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Volumn 62, Issue 4, 2003, Pages 774-792

Expression of myofibrillar proteins and parvalbumin isoforms in white muscle of dorada during development

Author keywords

Brycon moorei; Development; Fish; Muscle; Myofibrillar proteins; Parvalbumin isoforms

Indexed keywords

GENE EXPRESSION;

EID: 0038120739     PISSN: 00221112     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1095-8649.2003.00064.x     Document Type: Article
Times cited : (10)

References (47)
  • 1
    • 0001296127 scopus 로고
    • Myotomal muscle function at different locations in the body of a swimming fish
    • Altringham, J. D., Wardle, C. S. & Smith, C. I. (1993). Myotomal muscle function at different locations in the body of a swimming fish. Journal of Experimental Biology 182, 191-206.
    • (1993) Journal of Experimental Biology , vol.182 , pp. 191-206
    • Altringham, J.D.1    Wardle, C.S.2    Smith, C.I.3
  • 2
    • 0037030568 scopus 로고    scopus 로고
    • Dynamics of intracohort cannibalism in cultured fish
    • Baras, E. & Jobling, M. (2002). Dynamics of intracohort cannibalism in cultured fish. Aquaculture Research 33, 461-479.
    • (2002) Aquaculture Research , vol.33 , pp. 461-479
    • Baras, E.1    Jobling, M.2
  • 3
    • 0033784590 scopus 로고    scopus 로고
    • Sibling cannibalism in dorada under experimental conditions. I. Ontogeny, dynamics, bioenergetics of cannibalism and prey size selectivity
    • doi:10.1006/jfbi.2000.1366
    • Baras, E., Ndao, M., Maxi, M. Y. J., Jeandrain, D., Thomé, J. P., Vandewalle, P. & Mélard, C. (2000). Sibling cannibalism in dorada under experimental conditions. I. Ontogeny, dynamics, bioenergetics of cannibalism and prey size selectivity. Journal of Fish Biology 57, 1001-1020. doi: 10.1006/jfbi.2000.1366.
    • (2000) Journal of Fish Biology , vol.57 , pp. 1001-1020
    • Baras, E.1    Ndao, M.2    Maxi, M.Y.J.3    Jeandrain, D.4    Thomé, J.P.5    Vandewalle, P.6    Mélard, C.7
  • 4
    • 0022426735 scopus 로고
    • The myosin alkali light chain proteins and their genes
    • Barton, P. J. R. & Buckingham, M. E. (1985). The myosin alkali light chain proteins and their genes. Biochemical Journal 231, 249-261.
    • (1985) Biochemical Journal , vol.231 , pp. 249-261
    • Barton, P.J.R.1    Buckingham, M.E.2
  • 5
    • 2342624398 scopus 로고
    • Myosin isoforms in white, red and pink muscles of the teleost sea bass (Dicentrarchus labrax, L.)
    • Bassani, V. & Dalla Libera, L. (1991). Myosin isoforms in white, red and pink muscles of the teleost sea bass (Dicentrarchus labrax, L.). Basic and Applied Myology 1, 153-156.
    • (1991) Basic and Applied Myology , vol.1 , pp. 153-156
    • Bassani, V.1    Dalla Libera, L.2
  • 6
    • 77956847788 scopus 로고
    • Locomotor muscle
    • Hoar, W. S. & Randall, D. J., eds, . New York: Academic Press
    • Bone, Q. (1978). Locomotor muscle. In Fish Physiology, Vol. 7 (Hoar, W. S. & Randall, D. J., eds), pp. 361-424. New York: Academic Press.
    • (1978) Fish Physiology , vol.7 , pp. 361-424
    • Bone, Q.1
  • 7
    • 0000044945 scopus 로고
    • Influence of development and rearing temperature on the distribution, ultrastructure and myosin sub-unit composition of myotomal muscle-fibre types in the plaice Pleuronectes platessa
    • Brooks, S. & Johnston, I. A. (1993). Influence of development and rearing temperature on the distribution, ultrastructure and myosin sub-unit composition of myotomal muscle-fibre types in the plaice Pleuronectes platessa. Marine Biology 117, 501-513.
    • (1993) Marine Biology , vol.117 , pp. 501-513
    • Brooks, S.1    Johnston, I.A.2
  • 8
    • 0031430398 scopus 로고    scopus 로고
    • Isoform distribution of parvalbumins and of some myofibrillar proteins in adult and developing Chrysichthys auratus (Geoffroy St Hilaire, 1808) (Pisces, Claroteidae)
    • Chikou, A., Huriaux, F., Laleye, P., Vandewalle, P. & Focant, B. (1997). Isoform distribution of parvalbumins and of some myofibrillar proteins in adult and developing Chrysichthys auratus (Geoffroy St Hilaire, 1808) (Pisces, Claroteidae). Archives of Physiology and Biochemistry 105, 611-617.
    • (1997) Archives of Physiology and Biochemistry , vol.105 , pp. 611-617
    • Chikou, A.1    Huriaux, F.2    Laleye, P.3    Vandewalle, P.4    Focant, B.5
  • 9
    • 33751138851 scopus 로고
    • Developmental changes in the composition of myofibrillar proteins in the swimming muscles of Atlantic herring, Clupea harengus
    • Crockford, T. & Johnston, I. A. (1993). Developmental changes in the composition of myofibrillar proteins in the swimming muscles of Atlantic herring, Clupea harengus. Marine Biology 115, 15-22.
    • (1993) Marine Biology , vol.115 , pp. 15-22
    • Crockford, T.1    Johnston, I.A.2
  • 11
    • 0000210470 scopus 로고
    • Muscle fibers in rostral and caudal myotomes of the Atlantic cod (Gadus morhua L.) have different mechanical properties
    • Davies, M. L. F., Johnston, I. A. & van de Wal, J. (1995). Muscle fibers in rostral and caudal myotomes of the Atlantic cod (Gadus morhua L.) have different mechanical properties. Physiological Zoology 68, 673-697.
    • (1995) Physiological Zoology , vol.68 , pp. 673-697
    • Davies, M.L.F.1    Johnston, I.A.2    Van De Wal, J.3
  • 13
    • 0000623058 scopus 로고
    • Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development
    • Focant, B., Huriaux, F., Vandewalle, P., Castelli, M. & Goessens, G. (1992). Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development. Fish Physiology and Biochemistry 10, 133-143.
    • (1992) Fish Physiology and Biochemistry , vol.10 , pp. 133-143
    • Focant, B.1    Huriaux, F.2    Vandewalle, P.3    Castelli, M.4    Goessens, G.5
  • 15
    • 0033119870 scopus 로고    scopus 로고
    • Muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus: Isolation, characterisation and expression during development
    • Focant, B., Mélot, F., Collin, S., Chikou, A., Vandewalle, P. & Huriaux, F. (1999). Muscle parvalbumin isoforms of Clarias gariepinus, Heterobranchus longifilis and Chrysichthys auratus: isolation, characterisation and expression during development. Journal of Fish Biology 54, 832-851.
    • (1999) Journal of Fish Biology , vol.54 , pp. 832-851
    • Focant, B.1    Mélot, F.2    Collin, S.3    Chikou, A.4    Vandewalle, P.5    Huriaux, F.6
  • 16
    • 0009567828 scopus 로고    scopus 로고
    • Expression of myofibrillar proteins and parvalbumin isoforms in white muscle of the developing turbot Scophthalmus maximus (Pisces, Pleuronectiformes)
    • Focant, B., Collin, S., Vandewalle, P. & Huriaux, F. (2000). Expression of myofibrillar proteins and parvalbumin isoforms in white muscle of the developing turbot Scophthalmus maximus (Pisces, Pleuronectiformes). Basic and Applied Myology 10, 269-278.
    • (2000) Basic and Applied Myology , vol.10 , pp. 269-278
    • Focant, B.1    Collin, S.2    Vandewalle, P.3    Huriaux, F.4
  • 17
    • 0020034479 scopus 로고
    • Soluble calcium-binding proteins from fish and invertebrate muscle
    • Gerday, C. (1982). Soluble calcium-binding proteins from fish and invertebrate muscle. Molecular Physiology 2, 63-87.
    • (1982) Molecular Physiology , vol.2 , pp. 63-87
    • Gerday, C.1
  • 18
    • 0018539233 scopus 로고
    • Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins
    • Goodman, M., Pechère, J. F., Haiech, J. & Demaille, J. (1979). Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. Journal of Molecular Evolution 13, 331-352.
    • (1979) Journal of Molecular Evolution , vol.13 , pp. 331-352
    • Goodman, M.1    Pechère, J.F.2    Haiech, J.3    Demaille, J.4
  • 19
    • 0031080284 scopus 로고    scopus 로고
    • The two essential light chains of carp fast skeletal myosin, LC1 and LC3, are encoded by distinct genes and change their molar ratio following temperature acclimation
    • Hirayama, Y., Kanoh, S., Nakaya, M. & Watabe, S. (1997). The two essential light chains of carp fast skeletal myosin, LC1 and LC3, are encoded by distinct genes and change their molar ratio following temperature acclimation. Journal of Experimental Biology 200, 693-701.
    • (1997) Journal of Experimental Biology , vol.200 , pp. 693-701
    • Hirayama, Y.1    Kanoh, S.2    Nakaya, M.3    Watabe, S.4
  • 20
    • 0022295295 scopus 로고
    • Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes
    • Huriaux, F. & Focant, B. (1985). Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes. Comparative Biochemistry and Physiology 82B, 737-743.
    • (1985) Comparative Biochemistry and Physiology , vol.82 B , pp. 737-743
    • Huriaux, F.1    Focant, B.2
  • 21
    • 0025259979 scopus 로고
    • Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel (Barbus barbus) populations
    • Huriaux, F., Vandewalle, P., Philippart, J. C. & Focant, B. (1990). Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel (Barbus barbus) populations. Comparative Biochemistry and Physiology 97B, 547-553.
    • (1990) Comparative Biochemistry and Physiology , vol.97 B , pp. 547-553
    • Huriaux, F.1    Vandewalle, P.2    Philippart, J.C.3    Focant, B.4
  • 22
    • 0026093788 scopus 로고
    • Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.)
    • Huriaux, F., Vandewalle, P. & Focant, B. (1991). Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.). Comparative Biochemistry and Physiology 100B, 309-312.
    • (1991) Comparative Biochemistry and Physiology , vol.100 B , pp. 309-312
    • Huriaux, F.1    Vandewalle, P.2    Focant, B.3
  • 23
    • 0029915173 scopus 로고    scopus 로고
    • Parvalbumin isotypes in white muscle from three teleost fish: Characterization and their expression during development
    • Huriaux, F., Mélot, F., Vandewalle, P., Collin, S. & Focant, B. (1996). Parvalbumin isotypes in white muscle from three teleost fish: characterization and their expression during development. Comparative Biochemistry and Physiology 113B, 475-484.
    • (1996) Comparative Biochemistry and Physiology , vol.113 B , pp. 475-484
    • Huriaux, F.1    Mélot, F.2    Vandewalle, P.3    Collin, S.4    Focant, B.5
  • 24
    • 0031128292 scopus 로고    scopus 로고
    • Characterization of parvalbumin isotypes in white muscle from the barbel and expression during development
    • Huriaux, F., Collin, S., Vandewalle, P., Philippart, J. C. & Focant, B. (1997). Characterization of parvalbumin isotypes in white muscle from the barbel and expression during development. Journal of Fish Biology 50, 821-836.
    • (1997) Journal of Fish Biology , vol.50 , pp. 821-836
    • Huriaux, F.1    Collin, S.2    Vandewalle, P.3    Philippart, J.C.4    Focant, B.5
  • 25
    • 0037783116 scopus 로고    scopus 로고
    • Myofibrillar proteins in white muscle of the developing African catfish Heterobranchus longifilis (Siluriformes, Clariidae)
    • Huriaux, F., Vandewalle, P., Baras, E., Legendre, M. & Focant, B. (1999). Myofibrillar proteins in white muscle of the developing African catfish Heterobranchus longifilis (Siluriformes, Clariidae). Fish Physiology and Biochemistry 21, 287-301.
    • (1999) Fish Physiology and Biochemistry , vol.21 , pp. 287-301
    • Huriaux, F.1    Vandewalle, P.2    Baras, E.3    Legendre, M.4    Focant, B.5
  • 26
    • 0031924001 scopus 로고    scopus 로고
    • Scaling of intrinsic contractile properties and myofibrillar protein composition of fast muscle in the fish Myoxocephalus scorpius L.
    • James, R. S., Cole, N. J., Davies, M. L. F. & Johnston, I. A. (1998). Scaling of intrinsic contractile properties and myofibrillar protein composition of fast muscle in the fish Myoxocephalus scorpius L. Journal of Experimental Biology 201, 901-912.
    • (1998) Journal of Experimental Biology , vol.201 , pp. 901-912
    • James, R.S.1    Cole, N.J.2    Davies, M.L.F.3    Johnston, I.A.4
  • 28
  • 29
    • 0031920959 scopus 로고    scopus 로고
    • Embryonic temperature modulates muscle growth characteristics in larval and juvenile herring
    • Johnston, I. A., Cole, N. J., Abercromby, M. & Viera, V. L. A. (1998). Embryonic temperature modulates muscle growth characteristics in larval and juvenile herring. Journal of Experimental Biology 201, 623-646.
    • (1998) Journal of Experimental Biology , vol.201 , pp. 623-646
    • Johnston, I.A.1    Cole, N.J.2    Abercromby, M.3    Viera, V.L.A.4
  • 30
    • 0027515444 scopus 로고
    • Diversity of native myosin and myosin heavy chain in fish skeletal muscles
    • Karasinski, J. (1993). Diversity of native myosin and myosin heavy chain in fish skeletal muscles. Comparative Biochemistry and Physiology 106B, 1041-1047.
    • (1993) Comparative Biochemistry and Physiology , vol.106 B , pp. 1041-1047
    • Karasinski, J.1
  • 31
    • 0039640978 scopus 로고
    • Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, Fish)
    • Karasinski, J. & Kilarski, W. (1989). Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, Fish). Comparative Biochemistry and Physiology 92B, 727-731.
    • (1989) Comparative Biochemistry and Physiology , vol.92 B , pp. 727-731
    • Karasinski, J.1    Kilarski, W.2
  • 33
    • 0028013468 scopus 로고
    • Myofibrillar proteins in developing white muscle of the Arctic charr, Salvelinus alpinus (L.)
    • Martinez, I. & Christiansen, J. S. (1994). Myofibrillar proteins in developing white muscle of the Arctic charr, Salvelinus alpinus (L.). Comparative Biochemistry and Physiology 107B, 11-20.
    • (1994) Comparative Biochemistry and Physiology , vol.107 B , pp. 11-20
    • Martinez, I.1    Christiansen, J.S.2
  • 35
    • 0025969515 scopus 로고
    • Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle
    • Martinez, I., Christiansen, J. S., Ofstad, R. & Olsen, R. L. (1991). Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle. European Journal of Biochemistry 195, 743-753.
    • (1991) European Journal of Biochemistry , vol.195 , pp. 743-753
    • Martinez, I.1    Christiansen, J.S.2    Ofstad, R.3    Olsen, R.L.4
  • 36
    • 0027496841 scopus 로고
    • Myofibrillar proteins in skeletal muscles of parr, smolt and adult Atlantic salmon (Salmo salar L.). Comparison with another salmonid, the Arctic charr Salvelinus alpinus (L.)
    • Martinez, I., Bang, B., Hatlen, B. & Blix, P. (1993). Myofibrillar proteins in skeletal muscles of parr, smolt and adult Atlantic salmon (Salmo salar L.). Comparison with another salmonid, the Arctic charr Salvelinus alpinus (L.). Comparative Biochemistry and Physiology 106B, 1021-1028.
    • (1993) Comparative Biochemistry and Physiology , vol.106 B , pp. 1021-1028
    • Martinez, I.1    Bang, B.2    Hatlen, B.3    Blix, P.4
  • 37
    • 2642543909 scopus 로고
    • Varied expression of myosin alkali light chains is associated with altered speed of contraction in rabbit fast twitch skeletal muscles
    • Pette, D., ed., Berlin: de Gruyter
    • Moss, R. L., Reiser, P. J., Greaser, M. L. & Eddinger, T. J. (1990). Varied expression of myosin alkali light chains is associated with altered speed of contraction in rabbit fast twitch skeletal muscles. In The Dynamic State of Muscle Fibers (Pette, D., ed.), pp. 355-368. Berlin: de Gruyter.
    • (1990) The Dynamic State of Muscle Fibers , pp. 355-368
    • Moss, R.L.1    Reiser, P.J.2    Greaser, M.L.3    Eddinger, T.J.4
  • 38
    • 0022345897 scopus 로고
    • Comparative study of myosins present in the lateral muscle of some fish: Species variations in myosin isoforms and their distribution in red, pink and white muscle
    • Rowlerson, A., Scapolo, P. A., Mascarello, F., Carpenè, E. & Veggetti, A. (1985). Comparative study of myosins present in the lateral muscle of some fish: species variations in myosin isoforms and their distribution in red, pink and white muscle. Journal of Muscle Research and Cell Motility 6, 601-640.
    • (1985) Journal of Muscle Research and Cell Motility , vol.6 , pp. 601-640
    • Rowlerson, A.1    Scapolo, P.A.2    Mascarello, F.3    Carpenè, E.4    Veggetti, A.5
  • 39
    • 0023741330 scopus 로고
    • Developmental transitions of myosin isoforms and organisation of the lateral muscle in the teleost Dicentrarchus labrax (L.)
    • Scapolo, P. A., Veggetti, A., Mascarello, F. & Romanello, M. G. (1988). Developmental transitions of myosin isoforms and organisation of the lateral muscle in the teleost Dicentrarchus labrax (L.). Anatomy and Embryology 178, 287-295.
    • (1988) Anatomy and Embryology , vol.178 , pp. 287-295
    • Scapolo, P.A.1    Veggetti, A.2    Mascarello, F.3    Romanello, M.G.4
  • 40
    • 0023905464 scopus 로고
    • Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers
    • Sweeney, H. L., Kushmerick, M. J., Mabuchi, K., Sréter, F. A. & Gergely, J. (1988). Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. Journal of Biological Chemistry 263, 9034-9039.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 9034-9039
    • Sweeney, H.L.1    Kushmerick, M.J.2    Mabuchi, K.3    Sréter, F.A.4    Gergely, J.5
  • 41
    • 0035962740 scopus 로고    scopus 로고
    • Developmental program expression of myosin alkali light chain and skeletal actin genes in the rainbow trout Oncorhynchus mykiss
    • Thiébaud, P., Rescan, P. Y., Barillot, W., Rallière, C. & Thézé, N. (2001). Developmental program expression of myosin alkali light chain and skeletal actin genes in the rainbow trout Oncorhynchus mykiss. Biochimica et Biophysica Acta 1519, 139-142.
    • (2001) Biochimica et Biophysica Acta , vol.1519 , pp. 139-142
    • Thiébaud, P.1    Rescan, P.Y.2    Barillot, W.3    Rallière, C.4    Thézé, N.5
  • 42
    • 0032213879 scopus 로고    scopus 로고
    • Rostral-caudal variation in troponin T and parvalbumin correlates with differences in relaxation rates of cod axial muscle
    • Thys, T. M., Blank, J. M. & Schachat, F. H. (1998). Rostral-caudal variation in troponin T and parvalbumin correlates with differences in relaxation rates of cod axial muscle. Journal of Experimental Biology 201, 2993-3001.
    • (1998) Journal of Experimental Biology , vol.201 , pp. 2993-3001
    • Thys, T.M.1    Blank, J.M.2    Schachat, F.H.3
  • 43
    • 0035746141 scopus 로고    scopus 로고
    • Longitudinal variation in muscle protein expression and contraction kinetics of largemouth bass axial muscle
    • Thys, T. M., Blank, J. M., Coughlin, D. J. & Schachat, F. (2001). Longitudinal variation in muscle protein expression and contraction kinetics of largemouth bass axial muscle. Journal of Experimental Biology 204, 4249-4257.
    • (2001) Journal of Experimental Biology , vol.204 , pp. 4249-4257
    • Thys, T.M.1    Blank, J.M.2    Coughlin, D.J.3    Schachat, F.4
  • 44
    • 0021659767 scopus 로고
    • Chordate muscle actins differ distinctly from invertebrate muscle actins. The evolution of the different vertebrate muscle actins
    • Vandekerckhove, J. & Weber, K. (1984). Chordate muscle actins differ distinctly from invertebrate muscle actins. The evolution of the different vertebrate muscle actins. Journal of Molecular Biology 179, 391-413.
    • (1984) Journal of Molecular Biology , vol.179 , pp. 391-413
    • Vandekerckhove, J.1    Weber, K.2
  • 45
    • 0001214914 scopus 로고
    • Dynamics of increase in muscle fibers in fishes in relation to size and growth
    • Weatherley, A. H. & Gill, H. S. (1985). Dynamics of increase in muscle fibers in fishes in relation to size and growth. Experientia 41, 353-354.
    • (1985) Experientia , vol.41 , pp. 353-354
    • Weatherley, A.H.1    Gill, H.S.2
  • 46
    • 0026082636 scopus 로고
    • Thyroid hormone regulates developmental changes in muscle during flounder metamorphosis
    • Yamano, K., Miwa, S., Obinata, T. & Inui, Y. (1991). Thyroid hormone regulates developmental changes in muscle during flounder metamorphosis. General and Comparative Endocrinology 81, 464-472.
    • (1991) General and Comparative Endocrinology , vol.81 , pp. 464-472
    • Yamano, K.1    Miwa, S.2    Obinata, T.3    Inui, Y.4
  • 47
    • 0028209346 scopus 로고
    • Effect of thyroid hormone on developmental transition of myosin light chains during flounder metamorphosis
    • Yamano, K., Takano-Ohmuro, H., Obinata, T. & Inui, Y. (1994). Effect of thyroid hormone on developmental transition of myosin light chains during flounder metamorphosis. General and Comparative Endocrinology 93, 321-326.
    • (1994) General and Comparative Endocrinology , vol.93 , pp. 321-326
    • Yamano, K.1    Takano-Ohmuro, H.2    Obinata, T.3    Inui, Y.4


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