메뉴 건너뛰기




Volumn 86, Issue 3, 1999, Pages 1002-1008

Exercise-induced alterations in skeletal muscle myosin heavy chain phenotype: Dose-response relationship

Author keywords

Endurance exercise; Fiber type; Muscle plasticity; Oxidative capacity

Indexed keywords

CITRATE SYNTHASE; MYOSIN HEAVY CHAIN;

EID: 0032980433     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1999.86.3.1002     Document Type: Article
Times cited : (106)

References (35)
  • 1
    • 0022360239 scopus 로고
    • Rat muscle blood flows during high-speed locomotion
    • Armstrong, R. B., and M. H. Laughlin. Rat muscle blood flows during high-speed locomotion. J. Appl. Physiol. 59: 1322-1328, 1985.
    • (1985) J. Appl. Physiol. , vol.59 , pp. 1322-1328
    • Armstrong, R.B.1    Laughlin, M.H.2
  • 2
    • 0017363136 scopus 로고
    • Time course adaptations in cardiac and skeletal muscle to different running programs
    • Baldwin, K. M., D. A. Cooke, and W. G. Cheadle. Time course adaptations in cardiac and skeletal muscle to different running programs. J. Appl. Physiol. 42: 267-272, 1977.
    • (1977) J. Appl. Physiol. , vol.42 , pp. 267-272
    • Baldwin, K.M.1    Cooke, D.A.2    Cheadle, W.G.3
  • 3
    • 0023820311 scopus 로고
    • Three fast myosin heavy chains in adult rat skeletal muscle
    • Bar, A., and D. Pette. Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett. 235: 153-155, 1988.
    • (1988) FEBS Lett. , vol.235 , pp. 153-155
    • Bar, A.1    Pette, D.2
  • 4
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of shortening
    • Barany, M. ATPase activity of myosin correlated with speed of shortening. J. Gen. Physiol. 50: 197-216, 1967.
    • (1967) J. Gen. Physiol. , vol.50 , pp. 197-216
    • Barany, M.1
  • 5
    • 0023186436 scopus 로고
    • Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibers
    • Baumann, H., M. Jaggi, F. Soland, H. Howald, and M. C. Schaub. Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibers. Pflügers Arch. 409: 349-360, 1987.
    • (1987) Pflügers Arch. , vol.409 , pp. 349-360
    • Baumann, H.1    Jaggi, M.2    Soland, F.3    Howald, H.4    Schaub, M.C.5
  • 6
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, A. A rapid 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, A.1
  • 7
    • 0026655191 scopus 로고
    • Response of slow and fast muscle to hypothyroidism: Maximal shortening velocity and myosin isoforms
    • Cell Physiol. 32
    • Caiozzo, V. J., R. Herrick, and K. Baldwin. Response of slow and fast muscle to hypothyroidism: maximal shortening velocity and myosin isoforms. Am. J. Physiol. 263 (Cell Physiol. 32): C86-C94, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Caiozzo, V.J.1    Herrick, R.2    Baldwin, K.3
  • 8
    • 0015257535 scopus 로고
    • Dynamic properties of mammalian skeletal muscles
    • Close, R. I. Dynamic properties of mammalian skeletal muscles. Physiol. Rev. 52: 129-197, 1972.
    • (1972) Physiol. Rev. , vol.52 , pp. 129-197
    • Close, R.I.1
  • 9
    • 0019929103 scopus 로고
    • Influence of exercise intensity and duration on biochemical adaptations in skeletal muscle
    • Dudley, G. A., W. A. 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.A.2    Terjung, R.L.3
  • 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
  • 11
    • 0029689570 scopus 로고    scopus 로고
    • Muscle mechanics: Adaptation with exercise training
    • Fitts, R. H., and J. J. Widrick. Muscle mechanics: adaptation with exercise training. Exerc. Sport Sci. Rev. 24: 427-473, 1996.
    • (1996) Exerc. Sport Sci. Rev. , vol.24 , pp. 427-473
    • Fitts, R.H.1    Widrick, J.J.2
  • 12
    • 0025303456 scopus 로고
    • Effects of endurance exercise on isomyosin patterns in fast- and slow-twitch skeletal muscles
    • P.
    • Fitzsimons, D., P., G. M. Diffee, R. E. Herrick, and K. M. Baldwin. Effects of endurance exercise on isomyosin patterns in fast- and slow-twitch skeletal muscles. J. Appl. Physiol. 68: 1950-1955, 1990.
    • (1990) J. Appl. Physiol. , vol.68 , pp. 1950-1955
    • Fitzsimons, D.1    Diffee, G.M.2    Herrick, R.E.3    Baldwin, K.M.4
  • 13
    • 0016246130 scopus 로고
    • Selective glycogen depletion pattern in human skeletal muscle fibers after exercise of varying intensity and at varying pedalling rates
    • Gollnick, P. D., K. Piehl, and B. Saltin. Selective glycogen depletion pattern in human skeletal muscle fibers after exercise of varying intensity and at varying pedalling rates. J. Physiol. (Lond.) 241: 45-57, 1974.
    • (1974) J. Physiol. (Lond.) , vol.241 , pp. 45-57
    • Gollnick, P.D.1    Piehl, K.2    Saltin, B.3
  • 14
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret method
    • G.
    • Gornall, A., G., C. J. Bardawill, and M. M. David. Determination of serum proteins by means of the biuret method. J. Biol. Chem. 177: 751-756, 1949.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-756
    • Gornall, A.1    Bardawill, C.J.2    David, M.M.3
  • 15
    • 0021282213 scopus 로고
    • Exercise-induced fiber type transitions with regard to myosin, parvalbumin, and sarcoplasmic reticulum in muscles of the rat
    • Green, H. J., G. A. Klug, H. Reichmann, U. Seedorf, W. Wiehrer, and D. Pette. Exercise-induced fiber type transitions with regard to myosin, parvalbumin, and sarcoplasmic reticulum in muscles of the rat. Pflügers Arch. 400: 432-438, 1984.
    • (1984) Pflügers Arch. , vol.400 , pp. 432-438
    • Green, H.J.1    Klug, G.A.2    Reichmann, H.3    Seedorf, U.4    Wiehrer, W.5    Pette, D.6
  • 16
    • 0016888751 scopus 로고
    • Biochemical adaptations to endurance exercise in muscle
    • Holloszy, J. O., and F. W. Booth. Biochemical adaptations to endurance 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
  • 17
    • 0027201778 scopus 로고
    • Stimulation-induced expression of slow muscle myosin in a fast muscle of the rat-evidence of an unrestricted adaptive capacity
    • Mayne, C. N., T. M. Mokrusch, J. C. Jarvis, S. J. Gilroy, and S. Salmons. Stimulation-induced expression of slow muscle myosin in a fast muscle of the rat-evidence of an unrestricted adaptive capacity. FEBS Lett. 327: 297-300, 1993.
    • (1993) FEBS Lett. , vol.327 , pp. 297-300
    • Mayne, C.N.1    Mokrusch, T.M.2    Jarvis, J.C.3    Gilroy, S.J.4    Salmons, S.5
  • 18
    • 0029138892 scopus 로고
    • Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms
    • Moss, R., G. Diffee, and M. Greaser. Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms. Rev. Physiol. Biochem. Pharmacol. 126: 1-63, 1995.
    • (1995) Rev. Physiol. Biochem. Pharmacol. , vol.126 , pp. 1-63
    • Moss, R.1    Diffee, G.2    Greaser, M.3
  • 19
    • 0021661750 scopus 로고
    • Activity-induced fast to slow transitions in mammalian muscle
    • Pette, D. Activity-induced fast to slow transitions in mammalian muscle. Med. Sci. Sports Exerc. 16: 517-528, 1984.
    • (1984) Med. Sci. Sports Exerc. , vol.16 , pp. 517-528
    • Pette, D.1
  • 20
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transition
    • Pette, D., and R. S. Staron. Mammalian skeletal muscle fiber type transition. Int. Rev. Cytol. 170: 143-223, 1997.
    • (1997) Int. Rev. Cytol. , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 21
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation
    • Pette, D., and G. Vrbova. Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation. Rev. Physiol. Biochem. Pharmacol. 120: 115-202, 1992.
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 22
    • 0028331680 scopus 로고
    • Influence of exercise and fiber type on antioxidant enzyme activity in rat skeletal muscle
    • Regulatory Integrative Comp. Physiol. 35
    • Powers, S. K., D. Criswell, J. Lawler, D. Martin, L. L. Ji, R. A. Herb, and G. Dudley. Influence of exercise and fiber type on antioxidant enzyme activity in rat skeletal muscle. Am. J. Physiol. 266 (Regulatory Integrative Comp. Physiol. 35): R375-R380, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Powers, S.K.1    Criswell, D.2    Lawler, J.3    Martin, D.4    Ji, L.L.5    Herb, R.A.6    Dudley, G.7
  • 23
    • 0023065959 scopus 로고
    • Influence of exercise and training on motor unit activation
    • Sale, D. G. Influence of exercise and training on motor unit activation. Exerc. Sport Sci. Rev. 15: 95-15, 1987.
    • (1987) Exerc. Sport Sci. Rev. , vol.15 , pp. 95-115
    • Sale, D.G.1
  • 24
    • 0001887329 scopus 로고
    • The response of skeletal muscle to different patterns of use-some new development and concepts
    • edited by D. Pette. Berlin: de Gruyter
    • Salmons, S. The response of skeletal muscle to different patterns of use-some new development and concepts. In: Plasticity of Muscle, edited by D. Pette. Berlin: de Gruyter, 1980, p. 387-399.
    • (1980) Plasticity of Muscle , pp. 387-399
    • Salmons, S.1
  • 25
    • 0028294268 scopus 로고
    • Exercise, stimulation and type transformation of skeletal muscle
    • Salmons, S. Exercise, stimulation and type transformation of skeletal muscle. Int. J. Sports Med. 15: 136-141, 1994.
    • (1994) Int. J. Sports Med. , vol.15 , pp. 136-141
    • Salmons, S.1
  • 26
    • 0019470215 scopus 로고
    • The adaptive response of skeletal muscle to increased use
    • Salmons, S., and J. Henriksson. The adaptive response of skeletal muscle to increased use. Muscle Nerve 4: 94-105, 1981.
    • (1981) Muscle Nerve , vol.4 , pp. 94-105
    • Salmons, S.1    Henriksson, J.2
  • 27
    • 85047670871 scopus 로고
    • The mATPase histochemical profile of rat type IIX fibers; Correlation with myosin heavy chain immunolabeling
    • Santa'ana Pereira, J. A. A., A. De Haan, A. Wessels, A. F. M. Moorman, and A. J. Sargeant. The mATPase histochemical profile of rat type IIX fibers; correlation with myosin heavy chain immunolabeling. Histochem. J. 27: 715-722, 1995.
    • (1995) Histochem. J. , vol.27 , pp. 715-722
    • Santa'ana Pereira, J.A.A.1    De Haan, A.2    Wessels, A.3    Moorman, A.F.M.4    Sargeant, A.J.5
  • 28
    • 0028060295 scopus 로고
    • Myosin isoforms in mammalian skeletal muscle
    • Schiaffino, S., and C. Reggiani. Myosin isoforms in mammalian skeletal muscle. J. Appl. Physiol. 77: 493-501, 1994.
    • (1994) J. Appl. Physiol. , vol.77 , pp. 493-501
    • Schiaffino, S.1    Reggiani, C.2
  • 29
    • 0015213029 scopus 로고
    • The purification of cardiac myofibrils with Triton X-100
    • Solaro, R. J., D. C. Pang, and F. N. Briggs. The purification of cardiac myofibrils with Triton X-100. Biochim. Biophys. Acta 245: 259-262, 1971.
    • (1971) Biochim. Biophys. Acta , vol.245 , pp. 259-262
    • Solaro, R.J.1    Pang, D.C.2    Briggs, F.N.3
  • 30
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere, P. Citrate synthase. Methods Enzymol. 13: 3-5, 1969.
    • (1969) Methods Enzymol. , vol.13 , pp. 3-5
    • Srere, P.1
  • 31
    • 0023237796 scopus 로고
    • Myosin polymorphism in single fibers of chronically stimulated rabbit fast-twitch muscle
    • Staron, R. S., B. Gohlsch, and D. Pette. Myosin polymorphism in single fibers of chronically stimulated rabbit fast-twitch muscle. Pflügers Arch. 408: 444-450, 1987.
    • (1987) Pflügers Arch. , vol.408 , pp. 444-450
    • Staron, R.S.1    Gohlsch, B.2    Pette, D.3
  • 32
    • 0029055695 scopus 로고
    • Myosin heavy chain composition in young and old rat skeletal muscle: Effects of endurance exercise
    • Sullivan, V., S. Powers, D. Criswell, N. Turner, J. LaRochelle, and D. Lowenthal. Myosin heavy chain composition in young and old rat skeletal muscle: effects of endurance exercise. J. Appl. Physiol. 78: 2115-2120, 1995.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 2115-2120
    • Sullivan, V.1    Powers, S.2    Criswell, D.3    Turner, N.4    LaRochelle, J.5    Lowenthal, D.6
  • 33
    • 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
  • 34
    • 0026537505 scopus 로고
    • Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle
    • Termin, A., and D. Pette. Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle. Eur. J. Biochem. 204: 569-573, 1992.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 569-573
    • Termin, A.1    Pette, D.2
  • 35
    • 0024802588 scopus 로고
    • Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles: A single-fiber study
    • Termin, A., R. S. Staron, and D. Pette. Changes in myosin heavy chain isoforms during chronic low-frequency stimulation of rat fast hindlimb muscles: a single-fiber study. Eur. J. Biochem, 186: 749-754, 1989.
    • (1989) Eur. J. Biochem , vol.186 , pp. 749-754
    • Termin, A.1    Staron, R.S.2    Pette, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.