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Volumn 70, Issue 1, 1996, Pages 48-56

Cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle in the presence of antibody fragments against the N-terminus of actin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; IMMUNOGLOBULIN F(AB) FRAGMENT; TROPONIN I;

EID: 0030033895     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79579-6     Document Type: Article
Times cited : (6)

References (54)
  • 2
    • 0023654810 scopus 로고
    • New states of actomyosin
    • Applegate, D., and P. Flicker. 1987. New states of actomyosin. J. Biol. Chem. 262:6856-6863.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6856-6863
    • Applegate, D.1    Flicker, P.2
  • 4
    • 0024726038 scopus 로고
    • Microsecond rotational motion of spin-labeled myosin heads during isometric muscle contraction. Saturation transfer electron paramagnetic resonance
    • Barnett, V. A., and D. D. Thomas. 1989. Microsecond rotational motion of spin-labeled myosin heads during isometric muscle contraction. Saturation transfer electron paramagnetic resonance. Biophys. J. 56:517-523.
    • (1989) Biophys. J. , vol.56 , pp. 517-523
    • Barnett, V.A.1    Thomas, D.D.2
  • 5
    • 0025148366 scopus 로고
    • Characterization of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region
    • Bartegi, A., A. Fattoum, J. Derancourt, and R. Kassab. 1990. Characterization of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region. J. Biol. Chem. 265: 15231-15238.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15231-15238
    • Bartegi, A.1    Fattoum, A.2    Derancourt, J.3    Kassab, R.4
  • 6
    • 0028362279 scopus 로고
    • Rotational dynamics of actin-bound intermediates in the myosin adenosine triphosphate cycle in myofibrils
    • Berger, C. L., and D. D. Thomas. 1994. Rotational dynamics of actin-bound intermediates in the myosin adenosine triphosphate cycle in myofibrils. Biophys. J. 67:250-261.
    • (1994) Biophys. J. , vol.67 , pp. 250-261
    • Berger, C.L.1    Thomas, D.D.2
  • 8
    • 0019171105 scopus 로고
    • ++ concentration on maximum unloaded shortening velocity. Measurements on single glycerinated rabbit psoas muscle fibers
    • ++ concentration on maximum unloaded shortening velocity. Measurements on single glycerinated rabbit psoas muscle fibers. J. Muscle Res. Cell Motil 1:409-428
    • (1980) J. Muscle Res. Cell Motil , vol.1 , pp. 409-428
    • Brenner, B.1
  • 9
    • 0020536686 scopus 로고
    • A technique for stabilizing the striation pattern in fully activated skinned rabbit psoas fibers
    • Brenner, B. 1983. A technique for stabilizing the striation pattern in fully activated skinned rabbit psoas fibers. Biophys. J. 41:99-102.
    • (1983) Biophys. J. , vol.41 , pp. 99-102
    • Brenner, B.1
  • 10
    • 0002355231 scopus 로고
    • Muscle mechanics and biochemical kinetics
    • John Squire, editor. Macmillan Press Ltd., London
    • Brenner, B. 1990. Muscle mechanics and biochemical kinetics. In Molecular Mechanism of Muscular Contraction. John Squire, editor. Macmillan Press Ltd., London. 77-149.
    • (1990) Molecular Mechanism of Muscular Contraction , pp. 77-149
    • Brenner, B.1
  • 12
    • 0028954283 scopus 로고
    • Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release
    • Brenner, B., J. M. Chalovich, and L. C. Yu. 1995. Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release Biophys. J. 68:106s-111s.
    • (1995) Biophys. J. , vol.68
    • Brenner, B.1    Chalovich, J.M.2    Yu, L.C.3
  • 13
    • 24544459317 scopus 로고
    • Effect of antibodies against the N-terminal segment of actin on stiffness and active force of skinned rabbit psoas fibers
    • Abstr.
    • Brenner, B., G. DasGupta, and E. Reisler 1993. Effect of antibodies against the N-terminal segment of actin on stiffness and active force of skinned rabbit psoas fibers. Biophys. J. 64:24a. (Abstr.)
    • (1993) Biophys. J. , vol.64
    • Brenner, B.1    Dasgupta, G.2    Reisler, E.3
  • 14
    • 2042451727 scopus 로고
    • The rate of force generation in muscle: Correlation with the actomyosin ATPase in solution
    • Brenner, B., and E. Eisenberg. 1986. The rate of force generation in muscle: correlation with the actomyosin ATPase in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 15
    • 0027178461 scopus 로고
    • Structural changes in the actomyosin cross-bridges associated with force generation
    • Brenner, B , and L. C. Yu. 1993a. Structural changes in the actomyosin cross-bridges associated with force generation. Proc. Natl. Acad. Sci. USA. 90:5252-5256.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5252-5256
    • Brenner, B.1    Yu, L.C.2
  • 16
    • 0027421031 scopus 로고
    • Evidence for structural changes in cross-bridges during force generation
    • Brenner, B., and L. C. Yu. 1993b. Evidence for structural changes in cross-bridges during force generation. Adv. Exp. Med. Biol. 332: 461-467.
    • (1993) Adv. Exp. Med. Biol. , vol.332 , pp. 461-467
    • Brenner, B.1    Yu, L.C.2
  • 17
    • 0021150823 scopus 로고
    • X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths
    • Brenner, B., L. C. Yu, and R. J. Podolsky. 1984. X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys. J. 46:299-306.
    • (1984) Biophys. J. , vol.46 , pp. 299-306
    • Brenner, B.1    Yu, L.C.2    Podolsky, R.J.3
  • 18
    • 0342293921 scopus 로고
    • Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy chain is pan of the actin-binding site
    • Chaussepied, P., and M. Morales. 1989. Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is pan of the actin-binding site. Proc. Natl. Acad Sci. USA. 85:7471-7475.
    • (1989) Proc. Natl. Acad Sci. USA , vol.85 , pp. 7471-7475
    • Chaussepied, P.1    Morales, M.2
  • 20
    • 0021813998 scopus 로고
    • Structure of the actin-myosin complex in the presence of ATP
    • Craig R., L. E. Greene, and E. Eisenberg. 1985. Structure of the actin-myosin complex in the presence of ATP. Proc. Natl. Acad. Sci. USA. 82:3247-3251.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3247-3251
    • Craig, R.1    Greene, L.E.2    Eisenberg, E.3
  • 21
    • 0028274287 scopus 로고
    • Caldesmon. N-terminal yeast actin mutants, and the regulation of actomyosin interactions
    • Crosbie, R. H., C. Miller, J. M. Chalovich, P. A Rubenstein, and E. Reisler. 1994. Caldesmon. N-terminal yeast actin mutants, and the regulation of actomyosin interactions Biochemistry. 33:3210-3216.
    • (1994) Biochemistry , vol.33 , pp. 3210-3216
    • Crosbie, R.H.1    Miller, C.2    Chalovich, J.M.3    Rubenstein, P.A.4    Reisler, E.5
  • 23
    • 0024974811 scopus 로고
    • Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions in the presence of ATP
    • DasGupta, G., and E. Reisler. 1989. Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions in the presence of ATP. J. Mol Biol. 207:833-836.
    • (1989) J. Mol Biol. , vol.207 , pp. 833-836
    • DasGupta, G.1    Reisler, E.2
  • 24
    • 0025938170 scopus 로고
    • Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: Detection by antibodies against the N-terminal segment of actin
    • DasGupta, G., and E. Reisler. 1991. Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection by antibodies against the N-terminal segment of actin. Biochemistry. 30:9961-9966.
    • (1991) Biochemistry , vol.30 , pp. 9961-9966
    • DasGupta, G.1    Reisler, E.2
  • 25
    • 0026593988 scopus 로고
    • Actomyosin interactions in the presence of ATP and the N-terminal segment of actin
    • DasGupta, G., and E. Reisler. 1992. Actomyosin interactions in the presence of ATP and the N-terminal segment of actin. Biochemistry. 31: 1836-1841.
    • (1992) Biochemistry , vol.31 , pp. 1836-1841
    • DasGupta, G.1    Reisler, E.2
  • 26
    • 0024559493 scopus 로고
    • Nucleotide-induced states of myosin subfragment 1 cross-linked to actin
    • Duong, A. M., and E. Reisler, 1989. Nucleotide-induced states of myosin subfragment 1 cross-linked to actin. Biochemistry. 28:3502-3509.
    • (1989) Biochemistry , vol.28 , pp. 3502-3509
    • Duong, A.M.1    Reisler, E.2
  • 27
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg E., and L. E. Greene. 1980. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42:293-309.
    • (1980) Annu. Rev. Physiol. , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 28
    • 0021992946 scopus 로고
    • Muscular contraction and free energy transduction in biological systems
    • Eisenberg E., and T L. Hill. 1985. Muscular contraction and free energy transduction in biological systems. Science. 227:999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 30
    • 0001109417 scopus 로고
    • Thiophosphate analogs of nucleoside di- and triphosphates
    • Goody, R. S., and F. Eckstein. 1971. Thiophosphate analogs of nucleoside di- and triphosphates. J. Am. Chem. Soc. 93:6252-6257.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 6252-6257
    • Goody, R.S.1    Eckstein, F.2
  • 31
    • 0011196273 scopus 로고
    • Troponin I binds to the N-terminal twelve-residue segment of actin
    • Abstr.
    • Grabarek Z., and J. Gergely. 1987. Troponin I binds to the N-terminal twelve-residue segment of actin. Biophys. J. 51:331a. (Abstr.)
    • (1987) Biophys. J. , vol.51
    • Grabarek, Z.1    Gergely, J.2
  • 33
    • 0028954281 scopus 로고
    • The actomyosin interaction and its control by tropomyosin
    • Holmes, K. C. 1995. The actomyosin interaction and its control by tropomyosin. Biophys. J. 68:2s-7s.
    • (1995) Biophys. J. , vol.68
    • Holmes, K.C.1
  • 34
    • 0029005992 scopus 로고
    • Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions
    • Kraft, T., J. M. Chalovich, L. C. Yu, and B. Brenner. 1995a. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions. Biophys. J. 68:2404-2418.
    • (1995) Biophys. J. , vol.68 , pp. 2404-2418
    • Kraft, T.1    Chalovich, J.M.2    Yu, L.C.3    Brenner, B.4
  • 35
    • 0029155974 scopus 로고
    • Equilibration and exchange of fluorescently labeled molecules in skinned muscle fiber visualized by confocal microscopy
    • Kraft, T., M. Messerli, B. Rothen-Rutishauser, F.-C. Perriard, T. Wallimann, and B. Brenner. 1995b. Equilibration and exchange of fluorescently labeled molecules in skinned muscle fiber visualized by confocal microscopy. Biophys. J. 69:1246-1258.
    • (1995) Biophys. J. , vol.69 , pp. 1246-1258
    • Kraft, T.1    Messerli, M.2    Rothen-Rutishauser, B.3    Perriard, F.-C.4    Wallimann, T.5    Brenner, B.6
  • 36
    • 0026613697 scopus 로고
    • 2+ on weak cross-bridge interaction with actin in the presence of adenosine 5′-[γ-thio]triphosphate
    • 2+ on weak cross-bridge interaction with actin in the presence of adenosine 5′-[γ-thio]triphosphate. Proc. Natl. Acad. Sci. USA. 89:11362-11366.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11362-11366
    • Kraft, T.1    Yu, L.C.2    Kuhn, H.J.3    Brenner, B.4
  • 37
    • 0023970297 scopus 로고
    • The interaction of troponin-I with the N-terminal region of actin
    • Levine, B. A., A. J. Moir, and S. V. Perry. 1988. The interaction of troponin-I with the N-terminal region of actin. Eur. J. Biochem. 172:389-397.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 389-397
    • Levine, B.A.1    Moir, A.J.2    Perry, S.V.3
  • 39
    • 0021319632 scopus 로고
    • X-ray evidence for two structural states of the actomyosin cross-bridge in muscle fibers
    • Matsuda, T., and R. J. Podolsky. 1984. X-ray evidence for two structural states of the actomyosin cross-bridge in muscle fibers. Proc. Natl. Acad. Sci. USA 81:2364-2368.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2364-2368
    • Matsuda, T.1    Podolsky, R.J.2
  • 40
  • 41
    • 0023662527 scopus 로고
    • Antibodies directed against N-terminal residues on actin do not block actin-myosin binding
    • Miller, L., M. Kalnoski, Z. Yunossi, J. C. Bulinski, and E. Reisler. 1987. Antibodies directed against N-terminal residues on actin do not block actin-myosin binding. Biochemistry. 26:6064-6070.
    • (1987) Biochemistry , vol.26 , pp. 6064-6070
    • Miller, L.1    Kalnoski, M.2    Yunossi, Z.3    Bulinski, J.C.4    Reisler, E.5
  • 44
    • 0024421616 scopus 로고
    • Comparative aspects of the molecular basis for thin-filament linked regulation of energy transduction in skeletal and smooth muscle
    • Patchell, V. B., S. V. Perry, A. J. G. Moir, E. Audemard, D. Mornet, and B. A. Levine. 1989. Comparative aspects of the molecular basis for thin-filament linked regulation of energy transduction in skeletal and smooth muscle. Biochem. Soc. Trans. 17:901.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 901
    • Patchell, V.B.1    Perry, S.V.2    Moir, A.J.G.3    Audemard, E.4    Mornet, D.5    Levine, B.A.6
  • 45
    • 0027405710 scopus 로고
    • Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin ATPase cycle
    • Pollard, T., D. Bhandari, P. Maupin, D. Wachsstock, A. G. Weeds, and H. G. Zot 1993 Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin ATPase cycle. Biophys. J. 64: 454-471.
    • (1993) Biophys. J. , vol.64 , pp. 454-471
    • Pollard, T.1    Bhandari, D.2    Maupin, P.3    Wachsstock, D.4    Weeds, A.G.5    Zot, H.G.6
  • 47
    • 0027551520 scopus 로고
    • Actin molecular structure and function
    • Reisler, E. 1993. Actin molecular structure and function. Curr. Opin. Cell Biol. 5:41-47.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 41-47
    • Reisler, E.1
  • 48
    • 0020382825 scopus 로고
    • Identification of myosin binding sites on the actin sequence
    • Sutoh, K. 1982. Identification of myosin binding sites on the actin sequence. Biochemistry. 21:3654-3661.
    • (1982) Biochemistry , vol.21 , pp. 3654-3661
    • Sutoh, K.1
  • 49
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictiosrelium actin: Disruption of a negative charge cluster at the N-terminus
    • Sutoh, K., M. Ando, K. Sutoh, and Y. Y. Toyoshima. 1991 Site-directed mutations of Dictiosrelium actin: disruption of a negative charge cluster at the N-terminus. Proc. Natl. Acad Sci. USA. 88:7711-7714.
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1    Ando, M.2    Sutoh, K.3    Toyoshima, Y.Y.4
  • 50
    • 0028946841 scopus 로고
    • The mechanism of force generation in myosin: A disorder-to-order transition, coupled to internal structural changes
    • Thomas, D. D., S. Ramachandran, O. Roopnarine, D. W. Hayden, and E M. Ostrap. 1995. the mechanism of force generation in myosin: a disorder-to-order transition, coupled to internal structural changes Biophys. J. 68:135s-141s.
    • (1995) Biophys. J. , vol.68
    • Thomas, D.D.1    Ramachandran, S.2    Roopnarine, O.3    Hayden, D.W.4    Ostrap, E.M.5
  • 51
    • 17144450693 scopus 로고
    • Millisecond time resolution electron cryomicroscopy at the M-ATP transient kinetic state of the acto-myosin ATPase
    • Walker, M., J. Trinick, and H White. 1995. Millisecond time resolution electron cryomicroscopy at the M-ATP transient kinetic state of the acto-myosin ATPase. Biophys. J. 68:87s-91s.
    • (1995) Biophys. J. , vol.68
    • Walker, M.1    Trinick, J.2    White, H.3
  • 52
    • 0028210497 scopus 로고
    • Electron cryomicroscopy of the acto-myosin-S1 complex during steady-state ATP hydrolysis
    • Walker, M., H. White, B. Belknap, and J. Trinick. 1994. Electron cryomicroscopy of the acto-myosin-S1 complex during steady-state ATP hydrolysis. Biophys. J. 66:1563-1572.
    • (1994) Biophys. J. , vol.66 , pp. 1563-1572
    • Walker, M.1    White, H.2    Belknap, B.3    Trinick, J.4
  • 53
    • 0026101038 scopus 로고
    • Identification of the site important for the actinactivated MgATPase activity of myosin subfragment-1
    • Yamamoto, K. 1991. Identification of the site important for the actinactivated MgATPase activity of myosin subfragment-1. J. Mol. Biol. 217:229-233.
    • (1991) J. Mol. Biol. , vol.217 , pp. 229-233
    • Yamamoto, K.1
  • 54
    • 0024518455 scopus 로고
    • Structures of actomyosin cross-bridges in relaxed and rigor muscle fibers
    • Yu, L. C., and B. Brenner. 1989. Structures of actomyosin cross-bridges in relaxed and rigor muscle fibers. Biophys. J. 55:441-453.
    • (1989) Biophys. J. , vol.55 , pp. 441-453
    • Yu, L.C.1    Brenner, B.2


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