메뉴 건너뛰기




Volumn 87, Issue 1, 2004, Pages 430-441

Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CONTRACTILE PROTEIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 3042736851     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.035063     Document Type: Article
Times cited : (22)

References (50)
  • 2
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres
    • Dantzig, J. A., M. G. Hibberd, D. R. Trentham, and Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J. Physiol. (Lond.). 432:639-680.
    • (1991) J. Physiol. (Lond.) , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Trentham, D.R.3    Goldman, Y.E.4
  • 3
    • 0020438546 scopus 로고
    • Relaxation of muscle fibres by photolysis of caged ATP
    • Goldman, Y. E., M. G. Hibberd, J. A. McCray, and D. R. Trentham. 1982. Relaxation of muscle fibres by photolysis of caged ATP. Nature. 300:701-705.
    • (1982) Nature , vol.300 , pp. 701-705
    • Goldman, Y.E.1    Hibberd, M.G.2    McCray, J.A.3    Trentham, D.R.4
  • 4
    • 0021284583 scopus 로고
    • Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5′-triphosphate
    • Goldman, Y. E., M. G. Hibberd, and D. R. Trentham. 1984a. Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5′-triphosphate. J. Physiol. (Lond.). 354:577-604.
    • (1984) J. Physiol. (Lond.) , vol.354 , pp. 577-604
    • Goldman, Y.E.1    Hibberd, M.G.2    Trentham, D.R.3
  • 5
    • 0021284579 scopus 로고
    • Initiation of active contraction by photogeneration of adenosine-5′-triphosphate in rabbit psoas muscle fibres
    • Goldman, Y. E., M. G. Hibberd, and D. R. Trentham. 1984b. Initiation of active contraction by photogeneration of adenosine-5′-triphosphate in rabbit psoas muscle fibres. J. Physiol. (Lond.). 354:605-624.
    • (1984) J. Physiol. (Lond.) , vol.354 , pp. 605-624
    • Goldman, Y.E.1    Hibberd, M.G.2    Trentham, D.R.3
  • 6
    • 25344456991 scopus 로고
    • Time-resolved X-ray diffraction measurements on Lethocerus fribrillar flight muscle following the photolytic release of ATP from 'caged-ATP'
    • Goody, R. S., K. Güth, Y. Maéda, K. J. V. Poole, and G. Rapp. 1985. Time-resolved X-ray diffraction measurements on Lethocerus fribrillar flight muscle following the photolytic release of ATP from 'caged-ATP.' J. Physiol. (Lond.). 364:75P.
    • (1985) J. Physiol. (Lond.). , vol.364
    • Goody, R.S.1    Güth, K.2    Maéda, Y.3    Poole, K.J.V.4    Rapp, G.5
  • 7
    • 0016610095 scopus 로고
    • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle
    • Haselgrove, J. C. 1975. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J. Mol. Biol. 92: 113-143.
    • (1975) J. Mol. Biol. , vol.92 , pp. 113-143
    • Haselgrove, J.C.1
  • 8
    • 0032437985 scopus 로고    scopus 로고
    • 2+-sensitive transient contraction upon photolysis of caged ATP in rat muscle fibres: A study on the Bremel-Weber type cooperation
    • 2+-sensitive transient contraction upon photolysis of caged ATP in rat muscle fibres: a study on the Bremel-Weber type cooperation. J. Muscle Res. Cell Motil. 19:923-930.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 923-930
    • Horiuti, K.1    Kagawa, K.2
  • 10
    • 0030805514 scopus 로고    scopus 로고
    • Mechanical study of rat soleus muscle using caged ATP and X-ray diffraction: High ADP affinity of slow cross-bridges
    • Horiuti, K., N. Yagi, and S. Takemori. 1997. Mechanical study of rat soleus muscle using caged ATP and X-ray diffraction: high ADP affinity of slow cross-bridges. J. Physiol. (Lond.). 502:433-447.
    • (1997) J. Physiol. (Lond.) , vol.502 , pp. 433-447
    • Horiuti, K.1    Yagi, N.2    Takemori, S.3
  • 11
    • 0034840690 scopus 로고    scopus 로고
    • Single turnover of cross-bridge ATPase in rat muscle fibers studies by photolysis of caged ATP
    • Horiuti, K., N. Yagi, and S. Takemori. 2001. Single turnover of cross-bridge ATPase in rat muscle fibers studies by photolysis of caged ATP. J. Muscle Res. Cell Motil. 22:101-109.
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 101-109
    • Horiuti, K.1    Yagi, N.2    Takemori, S.3
  • 12
    • 0000244537 scopus 로고
    • Structural changes in the acitn- and myosin-containing filaments during contraction
    • Huxley, H. E. 1973. Structural changes in the acitn- and myosin-containing filaments during contraction. Cold Spring Harb. Symp. Quant. Biol. 37:361-376.
    • (1973) Cold Spring Harb. Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 13
    • 85010249552 scopus 로고
    • The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley, H. E., and W. Brown. 1967. The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30:383-434.
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 15
    • 0028878144 scopus 로고
    • Strain sensitivity and turnover rate of low force cross-bridges in contracting skeletal muscle fibers in the presence of phosphate
    • Iwamoto, H. 1995. Strain sensitivity and turnover rate of low force cross-bridges in contracting skeletal muscle fibers in the presence of phosphate. Biophys. J. 68:243-250.
    • (1995) Biophys. J. , vol.68 , pp. 243-250
    • Iwamoto, H.1
  • 16
    • 0035951287 scopus 로고    scopus 로고
    • X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex
    • Iwamoto, H., K. Oiwa, T. Suzuki, and T. Fujisawa. 2001. X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex. J. Mol. Biol. 305:863-874.
    • (2001) J. Mol. Biol. , vol.305 , pp. 863-874
    • Iwamoto, H.1    Oiwa, K.2    Suzuki, T.3    Fujisawa, T.4
  • 17
    • 0036293422 scopus 로고    scopus 로고
    • States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques
    • Iwamoto, H., K. Oiwa, T. Suzuki, and T. Fujisawa. 2002. States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques. J. Mol. Biol. 317:707-720.
    • (2002) J. Mol. Biol. , vol.317 , pp. 707-720
    • Iwamoto, H.1    Oiwa, K.2    Suzuki, T.3    Fujisawa, T.4
  • 18
    • 0141754066 scopus 로고    scopus 로고
    • Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles
    • Iwamoto, H., J. Wakayama, T. Fujisawa, and N. Yagi. 2003a. Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles. Biophys. J. 85:2492-2506.
    • (2003) Biophys. J. , vol.85 , pp. 2492-2506
    • Iwamoto, H.1    Wakayama, J.2    Fujisawa, T.3    Yagi, N.4
  • 19
    • 0141662405 scopus 로고    scopus 로고
    • X-ray evidence for structural changes of thin filament induced by cycling myosin heads
    • Iwamoto, H., J. Wakayama, T. Tamura, T. Fujisawa, and N. Yagi. 2003b. X-ray evidence for structural changes of thin filament induced by cycling myosin heads. Biophys. J. 84:248a.
    • (2003) Biophys. J. , vol.84
    • Iwamoto, H.1    Wakayama, J.2    Tamura, T.3    Fujisawa, T.4    Yagi, N.5
  • 21
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan, J. H., B. Forbush III, and J. F. Hoffman. 1978. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry. 17:1929-1935.
    • (1978) Biochemistry , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush III, B.2    Hoffman, J.F.3
  • 22
    • 0035997061 scopus 로고    scopus 로고
    • Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor
    • Koubassova, N. A., and A. K. Tsaturyan. 2002. Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor. Biophys. J. 83:1082-1097.
    • (2002) Biophys. J. , vol.83 , pp. 1082-1097
    • Koubassova, N.A.1    Tsaturyan, A.K.2
  • 23
    • 0032984795 scopus 로고    scopus 로고
    • The effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional x-ray diffraction study on single muscle fibers
    • Kraft, T., S. Xu, B. Brenner, and L. C. Yu. 1999. The effect of thin filament activation on the attachment of weak binding cross-bridges: a two-dimensional x-ray diffraction study on single muscle fibers. Biophys. J. 76:1494-1513.
    • (1999) Biophys. J. , vol.76 , pp. 1494-1513
    • Kraft, T.1    Xu, S.2    Brenner, B.3    Yu, L.C.4
  • 24
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle by time-resolved X-ray diffraction
    • Kress, M., H. E. Huxley, A. R. Faruqi, and J. Hendrix. 1986. Structural changes during activation of frog muscle by time-resolved X-ray diffraction. J. Mol. Biol. 188:325-342.
    • (1986) J. Mol. Biol. , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 25
    • 0032940756 scopus 로고    scopus 로고
    • A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibres: Effects of pH, MgADP, and inorganic phosphate
    • Lipscomb, S., R. E. Palmer, Q. Li, L. D. Allhouse, T. Miller, J. D. Potter, and C. C. Ashley. 1999. A diazo-2 study of relaxation mechanisms in frog and barnacle muscle fibres: effects of pH, MgADP, and inorganic phosphate. Pflügers Arch. 437:204-212.
    • (1999) Pflügers Arch. , vol.437 , pp. 204-212
    • Lipscomb, S.1    Palmer, R.E.2    Li, Q.3    Allhouse, L.D.4    Miller, T.5    Potter, J.D.6    Ashley, C.C.7
  • 26
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 27
    • 0028210495 scopus 로고
    • Kinetic mechanism of myofibril ATPase
    • Ma, Y.-Z., and E. W. Taylor. 1994. Kinetic mechanism of myofibril ATPase. Biophys. J. 66:1542-1553.
    • (1994) Biophys. J. , vol.66 , pp. 1542-1553
    • Ma, Y.-Z.1    Taylor, E.W.2
  • 28
    • 0023782821 scopus 로고
    • Cause of changes in the thin filament-associated reflexions on activation of frog muscle-myosin binding or conformational change of actin
    • Maeda, Y., D. Popp, and S. M. McLaughlin. 1988. Cause of changes in the thin filament-associated reflexions on activation of frog muscle-myosin binding or conformational change of actin. Adv. Exp. Med. Biol. 226:381-390.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 381-390
    • Maeda, Y.1    Popp, D.2    McLaughlin, S.M.3
  • 29
    • 0028294216 scopus 로고
    • Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP
    • Martin, H., and R. J. Barsotti. 1994. Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP. Biophys. J. 66:1115-1128.
    • (1994) Biophys. J. , vol.66 , pp. 1115-1128
    • Martin, H.1    Barsotti, R.J.2
  • 30
    • 0021773118 scopus 로고
    • Intensification of the 5.9-nm actin layer line in contracting muscle
    • Matsubara, I., N. Yagi, H. Miura, M. Ozeki, and T. Izumi. 1984. Intensification of the 5.9-nm actin layer line in contracting muscle. Nature. 312:471-473.
    • (1984) Nature , vol.312 , pp. 471-473
    • Matsubara, I.1    Yagi, N.2    Miura, H.3    Ozeki, M.4    Izumi, T.5
  • 31
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
    • Moore, P. B., H. E. Huxley, and D. J. DeRosier. 1970. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50:279-295.
    • (1970) J. Mol. Biol. , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    DeRosier, D.J.3
  • 32
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles
    • Parry, D. A. D., and J. M. Squire. 1973. Structural role of tropomyosin in muscle regulation: analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75:33-55.
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.D.1    Squire, J.M.2
  • 33
    • 0026279816 scopus 로고
    • Dynamic X-ray diffraction measurements following photolytic relaxation and activation of skinned rabbit psoas fibres
    • Poole, K. J. V., Y. Maéda, G. Rapp, and R. S. Goody. 1991. Dynamic X-ray diffraction measurements following photolytic relaxation and activation of skinned rabbit psoas fibres. Adv. Biophys. 27:63-75.
    • (1991) Adv. Biophys. , vol.27 , pp. 63-75
    • Poole, K.J.V.1    Maéda, Y.2    Rapp, G.3    Goody, R.S.4
  • 34
    • 0023710915 scopus 로고
    • The time course of changes in the equatorial diffraction patterns from different muscle types on photolysis of caged-ATP
    • Poole, K. J. V., G. Rapp, Y. Maéda, and R. S. Goody. 1988. The time course of changes in the equatorial diffraction patterns from different muscle types on photolysis of caged-ATP. Adv. Exp. Med. Biol. 226:391-404.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 391-404
    • Poole, K.J.V.1    Rapp, G.2    Maéda, Y.3    Goody, R.S.4
  • 37
    • 0028227181 scopus 로고
    • Inhibition of ATP binding to myofibrils and acto-myosin subfragment 1 by caged ATP
    • Sleep, J., C. Herrmann, T. Barman, and F. Travers. 1994. Inhibition of ATP binding to myofibrils and acto-myosin subfragment 1 by caged ATP. Biochemistry. 33:6038-6042.
    • (1994) Biochemistry , vol.33 , pp. 6038-6042
    • Sleep, J.1    Herrmann, C.2    Barman, T.3    Travers, F.4
  • 38
    • 0019003415 scopus 로고
    • Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1
    • Sleep, J. A., and R. L. Hutton. 1980. Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1. Biochemistry. 19:1276-1283.
    • (1980) Biochemistry , vol.19 , pp. 1276-1283
    • Sleep, J.A.1    Hutton, R.L.2
  • 39
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J. M., and E. P. Morris. 1998. A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12:761-771.
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 40
    • 3042710699 scopus 로고    scopus 로고
    • Intensity of X-ray reflections from skeletal muscle thin filaments partially occupied with myosin heads: Effect of cooperative binding
    • In press
    • Tamura, T., J. Wakayama, T. Fujisawa, N. Yagi, and H. Iwamoto. 2004. Intensity of X-ray reflections from skeletal muscle thin filaments partially occupied with myosin heads: effect of cooperative binding. J. Muscle Res. Cell Motil. In press.
    • (2004) J. Muscle Res. Cell Motil.
    • Tamura, T.1    Wakayama, J.2    Fujisawa, T.3    Yagi, N.4    Iwamoto, H.5
  • 41
    • 0028053976 scopus 로고
    • Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase
    • Thirlwell, H., J. E. T. Corrie, G. P. Reid, D. R. Trentham, and M. A. Ferenczi. 1994. Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase. Biophys. J. 67:2436-2447.
    • (1994) Biophys. J. , vol.67 , pp. 2436-2447
    • Thirlwell, H.1    Corrie, J.E.T.2    Reid, G.P.3    Trentham, D.R.4    Ferenczi, M.A.5
  • 42
    • 0028941575 scopus 로고
    • Inhibition of unloaded shortening velocity in permeabilised muscle fibers by caged-ATP compounds
    • Thirlwell, H., J. A. Sleep, and M. A. Ferenczi. 1995. Inhibition of unloaded shortening velocity in permeabilised muscle fibers by caged-ATP compounds. J. Muscle Res. Cell Motil. 16:131-137.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 131-137
    • Thirlwell, H.1    Sleep, J.A.2    Ferenczi, M.A.3
  • 43
    • 0036001362 scopus 로고    scopus 로고
    • Diffraction by partially occupied helices
    • Tsaturyan, A. K. 2002. Diffraction by partially occupied helices. Acta Crystallogr. A58:292-294.
    • (2002) Acta Crystallogr. A , vol.58 , pp. 292-294
    • Tsaturyan, A.K.1
  • 44
    • 0033231443 scopus 로고    scopus 로고
    • Structural responses to the photolytic release of ATP in frog muscle fibres, observed by time-resolved X-ray diffraction
    • Tsaturyan, A. K., S. Y. Bershitsky, R. Burns, Z. H. He, and M. A. Ferenczi. 1999. Structural responses to the photolytic release of ATP in frog muscle fibres, observed by time-resolved X-ray diffraction. J. Physiol. (Lond.). 520:681-696.
    • (1999) J. Physiol. (Lond.) , vol.520 , pp. 681-696
    • Tsaturyan, A.K.1    Bershitsky, S.Y.2    Burns, R.3    He, Z.H.4    Ferenczi, M.A.5
  • 46
    • 0021867708 scopus 로고
    • Time-resolved X-ray diffraction studies on the intensity changes of the 5.9 and 5.1 nm actin layer lines from frog skeletal muscle during an isometric tetanus using synchrotron radiation
    • Wakabayashi, K., H. Tanaka, Y. Amemiya, A. Fujishima, T. Kobayashi, T. Hamanaka, H. Sugi, and T. Mitsui. 1985. Time-resolved X-ray diffraction studies on the intensity changes of the 5.9 and 5.1 nm actin layer lines from frog skeletal muscle during an isometric tetanus using synchrotron radiation. Biophys. J. 47:847-850.
    • (1985) Biophys. J. , vol.47 , pp. 847-850
    • Wakabayashi, K.1    Tanaka, H.2    Amemiya, Y.3    Fujishima, A.4    Kobayashi, T.5    Hamanaka, T.6    Sugi, H.7    Mitsui, T.8
  • 47
    • 0023762517 scopus 로고
    • Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction
    • Wakabayashi, K., Y. Ueno, Y. Amemiya, and H. Tanaka. 1988. Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction. Adv. Exp. Med. Biol. 226:353-367.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 353-367
    • Wakabayashi, K.1    Ueno, Y.2    Amemiya, Y.3    Tanaka, H.4
  • 48
    • 0030485290 scopus 로고    scopus 로고
    • Labelling of thin filaments by myosin heads in contracting and rigor vertebrate skeletal muscles
    • Yagi, N. 1996. Labelling of thin filaments by myosin heads in contracting and rigor vertebrate skeletal muscles. Acta Crystallogr. D52: 1169-1173.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 1169-1173
    • Yagi, N.1
  • 49
    • 0037304613 scopus 로고    scopus 로고
    • An x-ray diffraction study on early structural changes in skeletal muscle contraction
    • Yagi, N. 2003. An x-ray diffraction study on early structural changes in skeletal muscle contraction. Biophys. J. 84:1093-1102.
    • (2003) Biophys. J. , vol.84 , pp. 1093-1102
    • Yagi, N.1
  • 50
    • 0042823508 scopus 로고    scopus 로고
    • Rigor force producing cross-bridges in skeletal muscle fibers activated by a sub-stoichiometric amount of ATP
    • Yamada, T., Y. Takezawa, H. Iwamoto, S. Suzuki, and K. Wakabayashi. 2003. Rigor force producing cross-bridges in skeletal muscle fibers activated by a sub-stoichiometric amount of ATP. Biophys. J. 85:1741-1753
    • (2003) Biophys. J. , vol.85 , pp. 1741-1753
    • Yamada, T.1    Takezawa, Y.2    Iwamoto, H.3    Suzuki, S.4    Wakabayashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.