메뉴 건너뛰기




Volumn 73, Issue 5, 1997, Pages 2667-2673

Mobility of creatine phosphokinase and β-enolase in cultured muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

CREATINE KINASE; ENOLASE;

EID: 0030777083     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78295-X     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0024212698 scopus 로고
    • An example of substrate channeling between co-immobilized enzymes. Coupled activity of myosin ATPase and cre- Atine kinase bound to frog heart myofilaments
    • Arrio-Dupont, M. 1988. An example of substrate channeling between co-immobilized enzymes. Coupled activity of myosin ATPase and cre- atine kinase bound to frog heart myofilaments. FEBS Lett. 240:181-185.
    • (1988) FEBS Lett. , vol.240 , pp. 181-185
    • Arrio-Dupont, M.1
  • 2
    • 0026748909 scopus 로고
    • A model system of coupled activity of co-immobilized creatine kinase and myosin
    • Arrio-Dupont, M., J. J. Bechet, and A. D'Albis. 1992. A model system of coupled activity of co-immobilized creatine kinase and myosin. Eur. J. Biochem. 207:951-955.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 951-955
    • Arrio-Dupont, M.1    Bechet, J.J.2    D'Albis, A.3
  • 3
    • 0029863409 scopus 로고    scopus 로고
    • Diffusion of fluorescently labeled macromolecules in cultured muscle cells
    • Arrio-Dupont, M., S. Cribier, G. Foucault, P. P. Devaux. and A. D'Albis. 1996. Diffusion of fluorescently labeled macromolecules in cultured muscle cells. Biophys. J. 70:2327-2332.
    • (1996) Biophys. J. , vol.70 , pp. 2327-2332
    • Arrio-Dupont, M.1    Cribier, S.2    Foucault, G.3    Devaux, P.P.4    D'Albis, A.5
  • 4
  • 5
    • 0025777376 scopus 로고
    • The biochemical and structural maturation of human skeletal muscle cells in culture: The effect of the serum substitute Ultroser G
    • Benders, A. A. G. M., T. H. S. M. Van Kuppevelt, A. Oosterhof, and J. H. Veerkamp. 1991. The biochemical and structural maturation of human skeletal muscle cells in culture: the effect of the serum substitute Ultroser G. Exp. Cell Res. 195:284-294.
    • (1991) Exp. Cell Res. , vol.195 , pp. 284-294
    • Benders, A.A.G.M.1    Van Kuppevelt, T.H.S.M.2    Oosterhof, A.3    Veerkamp, J.H.4
  • 6
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman, S. P., and C. L. Carpenter. 1985. The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem. 54:831-862.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 7
    • 0025957990 scopus 로고
    • Where is the glycolytic complexe? A critical evaluation of present data from muscle tissue
    • Brooks, S. P. J., and K. B. Storey. 1991, Where is the glycolytic complexe? A critical evaluation of present data from muscle tissue. FEBS Lett. 278:135-138.
    • (1991) FEBS Lett. , vol.278 , pp. 135-138
    • Brooks, S.P.J.1    Storey, K.B.2
  • 8
    • 0642351942 scopus 로고
    • Fringe pattern photobleach- Ing. a new method for the measurement of transport coefficients of biological macromolecules
    • Davoust, J., P. H. Devaux, and L. Léger. 1982. Fringe pattern photobleach- ing. a new method for the measurement of transport coefficients of biological macromolecules. EMBO J. 1:1233-1238.
    • (1982) EMBO J. , vol.1 , pp. 1233-1238
    • Davoust, J.1    Devaux, P.H.2    Léger, L.3
  • 9
    • 0016670453 scopus 로고
    • Immunofluorescent localization of glycolytic enzyme proteins and malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit
    • Dölken, G., E. Leisner, and D. Pette. 1975. Immunofluorescent localization of glycolytic enzyme proteins and malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit. Histochemistry. 43:113-121.
    • (1975) Histochemistry , vol.43 , pp. 113-121
    • Dölken, G.1    Leisner, E.2    Pette, D.3
  • 10
    • 0027968681 scopus 로고
    • A brief summary of the history of the detection of creatine kinase isoenzymes
    • Eppenberger, H. M. 1994. A brief summary of the history of the detection of creatine kinase isoenzymes. Mol. Cell. Biochem. 133:9-11.
    • (1994) Mol. Cell. Biochem. , vol.133 , pp. 9-11
    • Eppenberger, H.M.1
  • 11
  • 12
    • 0020654939 scopus 로고
    • Creatine kinase: Structure-activity relationship
    • Kenyon, G. L., and G. H. Reed. 1983. Creatine kinase: structure-activity relationship. Adv. Enzymol. 54:367-426.
    • (1983) Adv. Enzymol. , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 13
    • 0026489887 scopus 로고
    • Association of glycolytic enzymes with the cytoskeleton
    • Knull, H. R., and J. L. Walsh. 1992. Association of glycolytic enzymes with the cytoskeleton. Curr. Top. Cell. Regul. 33:15-30.
    • (1992) Curr. Top. Cell. Regul. , vol.33 , pp. 15-30
    • Knull, H.R.1    Walsh, J.L.2
  • 14
    • 0029155974 scopus 로고
    • Equilibration and exchange of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy
    • Kraft, T., M. Messerli, B. Rothenrutishauser, J. C. Perriard, T. Wallimann. and B. Brenner. 1995. Equilibration and exchange of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy. Biophys. J. 69:1246-1258.
    • (1995) Biophys. J. , vol.69 , pp. 1246-1258
    • Kraft, T.1    Messerli, M.2    Rothenrutishauser, B.3    Perriard, J.C.4    Wallimann, T.5    Brenner, B.6
  • 15
    • 0026787697 scopus 로고
    • Specific enhancement of the cardiac myofibrillar ATPase by bound creatine kinase
    • Krause, S. M., and W. E. Jacobus. 1992. Specific enhancement of the cardiac myofibrillar ATPase by bound creatine kinase. J. Biol. Chem. 267:2480-2486.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2480-2486
    • Krause, S.M.1    Jacobus, W.E.2
  • 16
    • 0002046465 scopus 로고
    • Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle
    • Kuby, S. A., I., Noda, and H. A. Lardy. 1954. Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. Biol. Chem. 209:191-201.
    • (1954) J. Biol. Chem. , vol.209 , pp. 191-201
    • Kuby, S.A.1    Noda, I.2    Lardy, H.A.3
  • 17
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., and B. Kolmerer. 1995. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 18
    • 0021204075 scopus 로고
    • Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery
    • Lanni, F., and B. R. Ware. 1984. Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery. Biophys. J. 46:97-110.
    • (1984) Biophys. J. , vol.46 , pp. 97-110
    • Lanni, F.1    Ware, B.R.2
  • 19
    • 0028078889 scopus 로고
    • Physical properties of cytoplasm
    • Luby-Phelps, K. 1994. Physical properties of cytoplasm. Curr. Opin. Cell Biol. 6:3-9.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 3-9
    • Luby-Phelps, K.1
  • 20
    • 0023690068 scopus 로고
    • Protein diffusivities in skinned frog skeletal muscle fibers
    • Maughan, D., and C. Lord. 1988. Protein diffusivities in skinned frog skeletal muscle fibers. Adv. Exp. Meet. Biol. 226:75-84.
    • (1988) Adv. Exp. Meet. Biol. , vol.226 , pp. 75-84
    • Maughan, D.1    Lord, C.2
  • 21
    • 0024395957 scopus 로고
    • On the organization and diffusion of glycolytic enzymes in skeletelal muscle
    • Maughan, D., and E. Wegner. 1989. On the organization and diffusion of glycolytic enzymes in skeletelal muscle. Muscle Energet. 315:137-147.
    • (1989) Muscle Energet. , vol.315 , pp. 137-147
    • Maughan, D.1    Wegner, E.2
  • 22
    • 0030908790 scopus 로고    scopus 로고
    • Biochemical characterization of the mouse muscle-specific enolase: Developmental changes in electrophoretic variants and selective binding to other proteins
    • Merkulova, T., M. Lucas, C. Jabet, N. Lamandé, J. D. Rouzeau, F. Gros. M. Lazar, and A. Keller. 1997. Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins. Biochem. J. 323:791-800.
    • (1997) Biochem. J. , vol.323 , pp. 791-800
    • Merkulova, T.1    Lucas, M.2    Jabet, C.3    Lamandé, N.4    Rouzeau, J.D.5    Gros, F.6    Lazar, M.7    Keller, A.8
  • 24
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin. M-protein. and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann, W. M. J., M. Gautel, F. Steiner, P. F. M. Vanderven, K. Weber, and D. O. Furst. 1996. The structure of the sarcomeric M band: localization of defined domains of myomesin. M-protein. and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell. Biol. 134:1441-1453.
    • (1996) J. Cell. Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    Vanderven, P.F.M.4    Weber, K.5    Furst, D.O.6
  • 25
    • 0024438502 scopus 로고
    • Immunohistochemical localization of creatine kinase M in canine myocardial cells: Most creatine kinase M is distributed in the A-band
    • Otsu, N., M. Hirata, S. Tuboi, and K. Miyazawa. 1989. Immunohistochemical localization of creatine kinase M in canine myocardial cells: most creatine kinase M is distributed in the A-band. J. Histochcm. Cytochem. 31:1465-1470.
    • (1989) J. Histochcm. Cytochem. , vol.31 , pp. 1465-1470
    • Otsu, N.1    Hirata, M.2    Tuboi, S.3    Miyazawa, K.4
  • 26
    • 0027421025 scopus 로고
    • Changes in creatine kinase-M localization in acute ischemic myocardial cells: Immunoelectron microscopic studies
    • Otsu, N., I. Yamaguchi, E. Komatsu, and K. Miyazawa. 1993. Changes in creatine kinase-M localization in acute ischemic myocardial cells: immunoelectron microscopic studies. Circ. Res. 73:935-942.
    • (1993) Circ. Res. , vol.73 , pp. 935-942
    • Otsu, N.1    Yamaguchi, I.2    Komatsu, E.3    Miyazawa, K.4
  • 27
    • 0024430062 scopus 로고
    • Enolase exists in the fluid phase of cytoplasm in 3T3 cells
    • Pagliaro, L., K. Kerr, and D. L. Taylor. 1989. Enolase exists in the fluid phase of cytoplasm in 3T3 cells. J. Cell Sci. 94:333-342.
    • (1989) J. Cell Sci. , vol.94 , pp. 333-342
    • Pagliaro, L.1    Kerr, K.2    Taylor, D.L.3
  • 29
    • 0016272164 scopus 로고
    • Enolase isozymes in rat tissues. Electrophoretic, chromatographic, immunological and kinetic properties
    • Rider, C. C., and C. B. Taylor. 1974. Enolase isozymes in rat tissues. Electrophoretic, chromatographic, immunological and kinetic properties, Biochim. Biophys. Acta. 365:285-300.
    • (1974) Biochim. Biophys. Acta. , vol.365 , pp. 285-300
    • Rider, C.C.1    Taylor, C.B.2
  • 30
    • 0023895438 scopus 로고
    • Intracellular targeting of isoproteins in muscle cytoarchitecture
    • Schäfer, B. W., and J. Perriard. 1988. Intracellular targeting of isoproteins in muscle cytoarchitecture. J. Cell Biol. 106:1161-1170.
    • (1988) J. Cell Biol. , vol.106 , pp. 1161-1170
    • Schäfer, B.W.1    Perriard, J.2
  • 31
    • 0027772143 scopus 로고
    • Evidence for proximal cysteine and lysine residues present at the nucleotide domain of rabbit muscle creatine kinase
    • Sheikh, S., K. Mukunda, and S. S. Katiyar. 1993. Evidence for proximal cysteine and lysine residues present at the nucleotide domain of rabbit muscle creatine kinase. Biochim. Biophys. Acta. 1203:276-281.
    • (1993) Biochim. Biophys. Acta. , vol.1203 , pp. 276-281
    • Sheikh, S.1    Mukunda, K.2    Katiyar, S.S.3
  • 33
    • 0028362281 scopus 로고
    • Ultrastruclure of skeletal muscle Tibers studied by a plunge quick freezing method: Myofilament lengths
    • Sosa, H., D. Popp, G. Ouyang, and H. E. Huxley. 1994. Ultrastruclure of skeletal muscle Tibers 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.E.4
  • 34
    • 0025359442 scopus 로고
    • Enzyme-enzyme interactions and their metabolic role
    • Srere, P. A., and J. Ovadi. 1990. Enzyme-enzyme interactions and their metabolic role. FEBS Lett. 268:360-364.
    • (1990) FEBS Lett. , vol.268 , pp. 360-364
    • Srere, P.A.1    Ovadi, J.2
  • 35
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick, J. 1994. Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19:405-409.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 405-409
    • Trinick, J.1
  • 36
    • 0021947598 scopus 로고
    • Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle
    • Wallimann, T., and H. M. Eppenberger. 1985. Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle. Cell Muscle Motil. 6:239-285.
    • (1985) Cell Muscle Motil. , vol.6 , pp. 239-285
    • Wallimann, T.1    Eppenberger, H.M.2
  • 37
    • 0026585611 scopus 로고
    • Intracellular companmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The phosphocreatine circuit for cellular energy homeostasis
    • Wallimann, T., M. Wyss, D. Brdiczka, K. Nicolay, and H. M. Eppenberger. 1992. Intracellular companmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the phosphocreatine circuit for cellular energy homeostasis. Biochem. J. 281:21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 38
    • 0026778172 scopus 로고
    • In situ compartmentation of creatine kinase in intact sarcomeric muscle: The actomyosin overlap zone as a molecular sieve
    • Wegmann, G., E. Zanolla, H. M. Eppenberger, and T. Wallimann. 1992. In situ compartmentation of creatine kinase in intact sarcomeric muscle: the actomyosin overlap zone as a molecular sieve. J. Muscle Res. Cell Motil. 13:420-435.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 420-435
    • Wegmann, G.1    Zanolla, E.2    Eppenberger, H.M.3    Wallimann, T.4
  • 39
    • 0017411635 scopus 로고
    • On the role of organized multienzyme systems in cellular metabolism: A general synthesis
    • Welch, G. R. 1977. On the role of organized multienzyme systems in cellular metabolism: a general synthesis. Prog. Biophys. Mol. Biol. 32:103-191.
    • (1977) Prog. Biophys. Mol. Biol. , vol.32 , pp. 103-191
    • Welch, G.R.1
  • 40
    • 0014144616 scopus 로고
    • Studies on adenosine triphosphate transphosphorylases. V. Studies on the polypeptide chains of the crystalline adenosine triphosphate transphosphorylase from rabbit skeletal muscle
    • Yue, R. H., R. H. Palmieri, O. E. Olson, and S. A. Kuby. 1967. Studies on adenosine triphosphate transphosphorylases. V. Studies on the polypeptide chains of the crystalline adenosine triphosphate transphosphorylase from rabbit skeletal muscle. Biochemistry. 6:3204-3227.
    • (1967) Biochemistry , vol.6 , pp. 3204-3227
    • Yue, R.H.1    Palmieri, R.H.2    Olson, O.E.3    Kuby, S.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.