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Volumn 355, Issue 3, 2006, Pages 432-442

What limits the velocity of fast-skeletal muscle contraction in mammals?

Author keywords

Fast kinetics; Flash photoplysis; Myosin isoforms; Subfragment 1; Temperature dependence

Indexed keywords

MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN;

EID: 28944440487     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.10.063     Document Type: Article
Times cited : (103)

References (41)
  • 1
    • 0035165415 scopus 로고    scopus 로고
    • Functional heterogeneity of mammalian single muscle fibres: Do myosin isoforms tell the whole story?
    • R. Bottinelli Functional heterogeneity of mammalian single muscle fibres: do myosin isoforms tell the whole story? Pflugers Arch. 443 2001 6 17
    • (2001) Pflugers Arch. , vol.443 , pp. 6-17
    • Bottinelli, R.1
  • 2
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • S. Schiaffino, and C. Reggiani Molecular diversity of myofibrillar proteins: gene regulation and functional significance Physiol. Rev. 76 1996 371 423
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 3
    • 0021368686 scopus 로고
    • Kinetics of the interaction between actin, ADP, and cardiac myosin-S1
    • R.F. Siemankowski, and H.D. White Kinetics of the interaction between actin, ADP, and cardiac myosin-S1 J. Biol. Chem. 259 1984 5045 5053
    • (1984) J. Biol. Chem. , vol.259 , pp. 5045-5053
    • Siemankowski, R.F.1    White, H.D.2
  • 4
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • R.F. Siemankowski, M.O. Wiseman, and H.D. White ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle Proc. Natl Acad. Sci. USA 82 1985 658 662
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 6
    • 0035824536 scopus 로고    scopus 로고
    • Release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers
    • S. Weiss, R. Rossi, M.A. Pellegrino, R. Bottinelli, M.A. Geeves, and A.D.P. Differing release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers J. Biol. Chem. 276 2001 45902 45908
    • (2001) J. Biol. Chem. , vol.276 , pp. 45902-45908
    • Weiss, S.1    Rossi, R.2    Pellegrino, M.A.3    Bottinelli, R.4    Geeves, M.A.5    Differing, A.D.P.6
  • 7
    • 0029145725 scopus 로고
    • Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: Structural characteristics of the neoformed isozymes
    • J.M. Burgat, C. Ghelis, and R. Cardinaud Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymes FEBS Letters 369 1995 255 259
    • (1995) FEBS Letters , vol.369 , pp. 255-259
    • Burgat, J.M.1    Ghelis, C.2    Cardinaud, R.3
  • 8
    • 0041902749 scopus 로고    scopus 로고
    • Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles
    • M.A. Pellegrino, M. Canepari, R. Rossi, G. D'Antona, C. Reggiani, and R. Bottinelli Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles J. Physiol. 546 2003 677 689
    • (2003) J. Physiol. , vol.546 , pp. 677-689
    • Pellegrino, M.A.1    Canepari, M.2    Rossi, R.3    D'Antona, G.4    Reggiani, C.5    Bottinelli, R.6
  • 9
    • 3042637781 scopus 로고    scopus 로고
    • Fast fibres in a large animal: Fibre types, contractile properties and myosin expression in pig skeletal muscles
    • L. Toniolo, M. Patruno, L. Maccatrozzo, M.A. Pellegrino, M. Canepari, and R. Rossi Fast fibres in a large animal: fibre types, contractile properties and myosin expression in pig skeletal muscles J. Expt. Biol. 207 2004 1875 1886
    • (2004) J. Expt. Biol. , vol.207 , pp. 1875-1886
    • Toniolo, L.1    Patruno, M.2    MacCatrozzo, L.3    Pellegrino, M.A.4    Canepari, M.5    Rossi, R.6
  • 10
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • R. Cooke, and E. Pate The effects of ADP and phosphate on the contraction of muscle fibers Biophys. J. 48 1985 789 798
    • (1985) Biophys. J. , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 11
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • S.B. Marston, and E.W. Taylor Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles J. Mol. Biol. 139 1980 573 600
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 12
    • 0027267667 scopus 로고
    • Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum
    • M.D. Ritchie, M.A. Geeves, S.K. Woodward, and D.J. Manstein Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum Proc. Natl Acad. Sci. USA 90 1993 8619 8623
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8619-8623
    • Ritchie, M.D.1    Geeves, M.A.2    Woodward, S.K.3    Manstein, D.J.4
  • 13
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. a myosin I designed for maintenance of tension?
    • L.M. Coluccio, and M.A. Geeves Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension? J. Biol. Chem. 274 1999 21575 21580
    • (1999) J. Biol. Chem. , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 14
    • 0020501746 scopus 로고
    • The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1
    • N.C. Millar, and M.A. Geeves The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1 FEBS Letters 160 1983 141 148
    • (1983) FEBS Letters , vol.160 , pp. 141-148
    • Millar, N.C.1    Geeves, M.A.2
  • 15
    • 0023788208 scopus 로고
    • The effect of nucleotide upon a specific isomerization of actomyosin subfragment 1
    • M.A. Geeves, and T.E. Jeffries The effect of nucleotide upon a specific isomerization of actomyosin subfragment 1 Biochem. J. 256 1988 41 46
    • (1988) Biochem. J. , vol.256 , pp. 41-46
    • Geeves, M.A.1    Jeffries, T.E.2
  • 16
    • 0033709850 scopus 로고    scopus 로고
    • A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins
    • S. Weiss, I. Chizhov, and M.A. Geeves A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins J. Muscle Res. Cell. Motil. 21 2000 423 432
    • (2000) J. Muscle Res. Cell. Motil. , vol.21 , pp. 423-432
    • Weiss, S.1    Chizhov, I.2    Geeves, M.A.3
  • 17
    • 0018581348 scopus 로고
    • Contraction of glycerinated muscle fibers as a function of the ATP concentration
    • R. Cooke, and W. Bialek Contraction of glycerinated muscle fibers as a function of the ATP concentration Biophys. J. 28 1979 241 258
    • (1979) Biophys. J. , vol.28 , pp. 241-258
    • Cooke, R.1    Bialek, W.2
  • 18
    • 0031806429 scopus 로고    scopus 로고
    • ATP analogs and muscle contraction: Mechanics and kinetics of nucleoside triphosphate binding and hydrolysis
    • M. Regnier, D.M. Lee, and E. Homsher ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis Biophys. J. 74 1998 3044 3058
    • (1998) Biophys. J. , vol.74 , pp. 3044-3058
    • Regnier, M.1    Lee, D.M.2    Homsher, E.3
  • 19
    • 0027393669 scopus 로고
    • Fast myosin heavy chain diversity in skeletal muscles of the rabbit: Heavy chain IId, not IIb predominates
    • S. Aigner, B. Gohlsch, N. Hamalainen, R.S. Staron, A. Uber, U. Wehrle, and D. Pette Fast myosin heavy chain diversity in skeletal muscles of the rabbit: heavy chain IId, not IIb predominates Eur. J. Biochem. 211 1993 367 372
    • (1993) Eur. J. Biochem. , vol.211 , pp. 367-372
    • Aigner, S.1    Gohlsch, B.2    Hamalainen, N.3    Staron, R.S.4    Uber, A.5    Wehrle, U.6    Pette, D.7
  • 20
    • 0028109639 scopus 로고
    • Electrophoretic separation of developmental and adult rabbit skeletal muscle myosin heavy chain isoforms: Example of application to muscle denervation study
    • C. Janmot, and A. d' Albis Electrophoretic separation of developmental and adult rabbit skeletal muscle myosin heavy chain isoforms: example of application to muscle denervation study FEBS Letters 353 1994 13 15
    • (1994) FEBS Letters , vol.353 , pp. 13-15
    • Janmot, C.1    Albis, A.D.'.2
  • 21
    • 0021287199 scopus 로고
    • The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures
    • K.W. Ranatunga The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures J. Physiol. 351 1984 517 529
    • (1984) J. Physiol. , vol.351 , pp. 517-529
    • Ranatunga, K.W.1
  • 22
    • 20544449370 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to actomyosin V and VI: A positive heat capacity change accompanies strong ADP binding
    • J.P. Robblee, W. Cao, A. Henn, D.E. Hannemann, and E.M. De La Cruz Thermodynamics of nucleotide binding to actomyosin V and VI: a positive heat capacity change accompanies strong ADP binding Biochemistry 44 2005 10238 10249
    • (2005) Biochemistry , vol.44 , pp. 10238-10249
    • Robblee, J.P.1    Cao, W.2    Henn, A.3    Hannemann, D.E.4    De La Cruz, E.M.5
  • 23
    • 20544475925 scopus 로고    scopus 로고
    • Magnesium ADP, and actin binding linkage of myosin V: Evidence for multiple myosin V-ADP and actomyosin V-ADP states
    • D.E. Hannemann, W. Cao, A.O. Olivares, J.P. Robblee, and E.M. De La Cruz Magnesium ADP, and actin binding linkage of myosin V: evidence for multiple myosin V-ADP and actomyosin V-ADP states Biochemistry 44 2005 8826 8840
    • (2005) Biochemistry , vol.44 , pp. 8826-8840
    • Hannemann, D.E.1    Cao, W.2    Olivares, A.O.3    Robblee, J.P.4    De La Cruz, E.M.5
  • 25
    • 28244468416 scopus 로고    scopus 로고
    • Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension
    • A. Henn, and E.M. De La Cruz Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension J. Biol. Chem. 2005 In the press
    • (2005) J. Biol. Chem.
    • Henn, A.1    De La Cruz, E.M.2
  • 26
    • 0034647735 scopus 로고    scopus 로고
    • Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding
    • M.A. Geeves, C. Perreault-Micale, and L.M. Coluccio Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding J. Biol. Chem. 275 2000 21624 21630
    • (2000) J. Biol. Chem. , vol.275 , pp. 21624-21630
    • Geeves, M.A.1    Perreault-Micale, C.2    Coluccio, L.M.3
  • 27
    • 14044268874 scopus 로고    scopus 로고
    • Magnesium regulates ADP dissociation from myosin V
    • S.S. Rosenfeld, A. Houdusse, and H.L. Sweeney Magnesium regulates ADP dissociation from myosin V J. Biol. Chem. 280 2005 6072 6079
    • (2005) J. Biol. Chem. , vol.280 , pp. 6072-6079
    • Rosenfeld, S.S.1    Houdusse, A.2    Sweeney, H.L.3
  • 28
    • 0034682764 scopus 로고    scopus 로고
    • Kinetic and spectroscopic evidence for three actomyosin:ADP states in smooth muscle
    • S.S. Rosenfeld, J. Xing, M. Whitaker, H.C. Cheung, F. Brown, and A. Wells Kinetic and spectroscopic evidence for three actomyosin:ADP states in smooth muscle J. Biol. Chem. 275 2000 25418 25426
    • (2000) J. Biol. Chem. , vol.275 , pp. 25418-25426
    • Rosenfeld, S.S.1    Xing, J.2    Whitaker, M.3    Cheung, H.C.4    Brown, F.5    Wells, A.6
  • 29
    • 13444263735 scopus 로고    scopus 로고
    • Adenosine diphosphate and strain sensitivity in myosin motors
    • M. Nyitrai, and M.A. Geeves Adenosine diphosphate and strain sensitivity in myosin motors Phil. Trans. Roy. Soc. ser. B 359 2004 1867 1877
    • (2004) Phil. Trans. Roy. Soc. Ser. B , vol.359 , pp. 1867-1877
    • Nyitrai, M.1    Geeves, M.A.2
  • 30
    • 0028656403 scopus 로고
    • Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres
    • R. Bottinelli, M. Canepari, C. Reggiani, and G.J. Stienen Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres J. Physiol. 481 1994 663 675
    • (1994) J. Physiol. , vol.481 , pp. 663-675
    • Bottinelli, R.1    Canepari, M.2    Reggiani, C.3    Stienen, G.J.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • R.J. Talmadge, and R.R. Roy Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms J. Appl. Physiol. 75 1993 2337 2340
    • (1993) J. Appl. Physiol. , vol.75 , pp. 2337-2340
    • Talmadge, R.J.1    Roy, R.R.2
  • 33
    • 0032797863 scopus 로고    scopus 로고
    • Speeds of actin translocation in vitro by myosins extracted from single rat muscle fibres of different types
    • M. Canepari, R. Rossi, M.A. Pellegrino, C. Reggiani, and R. Bottinelli Speeds of actin translocation in vitro by myosins extracted from single rat muscle fibres of different types Expt. Physiol. 84 1999 803 806
    • (1999) Expt. Physiol. , vol.84 , pp. 803-806
    • Canepari, M.1    Rossi, R.2    Pellegrino, M.A.3    Reggiani, C.4    Bottinelli, R.5
  • 34
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • S.S. Margossian, and S. Lowey Preparation of myosin and its subfragments from rabbit skeletal muscle Methods Enzymol. 85 1982 55 71
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 36
    • 0016851003 scopus 로고
    • Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin
    • S.S. Margossian, S. Lowey, and B. Barshop Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin Nature 258 1975 163 166
    • (1975) Nature , vol.258 , pp. 163-166
    • Margossian, S.S.1    Lowey, S.2    Barshop, B.3
  • 37
    • 0028132899 scopus 로고
    • Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres
    • R. Bottinelli, R. Betto, S. Schiaffino, and C. Reggiani Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres J. Physiol. 478 1994 341 349
    • (1994) J. Physiol. , vol.478 , pp. 341-349
    • Bottinelli, R.1    Betto, R.2    Schiaffino, S.3    Reggiani, C.4
  • 38
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • J.A. Spudich, and S. Watt The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin J. Biol. Chem. 246 1971 4866 4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 39
    • 0022381827 scopus 로고
    • The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin
    • A.H. Criddle, M.A. Geeves, and T. Jeffries The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin Biochem. J. 232 1985 343 349
    • (1985) Biochem. J. , vol.232 , pp. 343-349
    • Criddle, A.H.1    Geeves, M.A.2    Jeffries, T.3


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