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Volumn 95, Issue 3, 2003, Pages 1279-1286

Endogenous expression and developmental changes of HSP72 in rat skeletal muscles

Author keywords

Development; Heat shock proteins; Immunohistochemistry; Myosin heavy chain; Western blots

Indexed keywords

HEAT SHOCK COGNATE 73 PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 72; MYOSIN HEAVY CHAIN; UNCLASSIFIED DRUG;

EID: 0042423436     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/japplphysiol.00353.2003     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 0016701674 scopus 로고
    • Postnatal development of locomotion in the laboratory rat
    • Altman J and Sudarshan K. Postnatal development of locomotion in the laboratory rat. Anim Behav 23: 896-920, 1975.
    • (1975) Anim Behav , vol.23 , pp. 896-920
    • Altman, J.1    Sudarshan, K.2
  • 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 MM. 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
    • 0027787488 scopus 로고
    • Metabolic and contractile differentiation of rabbit muscles during growth
    • Briand M, Boissonnet G, Laplace-Marieze V, and Briand Y. Metabolic and contractile differentiation of rabbit muscles during growth. Int J Biochem 25: 1881-1887, 1993.
    • (1993) Int J Biochem , vol.25 , pp. 1881-1887
    • Briand, M.1    Boissonnet, G.2    Laplace-Marieze, V.3    Briand, Y.4
  • 4
    • 0032489016 scopus 로고    scopus 로고
    • The HSP70 and HSP60 chaperone machines
    • Bukau B and Horwich AL. The HSP70 and HSP60 chaperone machines. Cell 92: 351-366, 1998.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 5
    • 0021415139 scopus 로고
    • Myosin isozyme transitions occurring during postnatal development of the rat soleus muscle
    • Butler-Browne GS and Whalen RG. Myosin isozyme transitions occurring during postnatal development of the rat soleus muscle. Dev Biol 102: 324-334, 1984.
    • (1984) Dev Biol , vol.102 , pp. 324-334
    • Butler-Browne, G.S.1    Whalen, R.G.2
  • 6
    • 0015257535 scopus 로고
    • Dynamic properties of mammalian skeletal muscles
    • Close RI. Dynamic properties of mammalian skeletal muscles. Physiol Rev 52: 129-197, 1972.
    • (1972) Physiol Rev , vol.52 , pp. 129-197
    • Close, R.I.1
  • 7
    • 0025266785 scopus 로고
    • Development of muscle fiber types in the prenatal rat hindlimb
    • Condon K, Silberstein L, Blau HM, and Thompson WJ. Development of muscle fiber types in the prenatal rat hindlimb. Dev Biol 138: 256-274, 1990.
    • (1990) Dev Biol , vol.138 , pp. 256-274
    • Condon, K.1    Silberstein, L.2    Blau, H.M.3    Thompson, W.J.4
  • 8
    • 0034493114 scopus 로고    scopus 로고
    • HSP72 gene expression progressively increases in human skeletal muscle during prolonged, exhaustive exercise
    • Febbraio MA and Koukoulas I. HSP72 gene expression progressively increases in human skeletal muscle during prolonged, exhaustive exercise. J Appl Physiol 89: 1055-1060, 2000.
    • (2000) J Appl Physiol , vol.89 , pp. 1055-1060
    • Febbraio, M.A.1    Koukoulas, I.2
  • 9
    • 0036487228 scopus 로고    scopus 로고
    • Reduced glycogen availability is associated with an elevation in HSP72 in contracting human skeletal muscle
    • Febbraio MA, Steensberg A, Walsh R, Koukoulas I, Hall G, Saltin B, and Pedersen BK. Reduced glycogen availability is associated with an elevation in HSP72 in contracting human skeletal muscle. J Physiol 538: 911-917, 2002.
    • (2002) J Physiol , vol.538 , pp. 911-917
    • Febbraio, M.A.1    Steensberg, A.2    Walsh, R.3    Koukoulas, I.4    Hall, G.5    Saltin, B.6    Pedersen, B.K.7
  • 10
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ and Sambrook J. Protein folding in the cell. Nature 355: 33-45, 1992.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 11
    • 0032503968 scopus 로고    scopus 로고
    • HSP104, HSP70, and HSP40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR and Lindquist S. HSP104, HSP70, and HSP40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82, 1998.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 12
    • 0034097491 scopus 로고    scopus 로고
    • Stress proteins of 70 kDa in chronically exercised skeletal muscle
    • Gonzalez B, Hernando R, and Manso R. Stress proteins of 70 kDa in chronically exercised skeletal muscle. Pflügers Arch 440: 42-49, 2000.
    • (2000) Pflügers Arch , vol.440 , pp. 42-49
    • Gonzalez, B.1    Hernando, R.2    Manso, R.3
  • 14
    • 0031019990 scopus 로고    scopus 로고
    • Muscle fiber stress in response to exercise. Synthesis, accumulation and isoform transitions of 70-kDa heat-shock proteins
    • Hernando R and Manso R. Muscle fiber stress in response to exercise. Synthesis, accumulation and isoform transitions of 70-kDa heat-shock proteins. Eur J Biochem 243: 460-467, 1997.
    • (1997) Eur J Biochem , vol.243 , pp. 460-467
    • Hernando, R.1    Manso, R.2
  • 15
    • 0025931422 scopus 로고
    • Histochemical differentiation of fibers in the rat slow and fast twitch muscles
    • Ishihara A and Taguchi S. Histochemical differentiation of fibers in the rat slow and fast twitch muscles. Jpn J Physiol 41: 251-258, 1991.
    • (1991) Jpn J Physiol , vol.41 , pp. 251-258
    • Ishihara, A.1    Taguchi, S.2
  • 16
    • 0028297203 scopus 로고
    • Stress protein induction in skeletal muscle: Comparison of laboratory models to naturally occurring hypertrophy
    • Kilgore JL, Timson BF, Saunders DK, Kraemer RR, Klemm RD, and Ross CR. Stress protein induction in skeletal muscle: comparison of laboratory models to naturally occurring hypertrophy. J Appl Physiol 76: 598-601, 1994.
    • (1994) J Appl Physiol , vol.76 , pp. 598-601
    • Kilgore, J.L.1    Timson, B.F.2    Saunders, D.K.3    Kraemer, R.R.4    Klemm, R.D.5    Ross, C.R.6
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0033652995 scopus 로고    scopus 로고
    • Prior heat stress improves survival of ischemic-reperfused skeletal muscle in vivo
    • Lepore DA, Hurley JV, Stewart AG, Morrison WA, and Anderson RL. Prior heat stress improves survival of ischemic-reperfused skeletal muscle in vivo. Muscle Nerve 23: 1847-1855, 2000.
    • (2000) Muscle Nerve , vol.23 , pp. 1847-1855
    • Lepore, D.A.1    Hurley, J.V.2    Stewart, A.G.3    Morrison, W.A.4    Anderson, R.L.5
  • 20
    • 0028008086 scopus 로고
    • Shift in type I fiber proportion in rat hindlimb muscle are accompanied by changes in HSP72 content
    • Locke M, Atkinson BG, Tanguay RM, and Noble EG. Shift in type I fiber proportion in rat hindlimb muscle are accompanied by changes in HSP72 content. Am J Physiol Cell Physiol 266: C1240-C1246, 1994.
    • (1994) Am J Physiol Cell Physiol , vol.266
    • Locke, M.1    Atkinson, B.G.2    Tanguay, R.M.3    Noble, E.G.4
  • 21
    • 0026319184 scopus 로고
    • Inducible isoform of HSP70 is constitutively expressed in a muscle fiber type specific pattern
    • Locke M, Noble EG, and Atkinson BG. Inducible isoform of HSP70 is constitutively expressed in a muscle fiber type specific pattern. Am J Physiol Cell Physiol 261: C774-C779, 1991.
    • (1991) Am J Physiol Cell Physiol , vol.261
    • Locke, M.1    Noble, E.G.2    Atkinson, B.G.3
  • 22
    • 0036021808 scopus 로고    scopus 로고
    • Exercise-induced elevation of HSP70 is intensity dependent
    • Milne KJ and Noble EG. Exercise-induced elevation of HSP70 is intensity dependent. J Appl Physiol 93: 561-568, 2002.
    • (2002) J Appl Physiol , vol.93 , pp. 561-568
    • Milne, K.J.1    Noble, E.G.2
  • 23
    • 0020957845 scopus 로고
    • Changes of activity patterns in slow and fast muscles during postnatal development
    • Navarrete R and Vrvoba G. Changes of activity patterns in slow and fast muscles during postnatal development. Dev Brain Res 8: 11-19, 1983.
    • (1983) Dev Brain Res , vol.8 , pp. 11-19
    • Navarrete, R.1    Vrvoba, G.2
  • 24
    • 0027158727 scopus 로고
    • Activity-dependent interactions between motoneurons and muscles: Their role in the development of the motor unit
    • Navarrete R and Vrvoba G. Activity-dependent interactions between motoneurons and muscles: their role in the development of the motor unit. Prog Neurobiol 41: 93-124, 1993.
    • (1993) Prog Neurobiol , vol.41 , pp. 93-124
    • Navarrete, R.1    Vrvoba, G.2
  • 25
    • 0024343493 scopus 로고
    • Metabolic specialization in fast and slow muscle fibers of the developing rat
    • Nemeth PM, Norris BJ, Solanki L, and Kelly AM. Metabolic specialization in fast and slow muscle fibers of the developing rat. J Neurosci 9: 2336-2343, 1989.
    • (1989) J Neurosci , vol.9 , pp. 2336-2343
    • Nemeth, P.M.1    Norris, B.J.2    Solanki, L.3    Kelly, A.M.4
  • 28
    • 18744401334 scopus 로고    scopus 로고
    • Clenbuterol induces expression of multiple myosin heavy chain isoforms in rat soleus fibers
    • Oishi Y, Imoto K, Ogata T, Taniguchi K, Matsumoto H, and Roy RR. Clenbuterol induces expression of multiple myosin heavy chain isoforms in rat soleus fibers. Acta Physiol Scand 176: 311-318, 2002.
    • (2002) Acta Physiol Scand , vol.176 , pp. 311-318
    • Oishi, Y.1    Imoto, K.2    Ogata, T.3    Taniguchi, K.4    Matsumoto, H.5    Roy, R.R.6
  • 30
    • 0036092640 scopus 로고    scopus 로고
    • Muscle type-specific response of HSP60, HSP72, and HSC73 during recovery after elevation of muscle temperature
    • Oishi Y, Taniguchi K, Matsumoto H, Ishihara A, Ohira Y, and Roy RR. Muscle type-specific response of HSP60, HSP72, and HSC73 during recovery after elevation of muscle temperature. J Appl Physiol 92: 1097-1103, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 1097-1103
    • Oishi, Y.1    Taniguchi, K.2    Matsumoto, H.3    Ishihara, A.4    Ohira, Y.5    Roy, R.R.6
  • 31
    • 0031015918 scopus 로고    scopus 로고
    • Contractile properties and myosin heavy chain composition of newborn rat soleus muscles at different stages of postnatal development
    • Picquet F, Stevens L, Butler-Browne GS, and Mounier Y. Contractile properties and myosin heavy chain composition of newborn rat soleus muscles at different stages of postnatal development. J Muscle Res Cell Motil 18: 71-79, 1997.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 71-79
    • Picquet, F.1    Stevens, L.2    Butler-Browne, G.S.3    Mounier, Y.4
  • 33
    • 0027207956 scopus 로고
    • Tissue-specific expression of heat shock proteins of the mouse in the absence of stress
    • Tanguay RM, Wu Y, and Khandjian EW. Tissue-specific expression of heat shock proteins of the mouse in the absence of stress. Dev Genet 14: 112-118, 1993.
    • (1993) Dev Genet , vol.14 , pp. 112-118
    • Tanguay, R.M.1    Wu, Y.2    Khandjian, E.W.3
  • 34
    • 0034762262 scopus 로고    scopus 로고
    • Regulation of myosin heavy chain expression during rat skeletal muscle development in vitro
    • Torgan CE and Daniels MP. Regulation of myosin heavy chain expression during rat skeletal muscle development in vitro. Mol Biol Cell 12: 1499-1508, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 1499-1508
    • Torgan, C.E.1    Daniels, M.P.2
  • 35
    • 0034858859 scopus 로고    scopus 로고
    • Heat shock response and ageing: Mechanism and applications
    • Verbeke P, Fonager J, Clark BF, and Rattan SI. Heat shock response and ageing: mechanism and applications. Cell Biol Int 25: 845-857, 2001.
    • (2001) Cell Biol Int , vol.25 , pp. 845-857
    • Verbeke, P.1    Fonager, J.2    Clark, B.F.3    Rattan, S.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.