메뉴 건너뛰기




Volumn 40, Issue 4, 2002, Pages 362-369

Effects of pH and temperature on force and stiffness of skeletal muscle fibers during contraction and relaxation in relation to musculoskeletal disorders

Author keywords

Force; PH; Skeletal muscle; Stiffness; Temperature

Indexed keywords

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FEMALE; MUSCLE CONTRACTION; MUSCLE FORCE; MUSCLE INJURY; MUSCLE STIFFNESS; MUSCULOSKELETAL DISEASE; NONHUMAN; PH; PSOAS MUSCLE; RABBIT; SOLEUS MUSCLE; TEMPERATURE;

EID: 0036808809     PISSN: 00198366     EISSN: None     Source Type: Journal    
DOI: 10.2486/indhealth.40.362     Document Type: Article
Times cited : (3)

References (24)
  • 1
    • 0030920790 scopus 로고    scopus 로고
    • A new trend in the study of low back pain in workplaces
    • Yamamoto S (1997) A new trend in the study of low back pain in workplaces. Ind Health 35, 173-85.
    • (1997) Ind Health , vol.35 , pp. 173-185
    • Yamamoto, S.1
  • 2
    • 0032759034 scopus 로고    scopus 로고
    • Association between musculoskeletal pain in Japanese construction workers and job, age, alcohol consumption, and smoking
    • Ueno S, Hisanaga N, Jonai H, Shibata E, Kamijima M (1999) Association between musculoskeletal pain in Japanese construction workers and job, age, alcohol consumption, and smoking. Ind Health 37, 449-56.
    • (1999) Ind Health , vol.37 , pp. 449-456
    • Ueno, S.1    Hisanaga, N.2    Jonai, H.3    Shibata, E.4    Kamijima, M.5
  • 5
    • 0026149394 scopus 로고
    • 31P-MRS study of change in intracellular pH during sustained static contraction in Human Ann
    • 31P-MRS study of change in intracellular pH during sustained static contraction in Human Ann. Physiol Anthrop 10 (2) 83-90.
    • (1991) Physiol Anthrop , vol.10 , Issue.2 , pp. 83-90
    • Iwanaga, K.1    Yoshimitsu, H.2    Kamata, T.3    Sairyo, K.4
  • 6
    • 0020352953 scopus 로고
    • Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres An electrophoretic study of single fibres
    • Salviati G, Betto R, Danieli Betto D (1982) Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres An electrophoretic study of single fibres. Biochem J 207, 261-72.
    • (1982) Biochem J , vol.207 , pp. 261-272
    • Salviati, G.1    Betto, R.2    Danieli Betto, D.3
  • 7
    • 0016357627 scopus 로고
    • The elastic property of the frog skinned muscle fibre
    • Umazume Y (1974) The elastic property of the frog skinned muscle fibre. Jikei Med J 21, 11-24.
    • (1974) Jikei Med J , vol.21 , pp. 11-24
    • Umazume, Y.1
  • 8
    • 0021723069 scopus 로고
    • Fine structures in the light diffraction pattern of striated muscle
    • Leung AF (1984) Fine structures in the light diffraction pattern of striated muscle. J Muscle Res Cell Motil 5, 535-58.
    • (1984) J Muscle Res Cell Motil , vol.5 , pp. 535-558
    • Leung, A.F.1
  • 10
    • 0019390452 scopus 로고
    • The relation between stiffness and filament overlap in stimulated frog muscle fibres
    • Ford LE, Huxley AF, Simmons RM (1981) The relation between stiffness and filament overlap in stimulated frog muscle fibres. Journal of Physiology 311, 219-49.
    • (1981) Journal of Physiology , vol.311 , pp. 219-249
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 11
    • 0019946678 scopus 로고
    • Muscular contraction: Kinetics of crossbridge attachment studied by high-frequency stiffness measurements
    • Cecchi G, Griffiths PJ, Taylor S (1982) Muscular contraction: Kinetics of crossbridge attachment studied by high-frequency stiffness measurements. Science 217, 70-2.
    • (1982) Science , vol.217 , pp. 70-72
    • Cecchi, G.1    Griffiths, P.J.2    Taylor, S.3
  • 12
    • 0030989103 scopus 로고    scopus 로고
    • The effect of intracellular pH on contractile function of intact, single fibres of mouse muscle declines with increasing temperature
    • Westerblad H, Bruton JD, Lannergren J (1997) The effect of intracellular pH on contractile function of intact, single fibres of mouse muscle declines with increasing temperature. J Physiol 500 (1), 193-204.
    • (1997) J Physiol , vol.500 , Issue.1 , pp. 193-204
    • Westerblad, H.1    Bruton, J.D.2    Lannergren, J.3
  • 13
    • 0032976537 scopus 로고    scopus 로고
    • Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers
    • Tsaturyan AK, Bershitsky SY, Burns R, Ferenczi MA (1999) Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers. Biophys J 77, 354-72.
    • (1999) Biophys J , vol.77 , pp. 354-372
    • Tsaturyan, A.K.1    Bershitsky, S.Y.2    Burns, R.3    Ferenczi, M.A.4
  • 14
    • 0023574449 scopus 로고
    • Greater hydrogen ion-induced depression of tension and velocity in skinned single fibres of rat fast than slow muscles
    • Metzger JM, Moss RL (1987) Greater hydrogen ion-induced depression of tension and velocity in skinned single fibres of rat fast than slow muscles. J Physiol 393, 727-42.
    • (1987) J Physiol , vol.393 , pp. 727-742
    • Metzger, J.M.1    Moss, R.L.2
  • 15
    • 0027943305 scopus 로고
    • Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit
    • Potma EJ, Graas IAV, Stiene GJM (1994) Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit. Biophys J 67, 2404-10.
    • (1994) Biophys J , vol.67 , pp. 2404-2410
    • Potma, E.J.1    Graas, I.A.V.2    Stiene, G.J.M.3
  • 16
    • 0018631104 scopus 로고
    • Mitochondrial proteins of fast-twitch glycolytic, fast-twitch glycolytic-oxidative and slow-twitch-oxidative rabbit skeletal muscle
    • Takacs O, Scisllowski D, Zydowo M, Guba F (1979) Mitochondrial proteins of fast-twitch glycolytic, fast-twitch glycolytic-oxidative and slow-twitch-oxidative rabbit skeletal muscle. Int J Biochem 10 (10), 859-65.
    • (1979) Int J Biochem , vol.10 , Issue.10 , pp. 859-865
    • Takacs, O.1    Scisllowski, D.2    Zydowo, M.3    Guba, F.4
  • 17
    • 0035577182 scopus 로고    scopus 로고
    • Muscle damage from eccentric exercise: Mechanism, mechanical signs, adaptation and clinical applications
    • Proske U, Morgan DL (2001) Muscle damage from eccentric exercise: Mechanism, mechanical signs, adaptation and clinical applications. J Physiol 537 (2), 333-45.
    • (2001) J Physiol , vol.537 , Issue.2 , pp. 333-345
    • Proske, U.1    Morgan, D.L.2
  • 18
    • 0034741717 scopus 로고    scopus 로고
    • Excitation-induced Ca2+ influx and skeletal muscle cell damage
    • Gissel H, Clausen T (2001) Excitation-induced Ca2+ influx and skeletal muscle cell damage. Acta Physiol Scand 171 (3), 327-34.
    • (2001) Acta Physiol Scand , vol.171 , Issue.3 , pp. 327-334
    • Gissel, H.1    Clausen, T.2
  • 19
    • 0035865409 scopus 로고    scopus 로고
    • Effect of temperature on elementary steps of the crossbridge cycle in rabbit soleus slow-twitch muscle fibres
    • Wang G, Kawai M (2001) Effect of temperature on elementary steps of the crossbridge cycle in rabbit soleus slow-twitch muscle fibres. J Physiol 531 (1), 219-34.
    • (2001) J Physiol , vol.531 , Issue.1 , pp. 219-234
    • Wang, G.1    Kawai, M.2
  • 20
    • 0019974315 scopus 로고
    • Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog
    • Godt RE, Lindley BD (1982) Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J Gen Physiol 80, 279-97.
    • (1982) J Gen Physiol , vol.80 , pp. 279-297
    • Godt, R.E.1    Lindley, B.D.2
  • 21
    • 0023144784 scopus 로고
    • Tetrahymena actin. Cloning and sequencing of the Tetrahymena actin gene and identification of its gene product
    • Hirono M, Endoh H, Okada N, Numata O, Watanabe Y (1987) Tetrahymena actin. Cloning and sequencing of the Tetrahymena actin gene and identification of its gene product. J Mol Biol 194 (2), 181-92.
    • (1987) J Mol Biol , vol.194 , Issue.2 , pp. 181-192
    • Hirono, M.1    Endoh, H.2    Okada, N.3    Numata, O.4    Watanabe, Y.5
  • 22
    • 0025248687 scopus 로고
    • The human embryonic myosin heavy chain. Complete primary structure reveals evolutionary relationships with other developmental isoforms
    • Stedman HH, Eller M, Jullian EH, Fertels SH, Sarkar S, Sylvester JE, Kelly AM, Rubinstein NA (1990) The human embryonic myosin heavy chain. Complete primary structure reveals evolutionary relationships with other developmental isoforms. J Biol Chem 265, 3568-76.
    • (1990) J Biol Chem , vol.265 , pp. 3568-3576
    • Stedman, H.H.1    Eller, M.2    Jullian, E.H.3    Fertels, S.H.4    Sarkar, S.5    Sylvester, J.E.6    Kelly, A.M.7    Rubinstein, N.A.8
  • 23
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino S, Reggiani C (1996) Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiological Reviews 76 (2), 371-423.
    • (1996) Physiological Reviews , vol.76 , Issue.2 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 24
    • 0027080346 scopus 로고
    • A 4°C-1 min method of cold water immersion test for peripheral circulatory function in fingers
    • Ishitake T, Nakagawa K, Iwamoto J, Mori T, Matoba T (1992) A 4°C-1 min method of cold water immersion test for peripheral circulatory function in fingers. Jpn J Ind Health 34, 560-4.
    • (1992) Jpn J Ind Health , vol.34 , pp. 560-564
    • Ishitake, T.1    Nakagawa, K.2    Iwamoto, J.3    Mori, T.4    Matoba, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.