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Volumn 72, Issue 3, 1997, Pages 1006-1021

Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTIN; MYOSIN;

EID: 0031041817     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78753-8     Document Type: Article
Times cited : (224)

References (47)
  • 1
    • 0022655537 scopus 로고
    • Observation of a single-beam gradient force optical trap for dielectric particles
    • Ashkin, A., J. M. Dziedzic, J. E. Bjorkholm, and S. Chu. 1986. Observation of a single-beam gradient force optical trap for dielectric particles. Opt. Lett. 11:288-290.
    • (1986) Opt. Lett. , vol.11 , pp. 288-290
    • Ashkin, A.1    Dziedzic, J.M.2    Bjorkholm, J.E.3    Chu, S.4
  • 2
    • 0025790141 scopus 로고
    • Characterization of a mammalian smooth muscle myosin heavy-chain gene: Complete nucleotide and protein coding sequence and analysis of the 5′ end of the gene
    • Barbij, P., C. Kelly, and M. Periasamy. 1991. Characterization of a mammalian smooth muscle myosin heavy-chain gene: complete nucleotide and protein coding sequence and analysis of the 5′ end of the gene. Proc. Natl. Acad. Sci. USA. 88:10676-10680.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10676-10680
    • Barbij, P.1    Kelly, C.2    Periasamy, M.3
  • 3
    • 0028811467 scopus 로고
    • One small step for myosin
    • Block, S. M. 1995. One small step for myosin. Nature. 378:132-133.
    • (1995) Nature , vol.378 , pp. 132-133
    • Block, S.M.1
  • 4
    • 0028908413 scopus 로고
    • Analysis of high resolution recordings of motor movement
    • Block, S. M., and K. Svoboda. 1995. Analysis of high resolution recordings of motor movement. Biophys. J. 68:230s-241s.
    • (1995) Biophys. J. , vol.68
    • Block, S.M.1    Svoboda, K.2
  • 5
    • 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-11s.
    • (1995) Biophys. J , vol.68
    • Brenner, B.1    Chalovich, J.M.2    Yu, L.C.3
  • 7
    • 0342980830 scopus 로고
    • The contractile mechanism in smooth muscle
    • E. E. Bitter, editor. Wiley and Sons, New York
    • Fay, F. S., D. D. Rees, and D. M. Warshaw. 1981. The contractile mechanism in smooth muscle. In Membrane Structure and Function, Vol. 4. E. E. Bitter, editor. Wiley and Sons, New York. 80-130.
    • (1981) Membrane Structure and Function , vol.4 , pp. 80-130
    • Fay, F.S.1    Rees, D.D.2    Warshaw, D.M.3
  • 8
    • 0028932523 scopus 로고
    • Characterization of single actin-myosin interactions
    • Finer, J. T., A. D. Mehta, and J. A. Spudich. 1995. Characterization of single actin-myosin interactions. Biophys. J. 68:291s-97s.
    • (1995) Biophys. J. , vol.68
    • Finer, J.T.1    Mehta, A.D.2    Spudich, J.A.3
  • 9
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometer steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature. 368:113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 10
    • 0342980829 scopus 로고    scopus 로고
    • Smooth muscle myosin with an elongated neck region produces greater unitary displacements in vitro
    • 2
    • Guilford, W. H., M. J. Tyska, Y. Freyzon, D. M. Warshaw, and K. M. Trybus. 1996. Smooth muscle myosin with an elongated neck region produces greater unitary displacements in vitro. Biophys J. 70(2, part 2):A127.
    • (1996) Biophys J. , vol.70 , Issue.2 PART
    • Guilford, W.H.1    Tyska, M.J.2    Freyzon, Y.3    Warshaw, D.M.4    Trybus, K.M.5
  • 11
    • 0023145911 scopus 로고
    • Sliding movement of single actin filaments on one-headed myosin filaments
    • Harada, Y., A. Noguchi, A. Kishino, and T. Yanarida. 1987. Sliding movement of single actin filaments on one-headed myosin filaments. Nature. 326:805-808.
    • (1987) Nature , vol.326 , pp. 805-808
    • Harada, Y.1    Noguchi, A.2    Kishino, A.3    Yanarida, T.4
  • 12
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • Harris, D. E., and D. M. Warshaw. 1993a. Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J. Biol. Chem. 268:14764-14768.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 13
    • 0027223768 scopus 로고
    • Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay
    • Harris, D. E., and D. M. Warshaw. 1993b. Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay. Circ. Res. 72:219-224.
    • (1993) Circ. Res. , vol.72 , pp. 219-224
    • Harris, D.E.1    Warshaw, D.M.2
  • 14
    • 0028280745 scopus 로고
    • Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro
    • Harris, D. E., S. S. Work, R. K. Wright, N. R. Alpert, and D. M. Warshaw. 1994. Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro. J. Muscle Res. Cell Motil. 15:11-19.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 11-19
    • Harris, D.E.1    Work, S.S.2    Wright, R.K.3    Alpert, N.R.4    Warshaw, D.M.5
  • 15
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. 7:255-317.
    • (1957) Prog. Biophys. , vol.7 , pp. 255-317
    • Huxley, A.F.1
  • 16
    • 0025368569 scopus 로고
    • Sliding filaments and molecular motile systems
    • Huxley, H. E. 1990. Sliding filaments and molecular motile systems. J. Biol. Chem. 265:8347-8350.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8347-8350
    • Huxley, H.E.1
  • 18
    • 0027163347 scopus 로고
    • Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers
    • Kawai, M., and Y. Zhao. 1993. Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers. Biophys. J. 65: 638-651.
    • (1993) Biophys. J. , vol.65 , pp. 638-651
    • Kawai, M.1    Zhao, Y.2
  • 19
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S. J., and J. A. Spudich. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA. 83: 6272-6276.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 20
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • Marston, S. B., and E. W. Taylor. 1980. Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. J. Mol. Biol. 139:573-600.
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 21
    • 0028408334 scopus 로고
    • Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay
    • Miyata, H., H. Hakozaki, H. Yoshikawa, N. Suzuki, K. Kinosita, Jr., T. Naishizaka, and S. Ishiwata. 1994. Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay. J. Biochem. 115:644-647.
    • (1994) J. Biochem. , vol.115 , pp. 644-647
    • Miyata, H.1    Hakozaki, H.2    Yoshikawa, H.3    Suzuki, N.4    Kinosita K., Jr.5    Naishizaka, T.6    Ishiwata, S.7
  • 23
    • 0028964579 scopus 로고
    • Single-molecule mechanics of heavy meromyosin and sl interacting with rabbit or Drosophila actins using optical tweezers
    • Molloy, J. E., J. E. Burns, J. C. Sparrow, R. T. Tregear, J. Kendrick-Jones, and D. C. S. White. 1995b. single-molecule mechanics of heavy meromyosin and sl interacting with rabbit or Drosophila actins using optical tweezers. Biophys. J. 68:298s-305s.
    • (1995) Biophys. J. , vol.68
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Kendrick-Jones, J.5    White, D.C.S.6
  • 24
    • 0016327314 scopus 로고
    • Force-generating capacity and contractile protein content of arterial smooth muscle
    • Murphy, R. A., J. T. Herlihy, and J. Megerman. 1974. Force-generating capacity and contractile protein content of arterial smooth muscle. J. Gen. Physiol. 64:691-705.
    • (1974) J. Gen. Physiol. , vol.64 , pp. 691-705
    • Murphy, R.A.1    Herlihy, J.T.2    Megerman, J.3
  • 25
    • 0025274490 scopus 로고
    • The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker
    • Onishi, H., and K. Fujiwara. 1990. The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker. Biochemistry. 29:3013-3023.
    • (1990) Biochemistry , vol.29 , pp. 3013-3023
    • Onishi, H.1    Fujiwara, K.2
  • 26
    • 0025065292 scopus 로고
    • Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross-linking between the two heads of rigor smooth muscle heavy meromyosin
    • Onishi, H., T. Maita, G. Matsuda, and K. Fujiwara. 1990. Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross-linking between the two heads of rigor smooth muscle heavy meromyosin. J. Biol. Chem. 265:19362-19368.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19362-19368
    • Onishi, H.1    Maita, T.2    Matsuda, G.3    Fujiwara, K.4
  • 27
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and J. A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85:164-81.
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 28
    • 0027194750 scopus 로고
    • Measuring kinetics of complex single ion channel data using mean-variance histograms
    • Patlak, J. B. 1993. Measuring kinetics of complex single ion channel data using mean-variance histograms. Biophys. J. 65:29-42.
    • (1993) Biophys. J. , vol.65 , pp. 29-42
    • Patlak, J.B.1
  • 29
    • 0024455332 scopus 로고
    • + channel bursts in frog skeletal muscle
    • + channel bursts in frog skeletal muscle. J. Gen. Physiol. 94:279-301.
    • (1989) J. Gen. Physiol. , vol.94 , pp. 279-301
    • Patlak, J.B.1    Ortiz, M.2
  • 30
    • 0028952024 scopus 로고
    • Coordinated hydrolysis explains the mechanical behavior of kinesin
    • Peskin, C. S., and G. Oster. 1995. Coordinated hydrolysis explains the mechanical behavior of kinesin. Biophys. J. 68:202s-211s.
    • (1995) Biophys. J. , vol.68
    • Peskin, C.S.1    Oster, G.2
  • 33
    • 0029561337 scopus 로고    scopus 로고
    • Chimeric substitutions of the actin binding loop disrupt regulation of smooth muscle heavy meromyosin
    • Rovner, A. S., Y. Freyzon, and K. M. Trybus. 1996. Chimeric substitutions of the actin binding loop disrupt regulation of smooth muscle heavy meromyosin. J. Biol. Chem. 270:30260-302263.
    • (1996) J. Biol. Chem. , vol.270 , pp. 30260-302263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 34
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski, R. F., M. O. Wiseman, and H. D. White. 1985. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc. Natl. Acad. Sci. USA. 82:658-662.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 35
    • 0029976424 scopus 로고    scopus 로고
    • Quantitative measurements of force and displacement using an optical trap
    • Simmons, R. M., J. T. Finer, S. Chu, and J. A. Spudich. 1996. Quantitative measurements of force and displacement using an optical trap. Biophys. J. 70:1813-1822.
    • (1996) Biophys. J. , vol.70 , pp. 1813-1822
    • Simmons, R.M.1    Finer, J.T.2    Chu, S.3    Spudich, J.A.4
  • 37
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. A. 1994. How molecular motors work. Nature. 372:515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 40
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a a lever arm to generate movement
    • Uyeda, T. Q., P. D. Abramson, and J. A. Spudich. 1996. The neck region of the myosin motor domain acts as a a lever arm to generate movement. Proc. Natl. Acad. Sci. USA. 93:4459-4464.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 42
    • 0028085210 scopus 로고
    • Enhanced force generation by smooth muscle myosin in vitro
    • VanBuren, P., S. S. Work, and D. M. Warshaw. 1994b. Enhanced force generation by smooth muscle myosin in vitro. Proc. Natl. Acad. Sci. USA. 91:202-205.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 202-205
    • Vanburen, P.1    Work, S.S.2    Warshaw, D.M.3
  • 43
    • 0023194796 scopus 로고
    • Force:velocity relationship in single isolated toad stomach smooth muscle cells
    • Warshaw, D. M. 1987. Force:velocity relationship in single isolated toad stomach smooth muscle cells. J. Gen. Physiol. 89:771-789.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 771-789
    • Warshaw, D.M.1
  • 44
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw, D. M., J. M. Desrosiers, S. S. Work, and K. M. Trybus. 1990. Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J. Cell Biol. 111:453-463.
    • (1990) J. Cell Biol. , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4
  • 45
    • 0020505875 scopus 로고
    • Cross-bridge elasticity in single smooth muscle cells
    • Warshaw, D. M., and F. S. Fay. 1983. Cross-bridge elasticity in single smooth muscle cells. J. Gen. Physiol. 82:157-199.
    • (1983) J. Gen. Physiol. , vol.82 , pp. 157-199
    • Warshaw, D.M.1    Fay, F.S.2
  • 46
    • 0027223294 scopus 로고
    • Identification of a novel smooth muscle myosin heavy chain cDNA: Isoform diversity in the S1 head region
    • White, S., A. F. Martin, and M. Periasamy. 1993. Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region. Am. J. Physiol. 264(5, Pt 1):C1252-C1258.
    • (1993) Am. J. Physiol. , vol.264 , Issue.1-5 PT
    • White, S.1    Martin, A.F.2    Periasamy, M.3
  • 47
    • 0025373431 scopus 로고
    • Mechanical transients of single toad stomach smooth muscle cells
    • Yamakawa, M., D. E. Harris, F. S. Fay, and D. M. Warshaw. 1990. Mechanical transients of single toad stomach smooth muscle cells. J. Gen. Physiol. 95:697-715.
    • (1990) J. Gen. Physiol. , vol.95 , pp. 697-715
    • Yamakawa, M.1    Harris, D.E.2    Fay, F.S.3    Warshaw, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.