    • 0028914944 scopus 로고
    • Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosin for assembly
    • GREGORIO, C.C. and FOWLER, V.M. 1995. Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosin for assembly. J. Cell Biol., 129: 683-695.
    • (1995) J. Cell Biol. , vol.129 , pp. 683-695
    • Gregorio, C.C.1    Fowler, V.M.2
  • 9
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • GREGORIO, C.C., WEBER, A., BONDAD, M., PENNISE, C.R., and FOWLER, V.M. 1995. Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature, 377: 83-86.
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 10
    • 0029888857 scopus 로고    scopus 로고
    • Tropomodulin function and thin filament assembly in cardiac myocytes
    • GREGORIO, C.C. and FOWLER, V.M. 1996. Tropomodulin function and thin filament assembly in cardiac myocytes. Trends Card. Med., 6: 136-141.
    • (1996) Trends Card. Med. , vol.6 , pp. 136-141
    • Gregorio, C.C.1    Fowler, V.M.2
  • 11
    • 0001425662 scopus 로고
    • Muscle Cells
    • (J. Brachet A.E. Mirsky, eds). Academic Press, New York
    • HUXLEY, H.E. 1960. Muscle Cells. In The Cell: Biochemistry, Physiology, Morphology (J. Brachet A.E. Mirsky, eds). Academic Press, New York, pp. 365-481 [Vol. 1].
    • (1960) The Cell: Biochemistry, Physiology, Morphology , vol.1 , pp. 365-481
    • Huxley, H.E.1
  • 12
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • KELLER, T.C.S. III. 1995. Structure and function of titin and nebulin. Curr. Opin. Cell Biol., 7: 32-38.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 32-38
    • Keller III, T.C.S.1
  • 13
    • 0014483095 scopus 로고
    • Myofibrillogenesis and Z-band differentiation
    • KELLY, D.E. 1969. Myofibrillogenesis and Z-band differentiation. Anat. Rec., 163: 403-426.
    • (1969) Anat. Rec. , vol.163 , pp. 403-426
    • Kelly, D.E.1
  • 14
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filaments length, nebulin size, and epitope profile
    • KRUGER, M., WRIGHT, J. and WANG, K. 1991. Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filaments length, nebulin size, and epitope profile. J. Cell Biol., 115: 97-107.
    • (1991) J. Cell Biol. , vol.115 , pp. 97-107
    • Kruger, M.1    Wright, J.2    Wang, K.3
  • 16
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • LABEIT, S. and KOLMERER, B. 1995. The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol., 248: 308-315.
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 17
    • 0022380542 scopus 로고
    • Zeugmatin: A new high molecular weight protein associated with the Z-lines in adult and early embryonic striated muscle
    • MAHER, P.A., COX, G.F., and SINGER, S.J. 1985. Zeugmatin: a new high molecular weight protein associated with the Z-lines in adult and early embryonic striated muscle. J. Cell Biol., 101: 1871-1883.
    • (1985) J. Cell Biol. , vol.101 , pp. 1871-1883
    • Maher, P.A.1    Cox, G.F.2    Singer, S.J.3
  • 18
    • 0015835701 scopus 로고
    • Distribution and relationship of precursor Z material to organizing myofibrillar bundles in embryonic rat and hamster ventricular myocytes
    • MARKWALD, R.R. 1973. Distribution and relationship of precursor Z material to organizing myofibrillar bundles in embryonic rat and hamster ventricular myocytes. J. Mol. Cell Cardiol., 5: 341-350.
    • (1973) J. Mol. Cell Cardiol. , vol.5 , pp. 341-350
    • Markwald, R.R.1
  • 19
    • 0022980637 scopus 로고
    • Formation and alignment of Z-lines in living chick myotubes microinjected with rhodamine-labelled alpha-actinin
    • MCKENNA, N., JOHNSON, C., and WANG, Y. 1986. Formation and alignment of Z-lines in living chick myotubes microinjected with rhodamine-labelled alpha-actinin. J. Cell Biol., 103: 2163-2171.
    • (1986) J. Cell Biol. , vol.103 , pp. 2163-2171
    • Mckenna, N.1    Johnson, C.2    Wang, Y.3
  • 20
    • 0028784365 scopus 로고
    • Nebulette: A 107 kD nebulin-like protein in cardiac muscle
    • MONCMAN, C. and WANG, K. 1995. Nebulette: A 107 kD nebulin-like protein in cardiac muscle. Cell Motil. Cytoskel., 32: 205-225.
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 205-225
    • Moncman, C.1    Wang, K.2
  • 21
    • 0027263236 scopus 로고
    • Contractile Proteins and Myofibrillogenesis
    • OBINATA, T. 1993. Contractile Proteins and Myofibrillogenesis. Intern. Rev. Cytology, 143: 153-189.
    • (1993) Intern. Rev. Cytology , vol.143 , pp. 153-189
    • Obinata, T.1
  • 22
    • 0019869554 scopus 로고
    • The development of myofibrils in cultured muscle cells: A whole mount and thin-section electron microscopic study
    • PENG, H.B., WOLOSEWICK, J.J., and CHENG, P.-C. 1981. The development of myofibrils in cultured muscle cells: A whole mount and thin-section electron microscopic study. Dev. Biol., 88: 121-126.
    • (1981) Dev. Biol. , vol.88 , pp. 121-126
    • Peng, H.B.1    Wolosewick, J.J.2    Cheng, P.-C.3
  • 23
    • 0028278854 scopus 로고
    • The premyofibril: Evidence for its role in myofibrillogenesis
    • RHEE, D., SANGER, J.M., and SANGER, J.W. 1994. The premyofibril: evidence for its role in myofibrillogenesis. Cell Motil. Cytoskel., 28: 1-24.
    • (1994) Cell Motil. Cytoskel. , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 24
    • 0018333449 scopus 로고
    • The measurement and dynamic implications of thin filament lengths in heart muscle
    • ROBINSON, T.F. and WINEGRAD, S. 1979. The measurement and dynamic implications of thin filament lengths in heart muscle. J. Physiol. (London), 286: 617-619.
    • (1979) J. Physiol. (London) , vol.286 , pp. 617-619
    • Robinson, T.F.1    Winegrad, S.2
  • 25
    • 0027178964 scopus 로고
    • Localization of CapZ during myofibrillogenesis in cultured chicken muscle
    • SCHAFER, D.A., WADDLE, J.A., and COOPER, J.A. 1993. Localization of CapZ during myofibrillogenesis in cultured chicken muscle. Cell Motil. Cytoskel., 25: 317-335.
    • (1993) Cell Motil. Cytoskel. , vol.25 , pp. 317-335
    • Schafer, D.A.1    Waddle, J.A.2    Cooper, J.A.3
  • 26
    • 0028891855 scopus 로고
    • Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments
    • SCHAFER, D.A., HUG, C., and COOPER, J.A. 1995. Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments. J. Cell Biol., 128: 61-70.
    • (1995) J. Cell Biol. , vol.128 , pp. 61-70
    • Schafer, D.A.1    Hug, C.2    Cooper, J.A.3
  • 29
    • 0017341538 scopus 로고
    • Polarity of actin filaments at the initial stage of myofibril assembly in myogenic cells in vitro
    • SHIMADA, Y. and OBINATA, T. 1977. Polarity of actin filaments at the initial stage of myofibril assembly in myogenic cells in vitro. J. Cell Biol., 72: 777-785.
    • (1977) J. Cell Biol. , vol.72 , pp. 777-785
    • Shimada, Y.1    Obinata, T.2
  • 30
    • 0028362281 scopus 로고
    • Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: Myofilament lengths
    • SOSA, H., POPP, D., OUYANG, G., and HUXLEY, H. 1994. Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths. Biophys. J., 67: 283-292.
    • (1994) Biophys. J. , vol.67 , pp. 283-292
    • Sosa, H.1    Popp, D.2    Ouyang, G.3    Huxley, H.4
  • 31
    • 0023584384 scopus 로고
    • Immunocytochemical studies of caediac myofibrillogenesis in early chick embryos. II Generation of α-actinin dots within thin spots at the time of the first myofibril formation
    • TOKUYASY, K.T. and MAHER, P.A. 1987. Immunocytochemical studies of caediac myofibrillogenesis in early chick embryos. II Generation of α-actinin dots within thin spots at the time of the first myofibril formation. J. Cell Biol., 105: 2795-2801.
    • (1987) J. Cell Biol. , vol.105 , pp. 2795-2801
    • Tokuyasy, K.T.1    Maher, P.A.2
  • 32
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • TRINICK, J. 1994. Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci., 19: 405-408.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 405-408
    • Trinick, J.1
  • 33
    • 0029949254 scopus 로고    scopus 로고
    • Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin
    • In press
    • TURNACIOGLU, K., MITTAL, B., SANGER, J.M., and SANGER, J.W. 1996. Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin. Cell Motil. Cytosk. In press.
    • (1996) Cell Motil. Cytosk.
    • Turnacioglu, K.1    Mittal, B.2    Sanger, J.M.3    Sanger, J.W.4
  • 34
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggest a set of parallel inextensible nebulin filaments anchored at the Z-line
    • WANG, K. and WRIGHT, J. 1988. Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggest a set of parallel inextensible nebulin filaments anchored at the Z-line. J. Cell Biol., 107: 2199-2212.
    • (1988) J. Cell Biol. , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 35
    • 0015786195 scopus 로고
    • Molecular control mechanisms in muscle contraction
    • WEBER, A. and MURRAY, J.M. 1973. Molecular control mechanisms in muscle contraction. Physiol. Rev., 53: 612-673.
    • (1973) Physiol. Rev. , vol.53 , pp. 612-673
    • Weber, A.1    Murray, J.M.2
  • 36
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • WEBER, A., PENNISE, C.C., BABCOCK, G.G., and FOWLER, V.M. 1994. Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol., 127: 1627-1635.
    • (1994) J. Cell Biol. , vol.127 , pp. 1627-1635
    • Weber, A.1    Pennise, C.C.2    Babcock, G.G.3    Fowler, V.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.