메뉴 건너뛰기




Volumn 19, Issue 8, 1998, Pages 937-947

Assembly of force-expressed troponin-I isoforms in myofibrils of cultured cardiac and fast skeletal muscle cells as studied by epitope tagging

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; EPITOPE; MUSCLE PROTEIN; TROPONIN I;

EID: 0032444202     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005473422085     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 0026445344 scopus 로고
    • Contractile protein isoforms in muscle development
    • BANDMAN, E. (1992) Contractile protein isoforms in muscle development. Dev. Biol. 154, 273-83.
    • (1992) Dev. Biol. , vol.154 , pp. 273-283
    • Bandman, E.1
  • 2
    • 0022235739 scopus 로고
    • A single cardiac troponin T gene generates embryonic and adult isoforms via developmentally alternate splicing
    • COOPER, T. A. & ORDAHL, C. P. (1985) A single cardiac troponin T gene generates embryonic and adult isoforms via developmentally alternate splicing. J. Biol. Chem. 260, 11140-48.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11140-11148
    • Cooper, T.A.1    Ordahl, C.P.2
  • 3
    • 0027729269 scopus 로고
    • A novel strategy for the immunological tagging of cDNA constructs
    • CRAVCHIK, A. & MATUS, A. (1993) A novel strategy for the immunological tagging of cDNA constructs. Gene 137, 139-43.
    • (1993) Gene , vol.137 , pp. 139-143
    • Cravchik, A.1    Matus, A.2
  • 4
    • 0014866940 scopus 로고
    • The potassium-sensitivity of isolated embryonic heart cells increases with development
    • DEHAAN, R. L. (1970) The potassium-sensitivity of isolated embryonic heart cells increases with development. Dev. Biol. 23, 226-40.
    • (1970) Dev. Biol. , vol.23 , pp. 226-240
    • Dehaan, R.L.1
  • 5
    • 0019011262 scopus 로고
    • The components of the troponin complex and development in skeletal muscle
    • DHOOT, G. K. & PERRY, V. (1980) The components of the troponin complex and development in skeletal muscle. Exp. Cell Res. 127, 75-87.
    • (1980) Exp. Cell Res. , vol.127 , pp. 75-87
    • Dhoot, G.K.1    Perry, V.2
  • 6
    • 0023857518 scopus 로고
    • Incorporation of fluorescently labeled actin and tropomyosin into muscle cells
    • DOME, J. S., MITTAL, B., POCHAPIN, M. B., SANGER, J. M. & SANGER, J. W. (1988) Incorporation of fluorescently labeled actin and tropomyosin into muscle cells. Cell Differ. 23, 37-52.
    • (1988) Cell Differ. , vol.23 , pp. 37-52
    • Dome, J.S.1    Mittal, B.2    Pochapin, M.B.3    Sanger, J.M.4    Sanger, J.W.5
  • 7
    • 73049137785 scopus 로고
    • Calcium binding activity of vesicular relaxing factor
    • EBASHI, S. (1961) Calcium binding activity of vesicular relaxing factor. J. Biochem. 50, 236-44.
    • (1961) J. Biochem. , vol.50 , pp. 236-244
    • Ebashi, S.1
  • 9
    • 0027236371 scopus 로고
    • The fifth transmembrane segment of the neuromedin B receptor is critical for high affinity neuromedin B binding
    • FATHI, Z., BENYA, R. V., SHAPIRA, H., JANSEN, R. T. & BATTEY, J. F. (1993) The fifth transmembrane segment of the neuromedin B receptor is critical for high affinity neuromedin B binding. J. Biol. Chem. 268, 14622-6.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14622-14626
    • Fathi, Z.1    Benya, R.V.2    Shapira, H.3    Jansen, R.T.4    Battey, J.F.5
  • 10
    • 0027531725 scopus 로고
    • Regional differences in troponin I isoform switching during rat heart development
    • GORZA, L., AUSONI, S., MERCIAI, N., HASTINGS, K. E. M. & SCHIAFFINO, S. (1993) Regional differences in troponin I isoform switching during rat heart development. Dev. Biol. 156, 253-64.
    • (1993) Dev. Biol. , vol.156 , pp. 253-264
    • Gorza, L.1    Ausoni, S.2    Merciai, N.3    Hastings, K.E.M.4    Schiaffino, S.5
  • 11
    • 0029678036 scopus 로고    scopus 로고
    • Cardiac and skeletal muscle troponin I isoform are encoded by a dispersed gene family on mouse chromosomes 1 and 7
    • GUENET, J.-L., GRAVEL, M., HASTINGS, K. E. M. & SCHIAFFINO, S. (1996) Cardiac and skeletal muscle troponin I isoform are encoded by a dispersed gene family on mouse chromosomes 1 and 7. Mamm. Genome 7, 13-15.
    • (1996) Mamm. Genome , vol.7 , pp. 13-15
    • Guenet, J.-L.1    Gravel, M.2    Hastings, K.E.M.3    Schiaffino, S.4
  • 12
    • 0025937290 scopus 로고
    • Structure and developmental expression of troponin I isoforms: cDNA clone analysis of avian troponin I mRNA
    • HASTINGS, K. E., KOPPE, R. I., MARMOR, E., BADER, D., SHIMADA, Y. & TOYOTA, N. (1991) Structure and developmental expression of troponin I isoforms: cDNA clone analysis of avian troponin I mRNA. J. Biol. Chem. 266, 19659-65.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19659-19665
    • Hastings, K.E.1    Koppe, R.I.2    Marmor, E.3    Bader, D.4    Shimada, Y.5    Toyota, N.6
  • 13
    • 0029888297 scopus 로고    scopus 로고
    • Strong evolutionary conservation of broadly expressed protein isoforms in the troponin I gene family and other vertebrate gene families
    • HASTINGS, K. E. M. (1996) Strong evolutionary conservation of broadly expressed protein isoforms in the troponin I gene family and other vertebrate gene families. J. Mol. Evol. 42, 631-40.
    • (1996) J. Mol. Evol. , vol.42 , pp. 631-640
    • Hastings, K.E.M.1
  • 14
    • 0029837673 scopus 로고    scopus 로고
    • The intercompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition
    • KOMIYAMA, M., SOLDATI, T., VON ARX, P. & PERRIARD, J.-P. (1996) The intercompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition. J. Cell Sci. 109, 2089-99.
    • (1996) J. Cell Sci. , vol.109 , pp. 2089-2099
    • Komiyama, M.1    Soldati, T.2    Von Arx, P.3    Perriard, J.-P.4
  • 15
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: Intimations of translational control
    • KOZAK, M. (1991) An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115, 887-903.
    • (1991) J. Cell Biol. , vol.115 , pp. 887-903
    • Kozak, M.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-85.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0025933590 scopus 로고
    • Identification and functional significance of troponin isoforms in neuronal rat heart myofibrils
    • MARTIN, A. F., BALL, K., GAO, L., KUMAR, P. & SALARO, R. J. (1991) Identification and functional significance of troponin isoforms in neuronal rat heart myofibrils. Circ. Res. 69, 1244-52.
    • (1991) Circ. Res. , vol.69 , pp. 1244-1252
    • Martin, A.F.1    Ball, K.2    Gao, L.3    Kumar, P.4    Salaro, R.J.5
  • 18
    • 0022460153 scopus 로고
    • The chicken fast skeletal troponin I gene: Exon organization and sequence
    • NIKOVITS, W., KUNCIO, G. & ORDAHL, C. P. (1986) The chicken fast skeletal troponin I gene: exon organization and sequence. Nucleic Acids Res. 14, 3377-90.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 3377-3390
    • Nikovits, W.1    Kuncio, G.2    Ordahl, C.P.3
  • 19
    • 0023034376 scopus 로고
    • Regulatory and cytoskeletal proteins of vertebrate skeletal muscle
    • OHTSUKI, I., MARUYAMA, K. & EBASHI, S. (1986) Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Protein Chem. 38, 1-67.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 1-67
    • Ohtsuki, I.1    Maruyama, K.2    Ebashi, S.3
  • 20
    • 0027457944 scopus 로고
    • Genetic complementation reveals a novel regulatory role for 3′ untranslated regions in growth and differentiation
    • RASTINEJAD, F. & BLAU, H. M. (1993) Genetic complementation reveals a novel regulatory role for 3′ untranslated regions in growth and differentiation. Cell 72, 903-17.
    • (1993) Cell , vol.72 , pp. 903-917
    • Rastinejad, F.1    Blau, H.M.2
  • 21
    • 0028278854 scopus 로고
    • The premyofibril: Evidence of its role in myofibrillogeneses
    • RHEE, D. R., SANGER, J. M. & SANGER, J. W. (1994) The premyofibril: evidence of its role in myofibrillogeneses. Cell Motil. Cytoskeleton 28, 1-24.
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 1-24
    • Rhee, D.R.1    Sanger, J.M.2    Sanger, J.W.3
  • 22
    • 0024617390 scopus 로고
    • Identification and pattern of expression of a developmental isoform of troponin I in chicken and rat cardiac muscle
    • SABRY, M. A. & DHOOT, G. K. (1989) Identification and pattern of expression of a developmental isoform of troponin I in chicken and rat cardiac muscle. J. Muscle Res. Cell Motil. 10, 85-91.
    • (1989) J. Muscle Res. Cell Motil. , vol.10 , pp. 85-91
    • Sabry, M.A.1    Dhoot, G.K.2
  • 23
    • 0014981638 scopus 로고
    • Electron microscope observations on the fusion of chicken myoblasts in vitro
    • SHIMADA, Y. (1971) Electron microscope observations on the fusion of chicken myoblasts in vitro. J. Cell Biol. 48, 128-42.
    • (1971) J. Cell Biol. , vol.48 , pp. 128-142
    • Shimada, Y.1
  • 24
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • SOLDATI, T. & PERRIARD, J. C. (1991) Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell 66, 277-89.
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.C.2
  • 25
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • SYSKA, H., WILKINSON, J. M. & GRAND, R. J. A. (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J. 153, 375-87.
    • (1976) Biochem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3
  • 26
    • 0019806420 scopus 로고
    • Comparative studies on the inhibitory region of selected species of troponin-I
    • TALBOT, J. A. & HODGE, R. S. (1981) Comparative studies on the inhibitory region of selected species of troponin-I. J. Biol. Chem. 256, 12374-8.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12374-12378
    • Talbot, J.A.1    Hodge, R.S.2
  • 27
    • 0019789647 scopus 로고
    • Differentiation of troponin in cardiac and skeletal muscles in chicken embryos as studied by immunofluorescence
    • TOYOTA, N. & SHIMADA, Y. (1981) Differentiation of troponin in cardiac and skeletal muscles in chicken embryos as studied by immunofluorescence. J. Cell Biol. 91, 487-504.
    • (1981) J. Cell Biol. , vol.91 , pp. 487-504
    • Toyota, N.1    Shimada, Y.2
  • 28
    • 0020747231 scopus 로고
    • Isoform variants of troponin in skeletal and cardiac muscle cells cultured with and without nerves
    • TOYOTA, N. & SHIMADA, Y. (1983) Isoform variants of troponin in skeletal and cardiac muscle cells cultured with and without nerves. Cell 33, 297-304.
    • (1983) Cell , vol.33 , pp. 297-304
    • Toyota, N.1    Shimada, Y.2
  • 29
    • 21944432011 scopus 로고    scopus 로고
    • Force-expression of cardiac troponin I in C2C12 skeletal myoblasts suppresses myoblast fusion and induces actin bundle network formation
    • UZAWA, H., TOYOTA, N., BEGUM, S., MASUDA, Y. & SHIMADA, Y. (1997) Force-expression of cardiac troponin I in C2C12 skeletal myoblasts suppresses myoblast fusion and induces actin bundle network formation. Proc. Japan Acad. Ser. B 73, 215-18.
    • (1997) Proc. Japan Acad. Ser. B , vol.73 , pp. 215-218
    • Uzawa, H.1    Toyota, N.2    Begum, S.3    Masuda, Y.4    Shimada, Y.5
  • 30
    • 0023930339 scopus 로고
    • The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin
    • VAN EYKE, J. E. & HODGES, R. S. (1988) The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin. J. Biol. Chem. 263, 1726-32.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1726-1732
    • Van Eyke, J.E.1    Hodges, R.S.2
  • 31
    • 0017919767 scopus 로고
    • Comparison of amino acid sequence of troponin I from different striated muscles
    • WILKINSON, J. M. & GRAND, R. J. A. (1978) Comparison of amino acid sequence of troponin I from different striated muscles. Nature 271, 31-5.
    • (1978) Nature , vol.271 , pp. 31-35
    • Wilkinson, J.M.1    Grand, R.J.A.2
  • 32
    • 0029031964 scopus 로고
    • Developmental regulation of troponin I isoform genes in striated muscles of transgenic mice
    • ZHU, L., LYONS, G. E., JUHASZ, O., JOYA, J. E., HARDEMAN, E. C. & WADE, R. (1995) Developmental regulation of troponin I isoform genes in striated muscles of transgenic mice. Dev. Biol. 169, 487-503.
    • (1995) Dev. Biol. , vol.169 , pp. 487-503
    • Zhu, L.1    Lyons, G.E.2    Juhasz, O.3    Joya, J.E.4    Hardeman, E.C.5    Wade, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.