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Volumn 270, Issue 4 39-4, 1996, Pages

β-MHC and SMLC1 transgene induction in overloaded skeletal muscle of transgenic mice

Author keywords

chloramphenicol acetyltransferase; fiber type; gene expression; hypertrophy; mechanical overload

Indexed keywords

CHLORAMPHENICOL ACETYLTRANSFERASE; MESSENGER RNA; MYOSIN ADENOSINE TRIPHOSPHATASE ISOENZYME; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; TROPONIN C;

EID: 0029866259     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1996.270.4.c1111     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • Barany, M. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 5: 197-218, 1967.
    • (1967) J. Gen. Physiol. , vol.5 , pp. 197-218
    • Barany, M.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0026534294 scopus 로고
    • Making muscle in mammals
    • Buckingham, M. Making muscle in mammals. Trends Genet. 8: 144-148, 1992.
    • (1992) Trends Genet. , vol.8 , pp. 144-148
    • Buckingham, M.1
  • 4
    • 0028898228 scopus 로고
    • Regulation of skeletal α-actin promoter in young chickens during hypertrophy caused by stretch overload
    • Cell Physiol. 37
    • Carson, J. A., Z. Yan, F. W. Booth, M. E. Coleman, R. J. Schwartz, and C. S. Stump. Regulation of skeletal α-actin promoter in young chickens during hypertrophy caused by stretch overload. Am. J. Physiol. 268 (Cell Physiol. 37): C918-C924, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Carson, J.A.1    Yan, Z.2    Booth, F.W.3    Coleman, M.E.4    Schwartz, R.J.5    Stump, C.S.6
  • 5
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 6
    • 0019836421 scopus 로고
    • Structure and variation of human ribosomal DNA: Molecular analysis of cloned fragments
    • Erickson, J. M., C. L. Rushford, D. J. Dorney, G. N. Wilson, and R. D. Schmickel. Structure and variation of human ribosomal DNA: molecular analysis of cloned fragments. Gene 16: 1-9, 1981.
    • (1981) Gene , vol.16 , pp. 1-9
    • Erickson, J.M.1    Rushford, C.L.2    Dorney, D.J.3    Wilson, G.N.4    Schmickel, R.D.5
  • 7
    • 0026722533 scopus 로고
    • Characterization of a strong positive cis-acting element of the human β-myosin heavy chain gene in fetal rat heart cells
    • Flink, R. L., J. G. Edwards, J. J. Bahl, C.-C. Liew, M. Sole, and E. Morken. Characterization of a strong positive cis-acting element of the human β-myosin heavy chain gene in fetal rat heart cells. J. Biol. Chem. 267: 9917-9924, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9917-9924
    • Flink, R.L.1    Edwards, J.G.2    Bahl, J.J.3    Liew, C.-C.4    Sole, M.5    Morken, E.6
  • 8
    • 0022508019 scopus 로고
    • Increased EMG of rat plantaris during locomotion following surgical removal of its synergists
    • Gardiner, P. F., R. N. Michel, F. Browman, and E. Nobel. Increased EMG of rat plantaris during locomotion following surgical removal of its synergists. Brain Res. 380: 114-121, 1986.
    • (1986) Brain Res. , vol.380 , pp. 114-121
    • Gardiner, P.F.1    Michel, R.N.2    Browman, F.3    Nobel, E.4
  • 9
    • 0027327708 scopus 로고
    • Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones
    • Hughes, S. M., J. M. Taylor, S. J. Tapscott, C. M. Gurley, W. J. Carter, and C. A. Peterson. Selective accumulation of MyoD and myogenin mRNAs in fast and slow adult skeletal muscle is controlled by innervation and hormones. Development 118: 1137-1147, 1993.
    • (1993) Development , vol.118 , pp. 1137-1147
    • Hughes, S.M.1    Taylor, J.M.2    Tapscott, S.J.3    Gurley, C.M.4    Carter, W.J.5    Peterson, C.A.6
  • 10
    • 0028217492 scopus 로고
    • Skeletal muscle overload upregulates the sarcoplasmic reticulum slow calcium pump gene
    • Cell Physiol. 35
    • Kandarian, S. C., D. G. Peters, J. A. Taylor, and J. H. Williams. Skeletal muscle overload upregulates the sarcoplasmic reticulum slow calcium pump gene. Am. J. Physiol. 266 (Cell Physiol. 35): C1190-C1197, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Kandarian, S.C.1    Peters, D.G.2    Taylor, J.A.3    Williams, J.H.4
  • 11
    • 0028095108 scopus 로고
    • 1-adrenergic agonist and activated β-protein kinase C in hypertrophy of cardiac myocytes
    • 1-adrenergic agonist and activated β-protein kinase C in hypertrophy of cardiac myocytes. J. Biol. Chem. 269: 3775-3782, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3775-3782
    • Kariya, K.-I.1    Karns, L.R.2    Simpson, P.C.3
  • 12
    • 0028889199 scopus 로고
    • 1-adrenergic induction of the skeletal α-actin promoter during cardiac myocyte hypertrophy
    • 1-adrenergic induction of the skeletal α-actin promoter during cardiac myocyte hypertrophy. J. Biol. Chem. 270: 410-417, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 410-417
    • Karns, L.R.1    Kariya, K.-I.2    Simpson, P.C.3
  • 13
    • 0000704627 scopus 로고
    • Introduction of DNA into mammalian cells
    • edited by F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. New York: Wiley
    • Kingston, R. E., and J. Sheen. Introduction of DNA into mammalian cells. In: Current Protocol in Molecular Biology, edited by F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. New York: Wiley, 1989, p. 9.7.10.
    • (1989) Current Protocol in Molecular Biology
    • Kingston, R.E.1    Sheen, J.2
  • 14
    • 0027960578 scopus 로고
    • In vivo regulation in the mouse β-myosin heavy chain gene
    • Knotts, S., H. Rindt, J. Neumann, and J. Robbins. In vivo regulation in the mouse β-myosin heavy chain gene. J. Biol. Chem. 269: 31275-31282, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31275-31282
    • Knotts, S.1    Rindt, H.2    Neumann, J.3    Robbins, J.4
  • 15
    • 0027426228 scopus 로고
    • Skeletal muscle light chains are essential for physiological speeds of shortening
    • Lowey, S., G. S. Waller, and K. Trybus. Skeletal muscle light chains are essential for physiological speeds of shortening. Nature Lond. 365: 454-456, 1993.
    • (1993) Nature Lond. , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.3
  • 16
    • 0027305413 scopus 로고
    • Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay
    • Lowey, S., G. S. Waller, and K. M. Trybus. Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. J. Biol. Chem. 268: 20414-20418, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20414-20418
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 17
    • 0024841107 scopus 로고
    • Molecular basis of cardiac performance
    • Nadal-Ginard, B., and V. Mahdavi. Molecular basis of cardiac performance. J. Clin. Invest. 84: 1693-1700, 1989.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1693-1700
    • Nadal-Ginard, B.1    Mahdavi, V.2
  • 18
    • 0024832399 scopus 로고
    • Appearance of transitional motor units in overloaded rat skeletal muscle
    • Noble, R. G., and F. P. Pettigrew. Appearance of transitional motor units in overloaded rat skeletal muscle. J. Appl. Physiol. 67: 2049-2054, 1989.
    • (1989) J. Appl. Physiol. , vol.67 , pp. 2049-2054
    • Noble, R.G.1    Pettigrew, F.P.2
  • 20
    • 0026589213 scopus 로고
    • Structural and developmental analysis of two linked myosin heavy chain genes
    • Parker-Thornburg, J., B. Bauer, J. Palermo, and J. Robbins. Structural and developmental analysis of two linked myosin heavy chain genes. Dev. Biol. 150: 99-107, 1992.
    • (1992) Dev. Biol. , vol.150 , pp. 99-107
    • Parker-Thornburg, J.1    Bauer, B.2    Palermo, J.3    Robbins, J.4
  • 21
    • 0025142936 scopus 로고
    • The structure and regulation of expression of the murine fast skeletal troponin C gene
    • Parmacek, M. S., A. R. Bengur, A. J. Vora, and J. M. Leiden. The structure and regulation of expression of the murine fast skeletal troponin C gene. J. Biol. Chem. 265: 15970-15976, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15970-15976
    • Parmacek, M.S.1    Bengur, A.R.2    Vora, A.J.3    Leiden, J.M.4
  • 22
    • 0024333264 scopus 로고
    • Structure and expression of the murine slow/cardiac troponin C gene
    • Parmacek, M. S., and J. M. Leiden. Structure and expression of the murine slow/cardiac troponin C gene. J. Biol. Chem. 264: 13217-13225, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13217-13225
    • Parmacek, M.S.1    Leiden, J.M.2
  • 23
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation
    • Pette, D., and G. Vrbove. Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev. Physiol. Biochem. Pharmacol. 120: 116-202, 1992.
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.120 , pp. 116-202
    • Pette, D.1    Vrbove, G.2
  • 24
    • 0022252990 scopus 로고
    • Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition
    • Reiser, P. J., G. Moss, G. Giulian, and M. L. Greaser. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J. Biol. Chem. 260: 9077-9080, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9077-9080
    • Reiser, P.J.1    Moss, G.2    Giulian, G.3    Greaser, M.L.4
  • 25
    • 0027499946 scopus 로고
    • In vivo analysis of the murine β-myosin heavy chain gene promoter
    • Rindt, H., J. Gulick, S. Knotts, J. Neumann, and J. Robbins. In vivo analysis of the murine β-myosin heavy chain gene promoter. J. Biol. Chem. 268: 5332-5338, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5332-5338
    • Rindt, H.1    Gulick, J.2    Knotts, S.3    Neumann, J.4    Robbins, J.5
  • 26
    • 0022257888 scopus 로고
    • Biochemical and physiological changes in overloaded rat fast- and slow-twitch ankle extensors
    • Roy, R. R., K. M. Baldwin, T. P. Martin, S. P. Chimarusti, and V. R. Edgerton. Biochemical and physiological changes in overloaded rat fast- and slow-twitch ankle extensors. J. Appl. Physiol. 59: 639-646, 1985.
    • (1985) J. Appl. Physiol. , vol.59 , pp. 639-646
    • Roy, R.R.1    Baldwin, K.M.2    Martin, T.P.3    Chimarusti, S.P.4    Edgerton, V.R.5
  • 27
    • 0026530913 scopus 로고
    • Both muscle-specific and ubiquitous nuclear factors are required for muscle-specific expression of the myosin heavy-chain β-gene in cultured cells
    • Shimizu, N., E. Dizon, and R. Zak. Both muscle-specific and ubiquitous nuclear factors are required for muscle-specific expression of the myosin heavy-chain β-gene in cultured cells. Mol. Cell. Biol. 12: 619-630, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 619-630
    • Shimizu, N.1    Dizon, E.2    Zak, R.3
  • 28
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98: 503-517, 1975.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 29
    • 0023905464 scopus 로고
    • Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers
    • Sweeny, L. H., M. J. Kushmerick, and K. Mabuchi. Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. J. Biol. Chem. 2263: 9034-9039, 1988.
    • (1988) J. Biol. Chem. , vol.2263 , pp. 9034-9039
    • Sweeny, L.H.1    Kushmerick, M.J.2    Mabuchi, K.3
  • 30
    • 0022542030 scopus 로고
    • Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscle
    • Swynghedauw, B. Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscle. Physiol. Rev. 66: 710-771, 1986.
    • (1986) Physiol. Rev. , vol.66 , pp. 710-771
    • Swynghedauw, B.1
  • 31
    • 0027452352 scopus 로고
    • Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
    • Talmadge, R. J., and R. R. Roy. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75: 2337-2340, 1993.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 2337-2340
    • Talmadge, R.J.1    Roy, R.R.2
  • 32
    • 0025889701 scopus 로고
    • A MyoD1-independent muscle-specific enhancer controls the expres-sion of the β-myosin heavy chain gene in skeletal and cardiac muscle cells
    • Thompson, W. R., B. Nadal-Ginard, and V. Mahdavi. A MyoD1-independent muscle-specific enhancer controls the expres-sion of the β-myosin heavy chain gene in skeletal and cardiac muscle cells. J. Biol. Chem. 266: 22678-22688, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22678-22688
    • Thompson, W.R.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 33
    • 0025647623 scopus 로고
    • Evaluation of animal models for the study of exercise-induced muscle enlargement
    • Timson, B. F. Evaluation of animal models for the study of exercise-induced muscle enlargement. J. Appl. Physiol. 69: 1935-1945, 1990.
    • (1990) J. Appl. Physiol. , vol.69 , pp. 1935-1945
    • Timson, B.F.1
  • 34
    • 0021888719 scopus 로고
    • Fiber number, area, and composition of mouse soleus muscle following enlargement
    • Timson, B. F., B. K. Bowlin, G. A. Dudenhoeffer, and J. B. George. Fiber number, area, and composition of mouse soleus muscle following enlargement. J. Appl. Physiol. 58: 619-624, 1985.
    • (1985) J. Appl. Physiol. , vol.58 , pp. 619-624
    • Timson, B.F.1    Bowlin, B.K.2    Dudenhoeffer, G.A.3    George, J.B.4
  • 35
    • 0028317209 scopus 로고
    • Transgenic animal models
    • Tsika, R. W. Transgenic animal models. Exercise Sports Sci. Rev. 22: 361-388, 1994.
    • (1994) Exercise Sports Sci. Rev. , vol.22 , pp. 361-388
    • Tsika, R.W.1
  • 36
    • 0025023535 scopus 로고
    • Thyroid hormone regulates expression of a transfected human α-myosin heavy-chain fusion gene in fetal rat heart cells
    • Tsika, R. W., J. J. Bahl, L. A. Leinwand, and E. Morkin. Thyroid hormone regulates expression of a transfected human α-myosin heavy-chain fusion gene in fetal rat heart cells. Proc. Natl. Acad. Sci. USA 87: 379-383, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 379-383
    • Tsika, R.W.1    Bahl, J.J.2    Leinwand, L.A.3    Morkin, E.4
  • 37
    • 15844383358 scopus 로고
    • Metabolic and contractile protein adaptations in response to increased mechanical loading
    • edited by R. J. Manahan. Champaign, IL: Human Kinetics, Biochem. Exer. IX Conf. Proc.
    • Tsika, R. W., and L. Gao. Metabolic and contractile protein adaptations in response to increased mechanical loading. In: Biochemistry of Exercise. 9th International Conference on Biochemistry of Exercise, edited by R. J. Manahan. Champaign, IL: Human Kinetics, 1994. (Biochem. Exer. IX Conf. Proc.).
    • (1994) Biochemistry of Exercise. 9th International Conference on Biochemistry of Exercise
    • Tsika, R.W.1    Gao, L.2
  • 38
    • 0029131783 scopus 로고
    • M-creatine kinase gene expression in mechanically overloaded skeletal muscle of transgenic mice
    • Cell Physiol. 38
    • Tsika, R. W., S. D. Hauschka, and L. Gao. M-creatine kinase gene expression in mechanically overloaded skeletal muscle of transgenic mice. Am. J. Physiol. 269 (Cell Physiol. 38): C665-C674, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Tsika, R.W.1    Hauschka, S.D.2    Gao, L.3
  • 39
    • 0023217411 scopus 로고
    • Interaction of compensatory overload and hindlimb suspension on myosin isoform expression
    • Tsika, R. W., B. Herrick, and K. M. Baldwin. Interaction of compensatory overload and hindlimb suspension on myosin isoform expression. J. Appl. Physiol. 62: 2180-2186, 1987.
    • (1987) J. Appl. Physiol. , vol.62 , pp. 2180-2186
    • Tsika, R.W.1    Herrick, B.2    Baldwin, K.M.3
  • 40
    • 0023608028 scopus 로고
    • Time course adaptations in rat skeletal muscle isomyosins during compensatory growth and regression
    • Tsika, R. W., R. Herrick, and K. M. Baldwin. Time course adaptations in rat skeletal muscle isomyosins during compensatory growth and regression. J. Appl. Physiol. 63: 2111-2121, 1987.
    • (1987) J. Appl. Physiol. , vol.63 , pp. 2111-2121
    • Tsika, R.W.1    Herrick, R.2    Baldwin, K.M.3
  • 42
    • 0027722905 scopus 로고
    • Differential expression of muscle regulatory factor genes in normal and denervated adult rat hindlimb muscles
    • Voytik, S. L., M. Przyborski, S. F. Badylak, and S. F. Konieczny. Differential expression of muscle regulatory factor genes in normal and denervated adult rat hindlimb muscles. Dev. Dyn. 198: 214-224, 1993.
    • (1993) Dev. Dyn. , vol.198 , pp. 214-224
    • Voytik, S.L.1    Przyborski, M.2    Badylak, S.F.3    Konieczny, S.F.4
  • 43
    • 0029047267 scopus 로고
    • Inactivation of the myogenic bHLH gene MRF4 results in up-regulation in myogenin and rib anomalies
    • Zhang, W., R. R. Behringer, and E. N. Olson. Inactivation of the myogenic bHLH gene MRF4 results in up-regulation in myogenin and rib anomalies. Genes Dev. 9: 1388-1399, 1995.
    • (1995) Genes Dev. , vol.9 , pp. 1388-1399
    • Zhang, W.1    Behringer, R.R.2    Olson, E.N.3


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