메뉴 건너뛰기




Volumn 13, Issue 4, 1996, Pages 509-517

Differential assembly of cytoskeletal and sarcomeric actins in developing skeletal muscle cells in vitro

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MONOCLONAL ANTIBODY;

EID: 0030208165     PISSN: 02890003     EISSN: None     Source Type: Journal    
DOI: 10.2108/zsj.13.509     Document Type: Article
Times cited : (23)

References (34)
  • 1
    • 0024390193 scopus 로고
    • An actin-depolymerizing protein in embryonic chicken skeletal muscle: Purification and characterization
    • Tokyo
    • Abe H, Obinata T (1989) An actin-depolymerizing protein in embryonic chicken skeletal muscle: Purification and characterization. J Biochem (Tokyo) 106: 172-180
    • (1989) J Biochem , vol.106 , pp. 172-180
    • Abe, H.1    Obinata, T.2
  • 2
    • 0024468554 scopus 로고
    • A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle
    • Tokyo
    • Abe H, Ohshima S, Obinata T (1989) A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle. J Biochem (Tokyo) 106: 696-702
    • (1989) J Biochem , vol.106 , pp. 696-702
    • Abe, H.1    Ohshima, S.2    Obinata, T.3
  • 3
    • 0022549341 scopus 로고
    • Role of stress fiber-like structures in assembling nascent myofibrils in myosheets recovering from exposure to ethylmethanesulfonate
    • Antin PB, Tokunaka S, Nachmias VT, Holtzer H (1986) Role of stress fiber-like structures in assembling nascent myofibrils in myosheets recovering from exposure to ethylmethanesulfonate. J Cell Biol 102: 1464-1479
    • (1986) J Cell Biol , vol.102 , pp. 1464-1479
    • Antin, P.B.1    Tokunaka, S.2    Nachmias, V.T.3    Holtzer, H.4
  • 4
    • 0029615379 scopus 로고
    • Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocytes cytoarchitecture and function
    • Arx PV, Bantle S, Soldati T, and Perriard J-C (1995) Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocytes cytoarchitecture and function. J Cell Biol 131: 1759-1773
    • (1995) J Cell Biol , vol.131 , pp. 1759-1773
    • Arx, P.V.1    Bantle, S.2    Soldati, T.3    Perriard, J.-C.4
  • 5
    • 0020514396 scopus 로고
    • Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies
    • De Blas AL, Cherwinski HM (1983) Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies. Anal Biochem 133: 214-219
    • (1983) Anal Biochem , vol.133 , pp. 214-219
    • De Blas, A.L.1    Cherwinski, H.M.2
  • 6
    • 0021749672 scopus 로고
    • The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes
    • Dlugosz AA, Antin PB, Nachmias VT, Holtzer H (1984) The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes. J Cell Biol 99: 2268-2278
    • (1984) J Cell Biol , vol.99 , pp. 2268-2278
    • Dlugosz, A.A.1    Antin, P.B.2    Nachmias, V.T.3    Holtzer, H.4
  • 7
    • 0017769048 scopus 로고
    • Antibodies to major histocompatibility antigens produced by hybrid cell lines
    • Galfre G, Howe SC, Milstein C, Butcher GW, Howard JC (1977) Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature 266: 550-552
    • (1977) Nature , vol.266 , pp. 550-552
    • Galfre, G.1    Howe, S.C.2    Milstein, C.3    Butcher, G.W.4    Howard, J.C.5
  • 8
    • 0017272548 scopus 로고
    • Identification and characterization of multiple forms of actin
    • Garrels JI, Gibson W (1976) Identification and characterization of multiple forms of actin. Cell 9: 793-805
    • (1976) Cell , vol.9 , pp. 793-805
    • Garrels, J.I.1    Gibson, W.2
  • 9
    • 0017412469 scopus 로고
    • A simple method for polyethylene glycol-promoted fusion of mouse myeloma cells
    • Gefter ML, Margulies DH, Scharff MD (1977) A simple method for polyethylene glycol-promoted fusion of mouse myeloma cells. Somatic Cell Genet 3: 231-236
    • (1977) Somatic Cell Genet , vol.3 , pp. 231-236
    • Gefter, M.L.1    Margulies, D.H.2    Scharff, M.D.3
  • 10
    • 0024593196 scopus 로고
    • Skeletal muscle myofibrillogenesis as revealed with a monoclonal antibody to titin in combination with detection of the α- and γ-isoforms of actin
    • Handel SE, Wang S-M, Greaser ML, Schultz E, Bulinski JC, Lessard JL (1989) Skeletal muscle myofibrillogenesis as revealed with a monoclonal antibody to titin in combination with detection of the α- and γ-isoforms of actin. Dev Biol 132: 35-44
    • (1989) Dev Biol , vol.132 , pp. 35-44
    • Handel, S.E.1    Wang, S.-M.2    Greaser, M.L.3    Schultz, E.4    Bulinski, J.C.5    Lessard, J.L.6
  • 11
    • 0022552715 scopus 로고
    • Sequential expression of chicken actin genes during myogenesis
    • Hayward LJ, Schwartz RJ (1986) Sequential expression of chicken actin genes during myogenesis. J Cell Biol 102: 1485-1493
    • (1986) J Cell Biol , vol.102 , pp. 1485-1493
    • Hayward, L.J.1    Schwartz, R.J.2
  • 12
    • 0016279313 scopus 로고
    • A method of microinjection
    • Hiramoto Y (1974) A method of microinjection. Exp Cell Res 87: 403-406
    • (1974) Exp Cell Res , vol.87 , pp. 403-406
    • Hiramoto, Y.1
  • 13
    • 0020441912 scopus 로고
    • A myotropic protein from chick embryo extract; its purification, identity to transferrin, and indispensability for avian myogenesis
    • Ii I, Kimura I, Ozawa E (1982) A myotropic protein from chick embryo extract; Its purification, identity to transferrin, and indispensability for avian myogenesis. Dev Biol 94: 366-377
    • (1982) Dev Biol , vol.94 , pp. 366-377
    • Ii, I.1    Kimura, I.2    Ozawa, E.3
  • 14
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida K, Matsumoto S, Yahara I (1992) The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct 17: 39-46
    • (1992) Cell Struct Funct , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0023925979 scopus 로고
    • The effect of divalent cations on the interaction between calf spleen profilin and different actins
    • Larsson H, Lindberg U (1984) The effect of divalent cations on the interaction between calf spleen profilin and different actins. Biochim Biophys Acta 953: 95-105
    • (1984) Biochim Biophys Acta , vol.953 , pp. 95-105
    • Larsson, H.1    Lindberg, U.2
  • 17
    • 0019129296 scopus 로고
    • An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
    • Lubit BW, Schwartz JH (1980) An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins. J Cell Biol 86: 891-897
    • (1980) J Cell Biol , vol.86 , pp. 891-897
    • Lubit, B.W.1    Schwartz, J.H.2
  • 18
    • 0029829409 scopus 로고    scopus 로고
    • Quantitative analysis of low molecular weight G-actin-binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles
    • in press
    • Nagaoka R, Minami N, Hayakawa K, Abe H, Obinata T (1996) Quantitative analysis of low molecular weight G-actin-binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles. J Muscle Res Cell Motil 17: in press
    • (1996) J Muscle Res Cell Motil , vol.17
    • Nagaoka, R.1    Minami, N.2    Hayakawa, K.3    Abe, H.4    Obinata, T.5
  • 19
    • 0021358325 scopus 로고
    • Characterization of the action of porcine brain profilin on actin polymerization
    • Nishida E, Maekawa S, Sakai H (1984) Characterization of the action of porcine brain profilin on actin polymerization. J Biochem 95: 399-404
    • (1984) J Biochem , vol.95 , pp. 399-404
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 20
    • 0027263236 scopus 로고
    • Contractile proteins and myofibrillogenesis
    • Obinata T (1993) Contractile proteins and myofibrillogenesis. Int Rev Cytol 143: 153-189
    • (1993) Int Rev Cytol , vol.143 , pp. 153-189
    • Obinata, T.1
  • 21
    • 0024344742 scopus 로고
    • Isolation of profilin from embryonic chicken skeletal muscle and evaluation of its interaction with different actin isoforms
    • Ohshima S, Abe H, Obinata T (1989) Isolation of profilin from embryonic chicken skeletal muscle and evaluation of its interaction with different actin isoforms. J Biochem 105: 855-857
    • (1989) J Biochem , vol.105 , pp. 855-857
    • Ohshima, S.1    Abe, H.2    Obinata, T.3
  • 22
    • 0020967398 scopus 로고
    • Subcellular sorting of isoactins: Selective association of γ-actin with skeletal muscle mitochondria
    • Padro JV, Pittenger MF, Craig SW (1983) Subcellular sorting of isoactins: Selective association of γ-actin with skeletal muscle mitochondria. Cell 32: 1093-1103
    • (1983) Cell , vol.32 , pp. 1093-1103
    • Padro, J.V.1    Pittenger, M.F.2    Craig, S.W.3
  • 23
    • 0021255315 scopus 로고
    • α-cardiac actin is the major sarcomeric isoform expressed in embryonic avian skeletal muscle
    • Paterson BM, Eldridge JD (1984) α-cardiac actin is the major sarcomeric isoform expressed in embryonic avian skeletal muscle. Science 224: 1436-1438
    • (1984) Science , vol.224 , pp. 1436-1438
    • Paterson, B.M.1    Eldridge, J.D.2
  • 24
    • 0019869554 scopus 로고
    • The development of myofibrils in cultured muscle cells: A whole-mount and thin-section electron microscopic study
    • Peng HB, Wolosewick JJ, Vheng P-C (1981) The development of myofibrils in cultured muscle cells: A whole-mount and thin-section electron microscopic study. Dev Biol 88: 122-136
    • (1981) Dev Biol , vol.88 , pp. 122-136
    • Peng, H.B.1    Wolosewick, J.J.2    Vheng, P.-C.3
  • 25
    • 0020024452 scopus 로고
    • Selective isoactin release from cultured embryonic skeletal muscle cells
    • Rubinstein P, RuppertT, Sandra A (1982) Selective isoactin release from cultured embryonic skeletal muscle cells. J Cell Biol 92: 164-169
    • (1982) J Cell Biol , vol.92 , pp. 164-169
    • Rubinstein, P.1    Ruppert, T.2    Sandra, A.3
  • 26
    • 0023912712 scopus 로고
    • Distribution of microtubules and other cytoskeletal filaments during myotube elongation as revealed by fluorescence microscopy
    • Saitoh O, Arai T, Obinata T (1988) Distribution of microtubules and other cytoskeletal filaments during myotube elongation as revealed by fluorescence microscopy. Cell Tissue Res 252: 263-273
    • (1988) Cell Tissue Res , vol.252 , pp. 263-273
    • Saitoh, O.1    Arai, T.2    Obinata, T.3
  • 27
    • 0024836467 scopus 로고
    • Cellular distribution of smooth muscle actins during mammalian embryogenesis: Expression of the α-vascular but not the γ-enteric isoform in differentiatin striated myocytes
    • Sawtell NM, Lessard JL (1989) Cellular distribution of smooth muscle actins during mammalian embryogenesis: Expression of the α-vascular but not the γ-enteric isoform in differentiatin striated myocytes. J Cell Biol 109: 2929-2937
    • (1989) J Cell Biol , vol.109 , pp. 2929-2937
    • Sawtell, N.M.1    Lessard, J.L.2
  • 28
    • 0019874694 scopus 로고
    • Gene switching in myogenesis: Differential expression of the actin multigene family
    • Schwartz RJ, Rothblum KN (1981) Gene switching in myogenesis: Differential expression of the actin multigene family. Biochemistry 20: 4122-4129
    • (1981) Biochemistry , vol.20 , pp. 4122-4129
    • Schwartz, R.J.1    Rothblum, K.N.2
  • 29
    • 0019160373 scopus 로고
    • Presence of three actin types in skeletal muscle of chick embryo
    • Shimizu N, Obinata T (1980) Presence of three actin types in skeletal muscle of chick embryo. Dev Growth Differ 22: 789-796
    • (1980) Dev Growth Differ , vol.22 , pp. 789-796
    • Shimizu, N.1    Obinata, T.2
  • 30
    • 0022580732 scopus 로고
    • Actin concentration and monomerpolymer ratio in developing chicken skeletal muscle
    • Shimizu N, Obinata T (1986) Actin concentration and monomerpolymer ratio in developing chicken skeletal muscle. J Biochem 99: 751-759
    • (1986) J Biochem , vol.99 , pp. 751-759
    • Shimizu, N.1    Obinata, T.2
  • 31
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the tropomyosin-troponin complex with actin and the proteolytic fragment of myosin
    • Spudich JA, Watt S, (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the tropomyosin-troponin complex with actin and the proteolytic fragment of myosin. J Biol Chem 246: 4866-4871
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 32
    • 0019948311 scopus 로고
    • The regulation of actin polymerization and the inhibition of monomer actin ATPase activity by Acanthamoeba castellnii profilin
    • Tobacman LS, Korn E (1983) The regulation of actin polymerization and the inhibition of monomer actin ATPase activity by Acanthamoeba castellnii profilin. J Biol Chem 257: 4166-4170
    • (1983) J Biol Chem , vol.257 , pp. 4166-4170
    • Tobacman, L.S.1    Korn, E.2
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin HT, Stahelin HM, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Stahelin, H.M.2    Gordon, J.3
  • 34
    • 0018276994 scopus 로고
    • At least six different actins are expressed in higher mammals: An analysis based on the amino acid sequence of the amino terminal tryptic peptides
    • Vandekerckhove J, Weber K (1978) At least six different actins are expressed in higher mammals: an analysis based on the amino acid sequence of the amino terminal tryptic peptides. J Mol Biol 126: 783-802
    • (1978) J Mol Biol , vol.126 , pp. 783-802
    • Vandekerckhove, J.1    Weber, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.