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Volumn 519, Issue 3, 1999, Pages 669-678

Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; MUSCLE PROTEIN; MYOSIN;

EID: 0033198519     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.1999.0669n.x     Document Type: Article
Times cited : (106)

References (46)
  • 2
    • 0020064214 scopus 로고
    • Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit
    • ALPERT, N. R. & MULIERI, L. A. (1982). Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. Circulation Research 50, 491-500.
    • (1982) Circulation Research , vol.50 , pp. 491-500
    • Alpert, N.R.1    Mulieri, L.A.2
  • 3
    • 0024368773 scopus 로고
    • Shortening velocity and myosin and myofibrillar ATPase activity related to myosin isoenzyme composition during postnatal development in rat myocardium
    • CAPPELLI, V., BOTTINELLI, R., POGGESI, C., MOGGIO, R. & REGGIANI, C. (1989). Shortening velocity and myosin and myofibrillar ATPase activity related to myosin isoenzyme composition during postnatal development in rat myocardium. Circulation Research 65, 446-457.
    • (1989) Circulation Research , vol.65 , pp. 446-457
    • Cappelli, V.1    Bottinelli, R.2    Poggesi, C.3    Moggio, R.4    Reggiani, C.5
  • 4
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • DANTZIG, J. A., GOLDMAN, Y. E., MILLAR, N. C., LACKTIS, J. & HOMSHER, E. (1992). Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. Journal of Physiology 451, 247-278.
    • (1992) Journal of Physiology , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 6
    • 0021327172 scopus 로고
    • Regulation of myosin synthesis by thyroid hormone: Relative change in the α- and β-myosin heavy chain mRNA levels in rabbit heart
    • EVERETT, A. W., SINHA, A. M., UMEDA, P. K., JAKOVCIC, S., RABINOWITZ, M. & ZAK, R. (1984). Regulation of myosin synthesis by thyroid hormone: Relative change in the α- and β-myosin heavy chain mRNA levels in rabbit heart. Biochemistry 23, 1596-1599.
    • (1984) Biochemistry , vol.23 , pp. 1596-1599
    • Everett, A.W.1    Sinha, A.M.2    Umeda, P.K.3    Jakovcic, S.4    Rabinowitz, M.5    Zak, R.6
  • 7
    • 0028261701 scopus 로고
    • Single myosin molecules mechanics: Piconewton forces and nanometre steps
    • FINER, J. T., SIMMONS, R. M. & SPUDICH, J. A. (1994). Single myosin molecules mechanics: Piconewton forces and nanometre steps. Nature 368, 113-118.
    • (1994) Nature , vol.368 , pp. 113-118
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 8
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
    • GUILFORD, W. H., DUPUIS, D. E., KENNEDY, G., Wu, J., PATLAK, J. B. & WARSHAW, D. M. (1997). Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap. Biophysical Journal 72, 1006-1021.
    • (1997) Biophysical Journal , vol.72 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 10
    • 0025836526 scopus 로고
    • Contractile and calcium regulating capabilities of myocardia of different sized mammals scale with resting heart rate
    • HAMILTON, N. & IANUZZO, C. D. (1991). Contractile and calcium regulating capabilities of myocardia of different sized mammals scale with resting heart rate. Molecular and Cellular Biochemistry 106, 133-141.
    • (1991) Molecular and Cellular Biochemistry , vol.106 , pp. 133-141
    • Hamilton, N.1    Ianuzzo, C.D.2
  • 11
    • 0028280745 scopus 로고
    • Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro
    • HARRIS, D. E., WORK, S. S., WRIGHT, R. K., ALPERT, N. R. & WARSHAW, D. M. (1994). Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro. Journal of Muscle Research and Cell Motility 15, 11-19.
    • (1994) Journal of Muscle Research and Cell Motility , 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
  • 13
    • 0018345405 scopus 로고
    • Structural differences in the heavy chains of rat ventricular myosin isoenzymes
    • HOH, J. F. Y., YEOH, G. P. S., THOMAS, M. A. W. & HIGGENBOTTOM, L. (1979). Structural differences in the heavy chains of rat ventricular myosin isoenzymes. FEBS Letters 97, 330-334.
    • (1979) FEBS Letters , vol.97 , pp. 330-334
    • Hoh, J.F.Y.1    Yeoh, G.P.S.2    Thomas, M.A.W.3    Higgenbottom, L.4
  • 14
    • 0021916285 scopus 로고
    • The economy of isometric force development, myosin isoenzyme pattern and myofibrillar ATPase activity in normal and hypothyroid rat myocardium
    • HOLUBARSCH, C., GOULETTE, R. P., LITTEN, R. Z., MULIERI, L. A. & ALPERT, N. R. (1985). The economy of isometric force development, myosin isoenzyme pattern and myofibrillar ATPase activity in normal and hypothyroid rat myocardium. Circulation Research 56, 78-86.
    • (1985) Circulation Research , vol.56 , pp. 78-86
    • Holubarsch, C.1    Goulette, R.P.2    Litten, R.Z.3    Mulieri, L.A.4    Alpert, N.R.5
  • 15
    • 0025368569 scopus 로고
    • Sliding filaments and molecular motile systems
    • HUXLEY, H. E. (1990). Sliding filaments and molecular motile systems. Journal of Biological Chemistry 265, 8347-8350.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 8347-8350
    • Huxley, H.E.1
  • 16
    • 0026073088 scopus 로고
    • Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
    • KAWAI, M. & HALVORSON, H. R. (1991). Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle. Biophysical Journal 59, 329-342.
    • (1991) Biophysical Journal , vol.59 , pp. 329-342
    • Kawai, M.1    Halvorson, H.R.2
  • 18
    • 0019995903 scopus 로고
    • Altered myosin isozyme patterns from pressure-overloaded and thyrotoxic hypertrophied rabbit hearts
    • LITTEN, R. Z., MARTIN, B. J., LOW, R. B. & ALPERT, N. R. (1982). Altered myosin isozyme patterns from pressure-overloaded and thyrotoxic hypertrophied rabbit hearts. Circulation Research 50, 856-864.
    • (1982) Circulation Research , vol.50 , pp. 856-864
    • Litten, R.Z.1    Martin, B.J.2    Low, R.B.3    Alpert, N.R.4
  • 19
    • 0021153417 scopus 로고
    • Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated
    • LOMPRE, A.-M., NADAL-GINARD, B. & MAHDAVI, V. (1984). Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated. Journal of Biological Chemistry 259, 6437-6446.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 6437-6446
    • Lompre, A.-M.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 22
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • MARSTON, S. B. & TAYLOR, E. W. (1980). Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. Journal of Molecular Biology 139, 573-600.
    • (1980) Journal of Molecular Biology , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 31
    • 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. Biophysical Journal 65, 29-42.
    • (1993) Biophysical Journal , vol.65 , pp. 29-42
    • Patlak, J.B.1
  • 32
    • 0019319641 scopus 로고
    • The ATPase activities of rat cardiac myosin isoenzymes
    • POPE, B., HOH, J. F. Y. & WEEDS, A. (1980). The ATPase activities of rat cardiac myosin isoenzymes. FEBS Letters 118, 205-208.
    • (1980) FEBS Letters , vol.118 , pp. 205-208
    • Pope, B.1    Hoh, J.F.Y.2    Weeds, A.3
  • 34
    • 0020082955 scopus 로고
    • Structural and enzymatic comparison of human cardiac muscle myosins isolated from infants, adults, and patients with hypertrophic cardiomyopathy
    • SCHEIR, J. J. & ADELSTEIN, R. S. (1982). Structural and enzymatic comparison of human cardiac muscle myosins isolated from infants, adults, and patients with hypertrophic cardiomyopathy. Journal of Clinical Investigation 69, 816-825.
    • (1982) Journal of Clinical Investigation , vol.69 , pp. 816-825
    • Scheir, J.J.1    Adelstein, R.S.2
  • 35
    • 0021368686 scopus 로고
    • Kinetics of the interaction between actin, ADP, and cardiac myosin-S1
    • SIEMANKOWSKI, R. F. & WHITE, H. D. (1984). Kinetics of the interaction between actin, ADP, and cardiac myosin-S1. Journal of Biological Chemistry 259, 5045-5053.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 5045-5053
    • Siemankowski, R.F.1    White, H.D.2
  • 36
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of unitary displacements and forces between two cardiac myosin isoforms by the optical trap technique
    • SUGUIRA, S., KOBAYAKAWA, N., FUJITA, H., YAMISHITA, H., MOMOMURA, S., CHAEN, S., OMATA, M. & SUGI, H. (1998). Comparison of unitary displacements and forces between two cardiac myosin isoforms by the optical trap technique. Circulation Research 82, 1029-1034.
    • (1998) Circulation Research , vol.82 , pp. 1029-1034
    • Suguira, S.1    Kobayakawa, N.2    Fujita, H.3    Yamishita, H.4    Momomura, S.5    Chaen, S.6    Omata, M.7    Sugi, H.8
  • 40
    • 0028983138 scopus 로고
    • Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro
    • VANBUREN, P., HARRIS, D. E., ALPERT, N. R. & WARSHAW, D. M. (1995). Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circulation Research 77, 439-444.
    • (1995) Circulation Research , vol.77 , pp. 439-444
    • Vanburen, P.1    Harris, D.E.2    Alpert, N.R.3    Warshaw, D.M.4
  • 42
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • VEIOEL, C., BARTOO, M. L., WHITE, D. C. S., SPARROW, J. C. & MOLLOY, J. E. (1998). The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophysical Journal 75, 1424-1428.
    • (1998) Biophysical Journal , vol.75 , pp. 1424-1428
    • Veioel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 44
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • WARSHAW, D. M., DESROSIERS, J. M., WORK, S. S. & TRYBUS, K. M. (1990). Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. Journal of Cell Biology 111, 453-463.
    • (1990) Journal of Cell Biology , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.