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Volumn 543, Issue 3, 2002, Pages 757-766

Effects of thyroxine on myosin isoform expression and mechanical properties in guinea-pig smooth muscle

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ISOPROTEIN; MESSENGER RNA; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; THYROID HORMONE; THYROXINE; MYOSIN HEAVY CHAIN ALPHA; MYOSIN HEAVY CHAIN BETA; MYOSIN LIGHT CHAIN KINASE;

EID: 0037106415     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2002.025494     Document Type: Review
Times cited : (11)

References (54)
  • 1
    • 0028661135 scopus 로고
    • Influence of the thyroid state on the intrinsic contractile properties of the bladder muscle
    • Adeniyi, K. O., Ogunkeye, O. O., Senok, S. S., & Udoh, F. V. (1994). Influence of the thyroid state on the intrinsic contractile properties of the bladder muscle. Acta Physiologica Hungarica 82, 69-74.
    • (1994) Acta Physiologica Hungarica , vol.82 , pp. 69-74
    • Adeniyi, K.O.1    Ogunkeye, O.O.2    Senok, S.S.3    Udoh, F.V.4
  • 2
    • 0023720687 scopus 로고
    • Cross-bridge behaviour in skinned smooth muscle of the guinea-pig taenia coli at altered ionic strength
    • Arheden, H., Arner, A. & Hellstrand, P. (1988). Cross-bridge behaviour in skinned smooth muscle of the guinea-pig taenia coli at altered ionic strength. Journal of Physiology 403, 539-558.
    • (1988) Journal of Physiology , vol.403 , pp. 539-558
    • Arheden, H.1    Arner, A.2    Hellstrand, P.3
  • 3
    • 0022034172 scopus 로고
    • Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea-pig
    • Arner, A. & Hellstrand, P. (1985). Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea-pig. Journal of Physiology 360, 347-365.
    • (1985) Journal of Physiology , vol.360 , pp. 347-365
    • Arner, A.1    Hellstrand, P.2
  • 4
    • 0024791088 scopus 로고
    • Myosin heavy chain isoform diversity in smooth muscle is produced by differential RNA processing
    • Babij, P. & Periasamy, M. (1989). Myosin heavy chain isoform diversity in smooth muscle is produced by differential RNA processing. Journal of Molecular Biology 210, 673-679.
    • (1989) Journal of Molecular Biology , vol.210 , pp. 673-679
    • Babij, P.1    Periasamy, M.2
  • 6
    • 0028782187 scopus 로고
    • The molecular basis of thyroid hormone action
    • Brent, G. A. (1994). The molecular basis of thyroid hormone action. New England Journal of Medicine 331, 847-853.
    • (1994) New England Journal of Medicine , vol.331 , pp. 847-853
    • Brent, G.A.1
  • 8
    • 0025940380 scopus 로고
    • Influence of hyperthyroidism on maximal shortening velocity and myosin isoform distribution in skeletal muscles
    • Caiozzo, V. J., Herrick, R. E. & Baldwin, K. M. (1991). Influence of hyperthyroidism on maximal shortening velocity and myosin isoform distribution in skeletal muscles. American Journal of Physiology 261, C285-295.
    • (1991) American Journal of Physiology , vol.261
    • Caiozzo, V.J.1    Herrick, R.E.2    Baldwin, K.M.3
  • 9
    • 0027688033 scopus 로고
    • Identification of a thyroid hormone response element in the mouse myogenin gene: Characterization of the thyroid hormone and retinoid X receptor heterodimeric binding site
    • Downes, M., Griggs, R., Atkins, A., Olson, E. N. & Muscat, G. E. (1993). Identification of a thyroid hormone response element in the mouse myogenin gene: characterization of the thyroid hormone and retinoid X receptor heterodimeric binding site. Cell Growth and Differentiation 4, 901-909.
    • (1993) Cell Growth and Differentiation , vol.4 , pp. 901-909
    • Downes, M.1    Griggs, R.2    Atkins, A.3    Olson, E.N.4    Muscat, G.E.5
  • 10
    • 0019769492 scopus 로고
    • Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle
    • Fabiato, A. (1981). Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle. Journal of General Physiology 78, 457-497.
    • (1981) Journal of General Physiology , vol.78 , pp. 457-497
    • Fabiato, A.1
  • 11
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A. & Fabiato, F. (1979). Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. Journal de Physiologie 75, 463-505.
    • (1979) Journal de Physiologie , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 12
    • 0030980825 scopus 로고    scopus 로고
    • Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells
    • Fisher, S. A., Ikebe, M. & Brozovich, F. (1997). Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells. Circulation Research 80, 885-893.
    • (1997) Circulation Research , vol.80 , pp. 885-893
    • Fisher, S.A.1    Ikebe, M.2    Brozovich, F.3
  • 13
    • 0027787986 scopus 로고
    • Flash photolysis studies of relaxation and cross-bridge detachment: Higher sensitivity of tonic than phasic smooth muscle to MgADP
    • Fuglsang, A., Khromov, A., Torok, K., Somlyo, A. V. & Somlyo, A. P. (1993). Flash photolysis studies of relaxation and cross-bridge detachment: higher sensitivity of tonic than phasic smooth muscle to MgADP. Journal of Muscle Research and Cell Motility 14, 666-677.
    • (1993) Journal of Muscle Research and Cell Motility , vol.14 , pp. 666-677
    • Fuglsang, A.1    Khromov, A.2    Torok, K.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 14
    • 0024376145 scopus 로고
    • Dynamic interaction between actin and myosin subfragment 1 in the presence of ADP
    • Geeves, M. A. (1989). Dynamic interaction between actin and myosin subfragment 1 in the presence of ADP. Biochemistry 28, 5864-5871.
    • (1989) Biochemistry , vol.28 , pp. 5864-5871
    • Geeves, M.A.1
  • 16
    • 0025093608 scopus 로고
    • The influence of thyroid states upon responses of the rat aorta to catecholamines
    • Gunasekera, R. D. & Kuriyama, H. (1990). The influence of thyroid states upon responses of the rat aorta to catecholamines. British Journal of Pharmacology 99, 541-547.
    • (1990) British Journal of Pharmacology , vol.99 , pp. 541-547
    • Gunasekera, R.D.1    Kuriyama, H.2
  • 17
    • 0029947386 scopus 로고    scopus 로고
    • Alternative splicing of smooth muscle myosin heavy chains and its functional consequences
    • Haase, H. & Morano, I. (1996). Alternative splicing of smooth muscle myosin heavy chains and its functional consequences. Journal of Cellular Biochemistry 60, 521-528.
    • (1996) Journal of Cellular Biochemistry , vol.60 , pp. 521-528
    • Haase, H.1    Morano, I.2
  • 18
    • 0024500991 scopus 로고
    • Selective binding of L-thyroxine by myosin light chain kinase
    • Hagiwara, M., Mamiya, S. & Hidaka, H. (1989). Selective binding of L-thyroxine by myosin light chain kinase. Journal of Biological Chemistry 264, 40-44.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 40-44
    • Hagiwara, M.1    Mamiya, S.2    Hidaka, H.3
  • 20
    • 0022382511 scopus 로고
    • Myosin light chain phosphorylation and the cross-bridge cycle at low substrate concentration in chemically skinned guinea pig Taenia coli
    • Hellstrand, P. & Arner, A. (1985). Myosin light chain phosphorylation and the cross-bridge cycle at low substrate concentration in chemically skinned guinea pig Taenia coli. Pflügers Archiv 405, 323-328.
    • (1985) Pflügers Archiv , vol.405 , pp. 323-328
    • Hellstrand, P.1    Arner, A.2
  • 21
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd, M. G., Dantzig, J. A., Trentham, D. R. & Goldman, Y. E. (1985). Phosphate release and force generation in skeletal muscle fibers. Science 228, 1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 22
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of shortening
    • Hill, A. V. (1938). The heat of shortening and the dynamic constants of shortening. Proceedings of the Royal Society 126, 231-252.
    • (1938) Proceedings of the Royal Society , vol.126 , pp. 231-252
    • Hill, A.V.1
  • 23
    • 0018367891 scopus 로고
    • Action of triiodothyronine on the synthesis of rat ventricular myosin isoenzymes
    • Hoh, J. F. & Egerton, L. J. (1979). Action of triiodothyronine on the synthesis of rat ventricular myosin isoenzymes. FEBS Letters 101, 143-148.
    • (1979) FEBS Letters , vol.101 , pp. 143-148
    • Hoh, J.F.1    Egerton, L.J.2
  • 24
    • 0018093539 scopus 로고
    • Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacement
    • Hoh, J. F., McGrath, P. A. & Hale, P. T. (1978). Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. Journal of Molecular and Cellular Cardiology 10, 1053-1076.
    • (1978) Journal of Molecular and Cellular Cardiology , vol.10 , pp. 1053-1076
    • Hoh, J.F.1    McGrath, P.A.2    Hale, P.T.3
  • 26
    • 0022616134 scopus 로고
    • All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner
    • Izumo, S., Nadal-Ginard, B. & Mahdavi, V. (1986). All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner. Science 231, 597-600.
    • (1986) Science , vol.231 , pp. 597-600
    • Izumo, S.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 27
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • Kelley, C. A., Sellers, J. R., Gard, D. L., Bui, D., Adelstein, R. S. & Baines, I. C. (1996). Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities. Journal of Cell Biology 134, 675-687.
    • (1996) Journal of Cell Biology , vol.134 , pp. 675-687
    • Kelley, C.A.1    Sellers, J.R.2    Gard, D.L.3    Bui, D.4    Adelstein, R.S.5    Baines, I.C.6
  • 29
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C. A., Takahashi, M., Yu, J. H. & Adelstein, R. S. (1993). An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. Journal of Biological Chemistry 268, 12848-12854.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 31
    • 0025605092 scopus 로고
    • Nucleotide and deduced amino acid sequence of cDNAs encoding two isoforms for the 17,000 dalton myosin light chain in bovine aortic smooth muscle
    • Lash, J. A., Helper, D. J., Klug, M., Nicolozakes, A. W. & Hathaway, D. R. (1990). Nucleotide and deduced amino acid sequence of cDNAs encoding two isoforms for the 17,000 dalton myosin light chain in bovine aortic smooth muscle. Nucleic Acids Research 18, 7176.
    • (1990) Nucleic Acids Research , vol.18 , pp. 7176
    • Lash, J.A.1    Helper, D.J.2    Klug, M.3    Nicolozakes, A.W.4    Hathaway, D.R.5
  • 33
    • 0343338187 scopus 로고    scopus 로고
    • Substrate and product dependence of force and shortening in fast and slow smooth muscle
    • Löfgren, M., Malmqvist, U. & Arner, A. (2001). Substrate and product dependence of force and shortening in fast and slow smooth muscle. Journal of General Physiology 117, 407-418.
    • (2001) Journal of General Physiology , vol.117 , pp. 407-418
    • Löfgren, M.1    Malmqvist, U.2    Arner, A.3
  • 35
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle
    • Malmqvist, U. & Arner, A. (1991). Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflügers Archiv 418, 523-530.
    • (1991) Pflügers Archiv , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 36
    • 0032553296 scopus 로고    scopus 로고
    • Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges
    • Matthew, J. D., Khromov, A. S., Trybus, K. M., Somlyo, A. P. & Somlyo, A. V. (1998). Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges. Journal of Biological Chemistry 273, 31289-31296.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 31289-31296
    • Matthew, J.D.1    Khromov, A.S.2    Trybus, K.M.3    Somlyo, A.P.4    Somlyo, A.V.5
  • 38
    • 0027200232 scopus 로고
    • Expression of myosin heavy and light chains changes during pregnancy in the rat uterus
    • Morano, I., Erb, G. & Sogl, B. (1993). Expression of myosin heavy and light chains changes during pregnancy in the rat uterus. Pflügers Archiv 423, 434-441.
    • (1993) Pflügers Archiv , vol.423 , pp. 434-441
    • Morano, I.1    Erb, G.2    Sogl, B.3
  • 39
    • 0034665404 scopus 로고    scopus 로고
    • Control of cardiac myosin heavy chain gene expression
    • Morkin, E. (2000). Control of cardiac myosin heavy chain gene expression. Microscopy Research and Technique 50, 522-531.
    • (2000) Microscopy Research and Technique , vol.50 , pp. 522-531
    • Morkin, E.1
  • 40
    • 0028361264 scopus 로고
    • Activation of myoD gene transcription by 3,5,3′-triiodo-L-thyronine: A direct role for the thyroid hormone and retinoid X receptors
    • Muscat, G. E., Mynett-Johnson, L., Dowhan, D., Downes, M. & Griggs, R. (1994). Activation of myoD gene transcription by 3,5,3′-triiodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors. Nucleic Acids Research 22, 583-591.
    • (1994) Nucleic Acids Research , vol.22 , pp. 583-591
    • Muscat, G.E.1    Mynett-Johnson, L.2    Dowhan, D.3    Downes, M.4    Griggs, R.5
  • 41
    • 0029969119 scopus 로고    scopus 로고
    • Acute effects of thyroid hormone on vascular smooth muscle
    • Ojamaa, K., Klemperer, J. D. & Klein, I. (1996). Acute effects of thyroid hormone on vascular smooth muscle. Thyroid 6, 505-512.
    • (1996) Thyroid , vol.6 , pp. 505-512
    • Ojamaa, K.1    Klemperer, J.D.2    Klein, I.3
  • 42
    • 0028967798 scopus 로고
    • Effects of inorganic phosphate on cross-bridge kinetics at different activation levels in skinned guinea-pig smooth muscle
    • Österman, A. & Arner, A. (1995). Effects of inorganic phosphate on cross-bridge kinetics at different activation levels in skinned guinea-pig smooth muscle. Journal of Physiology 484, 369-383.
    • (1995) Journal of Physiology , vol.484 , pp. 369-383
    • Österman, A.1    Arner, A.2
  • 43
    • 0030871067 scopus 로고    scopus 로고
    • The direct vasomotor effect of thyroid hormones on rat skeletal muscle resistance arteries
    • Park, K. W., Dai, H. B., Ojamaa, K., Lowenstein, E., Klein, I. & Sellke, F. W. (1997). The direct vasomotor effect of thyroid hormones on rat skeletal muscle resistance arteries. Anesthesia and Analgesia 85, 734-738.
    • (1997) Anesthesia and Analgesia , vol.85 , pp. 734-738
    • Park, K.W.1    Dai, H.B.2    Ojamaa, K.3    Lowenstein, E.4    Klein, I.5    Sellke, F.W.6
  • 44
    • 0017663263 scopus 로고
    • Force-velocity relations of the portal vein of hyperthyroid rats
    • Peiper, U. (1977). Force-velocity relations of the portal vein of hyperthyroid rats. Pflügers Archiv 372, 23-27.
    • (1977) Pflügers Archiv , vol.372 , pp. 23-27
    • Peiper, U.1
  • 45
    • 0031031962 scopus 로고    scopus 로고
    • An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms
    • Rovner, A. S., Freyzon, Y. & Trybus, K. M. (1997). An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms. Journal of Muscle Research and Cell Motility 18, 103-110.
    • (1997) Journal of Muscle Research and Cell Motility , vol.18 , pp. 103-110
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 48
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski, R. F., Wiseman, M. O. & White, H. D. (1985). ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proceedings of the National Academy of Sciences of the USA 82, 658-662.
    • (1985) Proceedings of the National Academy of Sciences of the USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 49
    • 0035038958 scopus 로고    scopus 로고
    • Increased expression of non-muscle myosin heavy chain-B in connective tissue cells of hypertrophic rat urinary bladder
    • Sjuve, R., Haase, H., Ekblad, E., Malmqvist, U., Morano, I. & Arner, A. (2001). Increased expression of non-muscle myosin heavy chain-B in connective tissue cells of hypertrophic rat urinary bladder. Cell and Tissue Research 304, 271-278.
    • (2001) Cell and Tissue Research , vol.304 , pp. 271-278
    • Sjuve, R.1    Haase, H.2    Ekblad, E.3    Malmqvist, U.4    Morano, I.5    Arner, A.6
  • 50
    • 0029739853 scopus 로고    scopus 로고
    • Contraction kinetics and myosin isoform composition in smooth muscle from hypertrophied rat urinary bladder
    • Sjuve, R., Haase, H., Morano, I., Uvelius, B. & Arner, A. (1996). Contraction kinetics and myosin isoform composition in smooth muscle from hypertrophied rat urinary bladder. Journal of Cellular Biochemistry 63, 86-93.
    • (1996) Journal of Cellular Biochemistry , vol.63 , pp. 86-93
    • Sjuve, R.1    Haase, H.2    Morano, I.3    Uvelius, B.4    Arner, A.5
  • 51
    • 0014386880 scopus 로고
    • Vascular smooth muscle. I. Normal structure, pathology, biochemistry, and biophysics
    • Somlyo, A. P. & Somlyo, A. V. (1968). Vascular smooth muscle. I. Normal structure, pathology, biochemistry, and biophysics. Pharmacological Reviews 20, 197-272.
    • (1968) Pharmacological Reviews , vol.20 , pp. 197-272
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 53
    • 0027223294 scopus 로고
    • Identification of a novel smooth muscle myosin heavy chain cDNA: Isoform diversity in the S1 head region
    • White, S., Martin, A. F. & Periasamy, M. (1993). Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region. American Journal of Physiology 264, C1252-1258.
    • (1993) American Journal of Physiology , vol.264
    • White, S.1    Martin, A.F.2    Periasamy, M.3


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