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Volumn 144, Issue 2, 2006, Pages 238-244

Expression of thick filament proteins during ontogenesis of the mussel Mytilus trossulus (Mollusca: Bivalvia)

Author keywords

Larva; Mollusc; Mussel; Myogenesis; Myorod; Myosin; Paramyosin; Thick filament; Twitchin

Indexed keywords

ACTIN; MUSCLE PROTEIN; MYOROD; MYOSIN; MYOSIN HEAVY CHAIN; PARAMYOSIN; PROTEIN; TWITCHIN; UNCLASSIFIED DRUG;

EID: 33646510344     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2006.03.002     Document Type: Article
Times cited : (19)

References (44)
  • 2
    • 0031718945 scopus 로고    scopus 로고
    • Regulation of catch muscle by twitchin phosphorylation: effects on force, ATPase, and shortening
    • Butler T.M., Mooers S.U., Li C., Narayan S., and Siegman M.J. Regulation of catch muscle by twitchin phosphorylation: effects on force, ATPase, and shortening. Biophys. J. 75 (1998) 1904-1914
    • (1998) Biophys. J. , vol.75 , pp. 1904-1914
    • Butler, T.M.1    Mooers, S.U.2    Li, C.3    Narayan, S.4    Siegman, M.J.5
  • 4
    • 0042206432 scopus 로고    scopus 로고
    • Twitchin from molluscan catch muscle: primary structure and relationship between site-specific phosphorylation and mechanical function
    • Funabara D., Watabe S., Mooers S.U., Narayan S., Dudas C., Hartshorne D.J., Siegman M.J., and Butler T.M. Twitchin from molluscan catch muscle: primary structure and relationship between site-specific phosphorylation and mechanical function. J. Biol. Chem. 278 (2003) 29308-29316
    • (2003) J. Biol. Chem. , vol.278 , pp. 29308-29316
    • Funabara, D.1    Watabe, S.2    Mooers, S.U.3    Narayan, S.4    Dudas, C.5    Hartshorne, D.J.6    Siegman, M.J.7    Butler, T.M.8
  • 6
    • 0024348057 scopus 로고
    • Myogenesis in the mouse embryo: differential onset of expression of myogenic protein and the involvement of titin in myofibril assembly
    • Fürst D.O., Osborn M., and Weber K. Myogenesis in the mouse embryo: differential onset of expression of myogenic protein and the involvement of titin in myofibril assembly. J. Cell Biol. 109 (1989) 517-527
    • (1989) J. Cell Biol. , vol.109 , pp. 517-527
    • Fürst, D.O.1    Osborn, M.2    Weber, K.3
  • 7
    • 0017189110 scopus 로고
    • Paramyosin in invertebrate muscles
    • Elfvin M., Levine R., and Dewey M. Paramyosin in invertebrate muscles. J. Cell Biol. 71 (1976) 261-272
    • (1976) J. Cell Biol. , vol.71 , pp. 261-272
    • Elfvin, M.1    Levine, R.2    Dewey, M.3
  • 8
    • 0016227844 scopus 로고
    • The arrangement of myosin on the surface of paramyosin filaments in the white adductor muscle of Crassostrea angulata
    • Elliott A. The arrangement of myosin on the surface of paramyosin filaments in the white adductor muscle of Crassostrea angulata. Proc. R. Soc. Lond. 186B (1974) 53-66
    • (1974) Proc. R. Soc. Lond. , vol.186 B , pp. 53-66
    • Elliott, A.1
  • 9
    • 0022476931 scopus 로고
    • Monoclonal antibodies distinguish titins from heart and skeletal muscle
    • Hill C., and Weber K. Monoclonal antibodies distinguish titins from heart and skeletal muscle. J. Cell Biol. 102 (1986) 1099-1108
    • (1986) J. Cell Biol. , vol.102 , pp. 1099-1108
    • Hill, C.1    Weber, K.2
  • 10
    • 0025117599 scopus 로고
    • Modulation of muscle gene expression in Caenorhabditis elegans: differential levels of transcripts, mRNAs, and polypeptides for thick filament proteins during nematode development
    • Honda S., and Epstein H.F. Modulation of muscle gene expression in Caenorhabditis elegans: differential levels of transcripts, mRNAs, and polypeptides for thick filament proteins during nematode development. Cell Biol. 87 (1990) 876-880
    • (1990) Cell Biol. , vol.87 , pp. 876-880
    • Honda, S.1    Epstein, H.F.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly the head of bacteriophage T4. Nature 227 (1970) 680-682
    • (1970) Nature , vol.227 , pp. 680-682
    • Laemmli, U.K.1
  • 12
    • 0017091125 scopus 로고
    • Paramyosin in invertebrate muscles. II. Content in relation to structure and function
    • Levine R., Elfvin M., Dewey M.M., and Walcott B. Paramyosin in invertebrate muscles. II. Content in relation to structure and function. J. Cell Biol. 71 (1976) 273-279
    • (1976) J. Cell Biol. , vol.71 , pp. 273-279
    • Levine, R.1    Elfvin, M.2    Dewey, M.M.3    Walcott, B.4
  • 13
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle
    • Linke W.A. Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol. Histopathol. 15 (2000) 799-811
    • (2000) Histol. Histopathol. , vol.15 , pp. 799-811
    • Linke, W.A.1
  • 14
    • 0037451223 scopus 로고    scopus 로고
    • Drosophila paramyosin is important for myoblast fusion and essential for myofibril formation
    • Liu H., Mardahl-Dumesnil M., Sweeney S.T., O'Kane C.J., and Bernstein S.I. Drosophila paramyosin is important for myoblast fusion and essential for myofibril formation. J. Cell Biol. 160 (2003) 899-908
    • (2003) J. Cell Biol. , vol.160 , pp. 899-908
    • Liu, H.1    Mardahl-Dumesnil, M.2    Sweeney, S.T.3    O'Kane, C.J.4    Bernstein, S.I.5
  • 15
    • 0002632822 scopus 로고
    • Embryonic and early larval development of Mytilus edulis (Bivalvia)
    • (in Russian)
    • Malakhov V.V., and Medvedeva L.A. Embryonic and early larval development of Mytilus edulis (Bivalvia). Zool. J. 64 (1985) 1808-1815 (in Russian)
    • (1985) Zool. J. , vol.64 , pp. 1808-1815
    • Malakhov, V.V.1    Medvedeva, L.A.2
  • 16
    • 0018681449 scopus 로고
    • Major myofibrillar protein content and the structure of molluscs adductor contractile apparatus
    • Margulis B.A., Bobrova I.F., Mashanski V.F., and Pinaev G.P. Major myofibrillar protein content and the structure of molluscs adductor contractile apparatus. Comp. Biochem. Physiol., A 64 (1979) 291-298
    • (1979) Comp. Biochem. Physiol., A , vol.64 , pp. 291-298
    • Margulis, B.A.1    Bobrova, I.F.2    Mashanski, V.F.3    Pinaev, G.P.4
  • 17
    • 0033692585 scopus 로고    scopus 로고
    • Isolation and partial characterization of myogenic cells from mussel larvae in vitro
    • Odintsova N.A., Plotnikov S.V., and Karpenko A.A. Isolation and partial characterization of myogenic cells from mussel larvae in vitro. Tissue Cell 32 (2000) 417-424
    • (2000) Tissue Cell , vol.32 , pp. 417-424
    • Odintsova, N.A.1    Plotnikov, S.V.2    Karpenko, A.A.3
  • 18
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee J.D., and Spudich J. Purification of muscle actin. Meths Enzymol. 85 B (1982) 164-181
    • (1982) Meths Enzymol. , vol.85 B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.2
  • 19
    • 0142056122 scopus 로고    scopus 로고
    • Comparative characteristic of Mytilus muscle cells developed in vitro and in vivo
    • Plotnikov S.V., Karpenko A.A., and Odintsova N.A. Comparative characteristic of Mytilus muscle cells developed in vitro and in vivo. J. Exp. Zool. 298 A (2003) 77-85
    • (2003) J. Exp. Zool. , vol.298 A , pp. 77-85
    • Plotnikov, S.V.1    Karpenko, A.A.2    Odintsova, N.A.3
  • 20
    • 0014981534 scopus 로고
    • Smooth muscle tone
    • Ruegg J.C. Smooth muscle tone. Physiol. Rev. 51 (1971) 201-248
    • (1971) Physiol. Rev. , vol.51 , pp. 201-248
    • Ruegg, J.C.1
  • 21
    • 0007133684 scopus 로고
    • Myosin-actin weight ratio in phasic and tonic parts of scallop adductor
    • Shelud'ko N.S., and Preminger N.K. Myosin-actin weight ratio in phasic and tonic parts of scallop adductor. Comp. Biochem. Physiol., A 93 (1989) 327-330
    • (1989) Comp. Biochem. Physiol., A , vol.93 , pp. 327-330
    • Shelud'ko, N.S.1    Preminger, N.K.2
  • 23
    • 0034846822 scopus 로고    scopus 로고
    • Myorod, a thick filament protein of molluscan smooth muscle: isolation, polymerization and interaction with myosin
    • Shelud'ko N.S., Permyakova T.V., Tuturova K.Ph., Neverkina O., and Drozdov A. Myorod, a thick filament protein of molluscan smooth muscle: isolation, polymerization and interaction with myosin. J. Muscle Res. Cell Motil. 22 (2001) 91-100
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 91-100
    • Shelud'ko, N.S.1    Permyakova, T.V.2    Tuturova, K.Ph.3    Neverkina, O.4    Drozdov, A.5
  • 25
    • 7944233936 scopus 로고    scopus 로고
    • Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way
    • Shelud'ko N.S., Matusovskaya G.G., Permyakova T.V., and Matusovsky O.S. Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way. Arch. Biochem. Biophys. 423 (2004) 269-277
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 269-277
    • Shelud'ko, N.S.1    Matusovskaya, G.G.2    Permyakova, T.V.3    Matusovsky, O.S.4
  • 27
    • 0032574850 scopus 로고    scopus 로고
    • Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle
    • Siegman M.J., Funabara D., Kinoshita S., Watabe S., Hartshorne D.J., and Butler T.M. Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5383-5388
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5383-5388
    • Siegman, M.J.1    Funabara, D.2    Kinoshita, S.3    Watabe, S.4    Hartshorne, D.J.5    Butler, T.M.6
  • 29
    • 0009482260 scopus 로고
    • Electroforetic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Gordon J., and Staehelin T. Electroforetic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Gordon, J.2    Staehelin, T.3
  • 30
    • 0015880246 scopus 로고
    • Myosin content and filament structure in smooth and striated muscle
    • Treager R.T., and Squire J.M. Myosin content and filament structure in smooth and striated muscle. J. Mol. Biol. 77 (1973) 279-290
    • (1973) J. Mol. Biol. , vol.77 , pp. 279-290
    • Treager, R.T.1    Squire, J.M.2
  • 31
    • 33646520500 scopus 로고    scopus 로고
    • Role of titin in muscle regulation
    • Tskhovrebova L., and Trinick J. Role of titin in muscle regulation. Biophys. J. 82 (2002) 400a
    • (2002) Biophys. J. , vol.82
    • Tskhovrebova, L.1    Trinick, J.2
  • 34
    • 0027748233 scopus 로고
    • Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity
    • Vibert P., Edelstein S.M., Castellani L., and Elliott B.W. Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity. J. Muscle Res. Cell Motil. 14 (1993) 598-607
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 598-607
    • Vibert, P.1    Edelstein, S.M.2    Castellani, L.3    Elliott, B.W.4
  • 35
    • 0025866071 scopus 로고
    • Identification and characterization of Drosophila melanogaster paramyosin
    • Vinós J., Domingo A., Marco R., and Cervera M. Identification and characterization of Drosophila melanogaster paramyosin. J. Mol. Biol. 220 (1991) 687-700
    • (1991) J. Mol. Biol. , vol.220 , pp. 687-700
    • Vinós, J.1    Domingo, A.2    Marco, R.3    Cervera, M.4
  • 36
    • 0036006737 scopus 로고    scopus 로고
    • Chiton myogenesis: perspectives for the development and evolution of larval and adult muscle systems in molluscs
    • Wanninger A., and Haszprunar G. Chiton myogenesis: perspectives for the development and evolution of larval and adult muscle systems in molluscs. J. Morphol. 251 (2002) 103-113
    • (2002) J. Morphol. , vol.251 , pp. 103-113
    • Wanninger, A.1    Haszprunar, G.2
  • 37
    • 0036792922 scopus 로고    scopus 로고
    • Muscle development in Antalis entalis (Mollusca, Scaphopoda) and its significance for scaphopod relationships
    • Wanninger A., and Haszprunar G. Muscle development in Antalis entalis (Mollusca, Scaphopoda) and its significance for scaphopod relationships. J. Morphol. 254 (2002) 53-64
    • (2002) J. Morphol. , vol.254 , pp. 53-64
    • Wanninger, A.1    Haszprunar, G.2
  • 39
    • 0017202707 scopus 로고
    • Comparative studies of paramyosins
    • Winkelman L. Comparative studies of paramyosins. Comp. Biochem. Physiol., B 55 (1976) 391-397
    • (1976) Comp. Biochem. Physiol., B , vol.55 , pp. 391-397
    • Winkelman, L.1
  • 40
    • 0038120894 scopus 로고    scopus 로고
    • The pathway of myofibrillogenesis determines the interrelationship between myosin and paramyosin synthesis in Caenorhabditis elegans
    • White G.E., Petry C.M., and Schachat F. The pathway of myofibrillogenesis determines the interrelationship between myosin and paramyosin synthesis in Caenorhabditis elegans. J. Exp. Biol. 206 (2003) 1899-1906
    • (2003) J. Exp. Biol. , vol.206 , pp. 1899-1906
    • White, G.E.1    Petry, C.M.2    Schachat, F.3
  • 41
    • 0030805052 scopus 로고    scopus 로고
    • Bi-directional movement of actin filaments along long bipolar tracks of oriented rabbit skeletal muscle myosin molecules
    • Yamada A., Yoshio M., and Nakayama H. Bi-directional movement of actin filaments along long bipolar tracks of oriented rabbit skeletal muscle myosin molecules. FEBS Letts. 409 (1997) 380-384
    • (1997) FEBS Letts. , vol.409 , pp. 380-384
    • Yamada, A.1    Yoshio, M.2    Nakayama, H.3
  • 42
    • 0034645728 scopus 로고    scopus 로고
    • Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene
    • Yamada A., Yoshio M., Oiwa K., and Nyitray L. Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene. J. Mol. Biol. 295 (2000) 169-178
    • (2000) J. Mol. Biol. , vol.295 , pp. 169-178
    • Yamada, A.1    Yoshio, M.2    Oiwa, K.3    Nyitray, L.4
  • 43
    • 0035811060 scopus 로고    scopus 로고
    • An in vitro assay reveals essential protein components for the 'catch' state of invertebrate smooth muscle
    • Yamada A., Yoshio M., Kojima H., and Oiwa K. An in vitro assay reveals essential protein components for the 'catch' state of invertebrate smooth muscle. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 6635-6640
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6635-6640
    • Yamada, A.1    Yoshio, M.2    Kojima, H.3    Oiwa, K.4
  • 44
    • 0033824709 scopus 로고    scopus 로고
    • Drosophila D-titin is required for myoblast fusion and skeletal muscle striation
    • Zhang Y., Featherstone D., Davis W., Rushton E., and Broadie K. Drosophila D-titin is required for myoblast fusion and skeletal muscle striation. J. Cell Sci. 113 (2000) 3103-3115
    • (2000) J. Cell Sci. , vol.113 , pp. 3103-3115
    • Zhang, Y.1    Featherstone, D.2    Davis, W.3    Rushton, E.4    Broadie, K.5


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