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Volumn 81, Issue 5, 1996, Pages 1941-1945

Cytochrome c mRNA in skeletal muscles of immobilized limbs

Author keywords

atrophy; gene expression; mitochondria

Indexed keywords

CYTOCHROME C; MESSENGER RNA; MUSCLE PROTEIN;

EID: 0029849218     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1996.81.5.1941     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0025142634 scopus 로고
    • Muscular atrophy following immobilization. A review
    • Appell, H.-J. Muscular atrophy following immobilization. A review. Sports Med. 10: 42-58, 1990.
    • (1990) Sports Med. , vol.10 , pp. 42-58
    • Appell, H.-J.1
  • 2
    • 0023893243 scopus 로고
    • α-Actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle
    • Cell Physiol. 23
    • Babij, P., and F. W. Booth. α-Actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle. Am. J. Physiol. 254 (Cell Physiol. 23): C651-C656, 1988.
    • (1988) Am. J. Physiol. , vol.254
    • Babij, P.1    Booth, F.W.2
  • 3
    • 0017748593 scopus 로고
    • Time course of muscular atrophy during immobilization of hindlimbs in rats
    • Booth, F. W. Time course of muscular atrophy during immobilization of hindlimbs in rats. J. Appl. Physiol. 43: 656-661, 1977.
    • (1977) J. Appl. Physiol. , vol.43 , pp. 656-661
    • Booth, F.W.1
  • 4
    • 0019976871 scopus 로고
    • Effect of limb immobilization on skeletal muscle
    • Booth, F. W. Effect of limb immobilization on skeletal muscle. J. Appl. Physiol. 52: 1113-1118, 1982.
    • (1982) J. Appl. Physiol. , vol.52 , pp. 1113-1118
    • Booth, F.W.1
  • 5
    • 0015597764 scopus 로고
    • Production of rat muscle atrophy
    • Booth, F. W., and J. R. Kelso. Production of rat muscle atrophy. J. Appl. Physiol. 34: 404-406, 1973.
    • (1973) J. Appl. Physiol. , vol.34 , pp. 404-406
    • Booth, F.W.1    Kelso, J.R.2
  • 6
    • 0025782887 scopus 로고
    • Molecular and cellular adaptation of muscle in response to exercise. Perspectives of various models
    • Booth, F. W., and D. B. Thomason. Molecular and cellular adaptation of muscle in response to exercise. Perspectives of various models. Physiol. Rev. 71: 541-585, 1991.
    • (1991) Physiol. Rev. , vol.71 , pp. 541-585
    • Booth, F.W.1    Thomason, D.B.2
  • 7
    • 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
  • 8
    • 0019929103 scopus 로고
    • Influence of exercise intensity and duration on biochemical adaptations in skeletal muscle
    • Dudley, G. A., W. M. Abraham, and R. L. Terjung. Influence of exercise intensity and duration on biochemical adaptations in skeletal muscle. J. Appl. Physiol. 53: 844-850, 1982.
    • (1982) J. Appl. Physiol. , vol.53 , pp. 844-850
    • Dudley, G.A.1    Abraham, W.M.2    Terjung, R.L.3
  • 9
    • 0023746896 scopus 로고
    • Both upstream and intron sequence elements are required for elevated expression of the rat somatic cytochrome c gene in COS-1 cells
    • Evans, M. J., and R. C. Scarpulla. Both upstream and intron sequence elements are required for elevated expression of the rat somatic cytochrome c gene in COS-1 cells. Mol. Cell. Biol. 8: 35-41, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 35-41
    • Evans, M.J.1    Scarpulla, R.C.2
  • 10
    • 0016795518 scopus 로고
    • Skeletal muscle respiratory capacity, endurance and glycogen utilization
    • Fitts, R. H., F. W. Booth, W. W. Winder, and J. O. Holloszy. Skeletal muscle respiratory capacity, endurance and glycogen utilization. Am. J. Physiol. 228: 1029-1033, 1975.
    • (1975) Am. J. Physiol. , vol.228 , pp. 1029-1033
    • Fitts, R.H.1    Booth, F.W.2    Winder, W.W.3    Holloszy, J.O.4
  • 12
    • 0017348727 scopus 로고
    • The influence of immobilization and stretch on protein turnover of rat skeletal muscle
    • Goldspink, D. F. The influence of immobilization and stretch on protein turnover of rat skeletal muscle. J. Physiol. Lond. 264: 267-282, 1977.
    • (1977) J. Physiol. Lond. , vol.264 , pp. 267-282
    • Goldspink, D.F.1
  • 14
    • 0021824219 scopus 로고
    • Quantitative evaluation of electromyogram activity in rat extensor and flexor muscles immobilized at different lengths
    • Hník, P., R. Vejsada, D. F. Goldspink, S. Kasicki, and I. Krekule. Quantitative evaluation of electromyogram activity in rat extensor and flexor muscles immobilized at different lengths. Exp. Neurol. 88: 515-528, 1985.
    • (1985) Exp. Neurol. , vol.88 , pp. 515-528
    • Hník, P.1    Vejsada, R.2    Goldspink, D.F.3    Kasicki, S.4    Krekule, I.5
  • 15
    • 0016888751 scopus 로고
    • Biochemical adaptations to exercise in muscle
    • Holloszy, J. O., and F. W. Booth. Biochemical adaptations to exercise in muscle. Annu. Rev. Physiol. 38: 273-291, 1976.
    • (1976) Annu. Rev. Physiol. , vol.38 , pp. 273-291
    • Holloszy, J.O.1    Booth, F.W.2
  • 16
    • 0021343295 scopus 로고
    • Adaptations of skeletal muscle to endurance exercise and their metabolic consequences
    • Holloszy, J. O., and E. F. Coyle. Adaptations of skeletal muscle to endurance exercise and their metabolic consequences. J. Appl. Physiol. 56: 831-839, 1984.
    • (1984) J. Appl. Physiol. , vol.56 , pp. 831-839
    • Holloszy, J.O.1    Coyle, E.F.2
  • 17
    • 0020528284 scopus 로고
    • The effect of limb immobilization on muscle function and protein composition
    • Jokl, P., and S. Konstadt. The effect of limb immobilization on muscle function and protein composition. Clin. Orthop. Clin. Orthop. Rel. Res. 174: 222-229, 1983.
    • (1983) Clin. Orthop. Clin. Orthop. Rel. Res. , vol.174 , pp. 222-229
    • Jokl, P.1    Konstadt, S.2
  • 19
    • 0023153987 scopus 로고
    • Cytochrome c protein-synthesis rates and mRNA contents during atrophy and recovery in skeletal muscle
    • Morrison, P. R., J. A. Montgomery, T. S. Wong, and F. W. Booth. Cytochrome c protein-synthesis rates and mRNA contents during atrophy and recovery in skeletal muscle. Biochem. J. 241: 257-263, 1987.
    • (1987) Biochem. J. , vol.241 , pp. 257-263
    • Morrison, P.R.1    Montgomery, J.A.2    Wong, T.S.3    Booth, F.W.4
  • 21
    • 10544240418 scopus 로고
    • Knee rehabilitation after knee ligament injury and surgery
    • edited by W. N. Scott. St. Louis, MO: Mosby
    • Paulos, L. E. Knee rehabilitation after knee ligament injury and surgery. In: The Knee, edited by W. N. Scott. St. Louis, MO: Mosby, 1994, p. 945.
    • (1994) The Knee , pp. 945
    • Paulos, L.E.1
  • 22
    • 0016153749 scopus 로고
    • Substrate utilization in disused rat skeletal muscles
    • Riffenberick, D. H., and S. R. Max. Substrate utilization in disused rat skeletal muscles. Am. J. Physiol. 226: 295-297, 1974.
    • (1974) Am. J. Physiol. , vol.226 , pp. 295-297
    • Riffenberick, D.H.1    Max, S.R.2
  • 25
    • 0019407867 scopus 로고
    • Isolation and structure of a rat cytochrome c gene
    • Scarpulla, R. C., K. M. Agne, and R. Wu. Isolation and structure of a rat cytochrome c gene. J. Biol. Chem. 256: 6480-6486, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6480-6486
    • Scarpulla, R.C.1    Agne, K.M.2    Wu, R.3
  • 26
    • 0019917907 scopus 로고
    • Contractile properties of rat hind limb muscles immobilized at different lengths
    • Simard, C. P., S. A. Spector, and V. R. Edgerton. Contractile properties of rat hind limb muscles immobilized at different lengths. Exp. Neurol. 77: 467-482, 1982.
    • (1982) Exp. Neurol. , vol.77 , pp. 467-482
    • Simard, C.P.1    Spector, S.A.2    Edgerton, V.R.3
  • 27
    • 0020031623 scopus 로고
    • Architectural alterations of rat hind-limb skeletal muscles immobilized at different lengths
    • Spector, S. A., C. P. Simard, M. Fournier, E. Sternlicht, and V. R. Edgerton. Architectural alterations of rat hind-limb skeletal muscles immobilized at different lengths. Exp. Neurol. 76: 94-110, 1982.
    • (1982) Exp. Neurol. , vol.76 , pp. 94-110
    • Spector, S.A.1    Simard, C.P.2    Fournier, M.3    Sternlicht, E.4    Edgerton, V.R.5
  • 28
    • 0000526734 scopus 로고
    • Effect of immobilization in various positions upon the weight and strength of skeletal muscle
    • Summers, T. B., and H. M. Hines. Effect of immobilization in various positions upon the weight and strength of skeletal muscle. Arch. Phys. Med. Rehabil. 32: 142-145, 1951.
    • (1951) Arch. Phys. Med. Rehabil. , vol.32 , pp. 142-145
    • Summers, T.B.1    Hines, H.M.2
  • 29
    • 0000134497 scopus 로고
    • Changes of weight and neuromuscular transmission in muscles of immobilized joints
    • Thomsen, P., and J. V. Luco. Changes of weight and neuromuscular transmission in muscles of immobilized joints. J. Neurophysiol. 7: 245-251, 1944.
    • (1944) J. Neurophysiol. , vol.7 , pp. 245-251
    • Thomsen, P.1    Luco, J.V.2
  • 31
    • 0020570217 scopus 로고
    • Effect of hindlimb immobilization on the fatigability of skeletal muscle
    • Witzmann, F. A., D. H. Kim, and R. H. Fitts. Effect of hindlimb immobilization on the fatigability of skeletal muscle. J. Appl. Physiol. 54: 1242-1248, 1983.
    • (1983) J. Appl. Physiol. , vol.54 , pp. 1242-1248
    • Witzmann, F.A.1    Kim, D.H.2    Fitts, R.H.3
  • 32
    • 0029862518 scopus 로고    scopus 로고
    • Increased contractile activity decreases RNA-protein interaction in the 3′-UTR of cytochrome c mRNA
    • Cell Physiol. 40
    • Yan, Z., S. Salmons, Y. L. Dang, M. T. Hamilton, and F. W. Booth. Increased contractile activity decreases RNA-protein interaction in the 3′-UTR of cytochrome c mRNA. Am. J. Physiol. 271 (Cell Physiol. 40): C1157-C1166, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Yan, Z.1    Salmons, S.2    Dang, Y.L.3    Hamilton, M.T.4    Booth, F.W.5
  • 33
    • 0028936548 scopus 로고
    • Increased muscle carnitine palmitoyltransferase II mRNA after increased contractile activity
    • Endocrinol. Metab. 31
    • Yan, Z., S. Salmons, J. Jarvis, and F. W. Booth. Increased muscle carnitine palmitoyltransferase II mRNA after increased contractile activity. Am. J. Physiol. 268 (Endocrinol. Metab. 31): E277-E281, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Yan, Z.1    Salmons, S.2    Jarvis, J.3    Booth, F.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.