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Volumn 93, Issue 3, 2008, Pages 415-425

Time-dependent changes in caspase-3 activity and heat shock protein 25 after spinal cord transection in adult rats

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; HEAT SHOCK PROTEIN 25;

EID: 39149111886     PISSN: 09580670     EISSN: 1469445X     Source Type: Journal    
DOI: 10.1113/expphysiol.2007.041228     Document Type: Article
Times cited : (13)

References (55)
  • 2
    • 0021261014 scopus 로고
    • EMG activity of slow and fast ankle extensors following spinal cord transection
    • &
    • Alaimo MA, Smith JL, Roy RR & Edgerton VR (1984). EMG activity of slow and fast ankle extensors following spinal cord transection. J Appl Physiol 56, 1608 1613.
    • (1984) J Appl Physiol , vol.56 , pp. 1608-1613
    • Alaimo, M.A.1    Smith, J.L.2    Roy, R.R.3    Edgerton, V.R.4
  • 3
    • 0024391714 scopus 로고
    • A comparison of the effects of denervation on the mechanical properties of rat and guinea-pig skeletal muscle
    • &
    • al-Amood WS & Lewis DM (1989). A comparison of the effects of denervation on the mechanical properties of rat and guinea-pig skeletal muscle. J Physiol 414, 1 16.
    • (1989) J Physiol , vol.414 , pp. 1-16
    • Al-Amood, W.S.1    Lewis, D.M.2
  • 4
    • 0023179135 scopus 로고
    • Electromyography of rat soleus, medial gastrocnemius, and tibialis anterior during hind limb suspension
    • &
    • Alford EK, Roy RR, Hodgson JA & Edgerton VR (1987). Electromyography of rat soleus, medial gastrocnemius, and tibialis anterior during hind limb suspension. Exp Neurol 96, 635 649.
    • (1987) Exp Neurol , vol.96 , pp. 635-649
    • Alford, E.K.1    Roy, R.R.2    Hodgson, J.A.3    Edgerton, V.R.4
  • 5
    • 0035168989 scopus 로고    scopus 로고
    • Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle
    • &
    • Baldwin KM & Haddad F (2001). Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. J Appl Physiol 90, 345 357.
    • (2001) J Appl Physiol , vol.90 , pp. 345-357
    • Baldwin, K.M.1    Haddad, F.2
  • 6
    • 0025191395 scopus 로고
    • Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle
    • &
    • Baldwin KM, Herrick RE, Ilyina-Kakueva E & Oganov VS (1990). Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle. FASEB J 4, 79 83.
    • (1990) FASEB J , vol.4 , pp. 79-83
    • Baldwin, K.M.1    Herrick, R.E.2    Ilyina-Kakueva, E.3    Oganov, V.S.4
  • 7
    • 34249912645 scopus 로고    scopus 로고
    • Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading
    • &
    • Berthon P, Duguez S, Favier FB, Amirouche A, Feasson L, Vico L, Denis C & Freyssenet D (2007). Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading. Pflugers Arch 454, 625 633.
    • (2007) Pflugers Arch , vol.454 , pp. 625-633
    • Berthon, P.1    Duguez, S.2    Favier, F.B.3    Amirouche, A.4    Feasson, L.5    Vico, L.6    Denis, C.7    Freyssenet, D.8
  • 8
    • 0024578954 scopus 로고
    • αb subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
    • &
    • Bhat SP & Nagineni CN (1989). αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun 158, 319 325.
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 10
    • 0037246247 scopus 로고    scopus 로고
    • On the role of Hsp27 in regulating apoptosis
    • &
    • Concannon CG, Gorman AM & Samali A (2003). On the role of Hsp27 in regulating apoptosis. Apoptosis 8, 61 70.
    • (2003) Apoptosis , vol.8 , pp. 61-70
    • Concannon, C.G.1    Gorman, A.M.2    Samali, A.3
  • 11
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • &
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR & Mitch WE (2004). Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113, 115 123.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 13
    • 0031751810 scopus 로고    scopus 로고
    • Early changes in muscle fiber size and gene expression in response to spinal cord transection and exercise
    • &
    • Dupont-Versteegden EE, Houle JD, Gurley CM & Peterson CA (1998). Early changes in muscle fiber size and gene expression in response to spinal cord transection and exercise. Am J Physiol Cell Physiol 275, C1124 C1133.
    • (1998) Am J Physiol Cell Physiol , vol.275
    • Dupont-Versteegden, E.E.1    Houle, J.D.2    Gurley, C.M.3    Peterson, C.A.4
  • 16
    • 34548515738 scopus 로고    scopus 로고
    • Cellular patterns of the atrophic response in murine soleus and gastrocnemius muscles submitted to simulated weightlessness
    • &
    • Ferreira R, Vitorino R, Neuparth MJ, Appell HJ, Amado F & Duarte JA (2007). Cellular patterns of the atrophic response in murine soleus and gastrocnemius muscles submitted to simulated weightlessness. Eur J Appl Physiol 101, 331 340.
    • (2007) Eur J Appl Physiol , vol.101 , pp. 331-340
    • Ferreira, R.1    Vitorino, R.2    Neuparth, M.J.3    Appell, H.J.4    Amado, F.5    Duarte, J.A.6
  • 17
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment invited review: Microgravity and skeletal muscle
    • &
    • Fitts RH, Riley DR & Widrick JJ (2000). Physiology of a microgravity environment invited review: microgravity and skeletal muscle. J Appl Physiol 89, 823 839.
    • (2000) J Appl Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 18
    • 12944328888 scopus 로고    scopus 로고
    • Comparison of the small heat shock proteins αb-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle
    • &
    • Golenhofen N, Perng MD, Quinlan RA & Drenckhahn D (2004). Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol 122, 415 425.
    • (2004) Histochem Cell Biol , vol.122 , pp. 415-425
    • Golenhofen, N.1    Perng, M.D.2    Quinlan, R.A.3    Drenckhahn, D.4
  • 19
    • 0034604721 scopus 로고    scopus 로고
    • αb-crystallin gene induction and phosphorylation by MKK6-activated p38. a potential role for αb-crystallin as a target of the p38 branch of the cardiac stress response
    • &
    • Hoover HE, Thuerauf DJ, Martindale JJ & Glembotski CC (2000). αB-crystallin gene induction and phosphorylation by MKK6-activated p38. A potential role for αB-crystallin as a target of the p38 branch of the cardiac stress response. J Biol Chem 275, 23825 23833.
    • (2000) J Biol Chem , vol.275 , pp. 23825-23833
    • Hoover, H.E.1    Thuerauf, D.J.2    Martindale, J.J.3    Glembotski, C.C.4
  • 20
    • 0032814359 scopus 로고    scopus 로고
    • Effects of fetal spinal cord tissue transplants and cycling exercise on the soleus muscle in spinalized rats
    • &
    • Houle JD, Morris K, Skinner RD, Garcia-Rill E & Peterson CA (1999). Effects of fetal spinal cord tissue transplants and cycling exercise on the soleus muscle in spinalized rats. Muscle Nerve 22, 846 856.
    • (1999) Muscle Nerve , vol.22 , pp. 846-856
    • Houle, J.D.1    Morris, K.2    Skinner, R.D.3    Garcia-Rill, E.4    Peterson, C.A.5
  • 21
    • 27244451504 scopus 로고    scopus 로고
    • Effects of innervation state on Hsp25 content and phosphorylation in inactive rat plantaris muscles
    • &
    • Huey KA, Hyatt JP, Zhong H & Roy RR (2005). Effects of innervation state on Hsp25 content and phosphorylation in inactive rat plantaris muscles. Acta Physiol Scand 185, 219 227.
    • (2005) Acta Physiol Scand , vol.185 , pp. 219-227
    • Huey, K.A.1    Hyatt, J.P.2    Zhong, H.3    Roy, R.R.4
  • 22
    • 34447519135 scopus 로고    scopus 로고
    • Modulation of HSP25 and TNF-α during the early stages of functional overload of a rat slow and fast muscle
    • &
    • Huey KA, McCall GE, Zhong H & Roy RR (2007). Modulation of HSP25 and TNF-α during the early stages of functional overload of a rat slow and fast muscle. J Appl Physiol 102, 2307 2314.
    • (2007) J Appl Physiol , vol.102 , pp. 2307-2314
    • Huey, K.A.1    McCall, G.E.2    Zhong, H.3    Roy, R.R.4
  • 23
    • 3042773720 scopus 로고    scopus 로고
    • Inactivity-induced modulation of Hsp20 and Hsp25 content in rat hindlimb muscles
    • &
    • Huey KA, Thresher JS, Brophy CM & Roy RR (2004). Inactivity-induced modulation of Hsp20 and Hsp25 content in rat hindlimb muscles. Muscle Nerve 30, 95 101.
    • (2004) Muscle Nerve , vol.30 , pp. 95-101
    • Huey, K.A.1    Thresher, J.S.2    Brophy, C.M.3    Roy, R.R.4
  • 24
    • 0034782507 scopus 로고    scopus 로고
    • Skeletal muscle adaptations following spinal cord contusion injury in rat and the relationship to locomotor function: A time course study
    • &
    • Hutchinson KJ, Linderman JK & Basso DM (2001). Skeletal muscle adaptations following spinal cord contusion injury in rat and the relationship to locomotor function: a time course study. J Neurotrauma 18, 1075 1089.
    • (2001) J Neurotrauma , vol.18 , pp. 1075-1089
    • Hutchinson, K.J.1    Linderman, J.K.2    Basso, D.M.3
  • 25
    • 0027423184 scopus 로고
    • Physiological and pathological changes in levels of the two small stress proteins, HSP27 and αb crystallin, in rat hindlimb muscles
    • &
    • Inaguma Y, Goto S, Shinohara H, Hasegawa K, Ohshima K & Kato K (1993). Physiological and pathological changes in levels of the two small stress proteins, HSP27 and αB crystallin, in rat hindlimb muscles. J Biochem 114, 378 384.
    • (1993) J Biochem , vol.114 , pp. 378-384
    • Inaguma, Y.1    Goto, S.2    Shinohara, H.3    Hasegawa, K.4    Ohshima, K.5    Kato, K.6
  • 26
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • &
    • Jagoe RT & Goldberg AL (2001). What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 4, 183 190.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 27
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein αb-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • &
    • Kamradt MC, Chen F & Cryns VL (2001). The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J Biol Chem 276, 16059 16063.
    • (2001) J Biol Chem , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 29
    • 0034862016 scopus 로고    scopus 로고
    • Heat shock proteins and cardiac protection
    • Latchman DS (2001). Heat shock proteins and cardiac protection. Cardiovasc Res 51, 637 646.
    • (2001) Cardiovasc Res , vol.51 , pp. 637-646
    • Latchman, D.S.1
  • 32
    • 0028008086 scopus 로고
    • Shifts in type I fiber proportion in rat hindlimb muscle are accompanied by changes in HSP72 content
    • &
    • Locke M, Atkinson BG, Tanguay RM & Noble EG (1994). Shifts 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) Am J Physiol Cell Physiol , vol.266
    • Locke, M.1    Atkinson, B.G.2    Tanguay, R.M.3    Noble, E.G.4
  • 33
    • 0029310491 scopus 로고
    • Stress proteins: The exercise response
    • &
    • Locke M & Noble EG (1995). Stress proteins: the exercise response. Can J Appl Physiol 20, 155 167.
    • (1995) Can J Appl Physiol , vol.20 , pp. 155-167
    • Locke, M.1    Noble, E.G.2
  • 35
    • 0037422859 scopus 로고    scopus 로고
    • Mimicking phosphorylation of αb-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis
    • &
    • Morrison LE, Hoover HE, Thuerauf DJ & Glembotski CC (2003). Mimicking phosphorylation of αB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis. Circ Res 92, 203 211.
    • (2003) Circ Res , vol.92 , pp. 203-211
    • Morrison, L.E.1    Hoover, H.E.2    Thuerauf, D.J.3    Glembotski, C.C.4
  • 36
    • 0031772471 scopus 로고    scopus 로고
    • Heat shock proteins and the inflammatory response
    • Moseley PL (1998). Heat shock proteins and the inflammatory response. Ann N Y Acad Sci 856, 206 213.
    • (1998) Ann N Y Acad Sci , vol.856 , pp. 206-213
    • Moseley, P.L.1
  • 37
    • 18844455247 scopus 로고    scopus 로고
    • Effects of T3 treatment on HSP72 and calcineurin content of functionally overloaded rat plantaris muscle
    • &
    • Ogata T, Oishi Y, Roy RR & Ohmori H (2005). Effects of T3 treatment on HSP72 and calcineurin content of functionally overloaded rat plantaris muscle. Biochem Biophys Res Commun 331, 1317 1323.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1317-1323
    • Ogata, T.1    Oishi, Y.2    Roy, R.R.3    Ohmori, H.4
  • 38
    • 2442691422 scopus 로고    scopus 로고
    • Calcineurin and heat-shock proteins modulation in clenbuterol-induced hypertrophied rat skeletal muscles
    • &
    • Oishi Y, Imoto K, Ogata T, Taniguchi K, Matsumoto H, Fukuoka Y & Roy RR (2004). Calcineurin and heat-shock proteins modulation in clenbuterol-induced hypertrophied rat skeletal muscles. Pflugers Arch 448, 114 122.
    • (2004) Pflugers Arch , vol.448 , pp. 114-122
    • Oishi, Y.1    Imoto, K.2    Ogata, T.3    Taniguchi, K.4    Matsumoto, H.5    Fukuoka, Y.6    Roy, R.R.7
  • 39
    • 33645804792 scopus 로고    scopus 로고
    • Slower skeletal muscle phenotypes are critical for constitutive expression of Hsp70 in overloaded rat plantaris muscle
    • &
    • O'Neill DE, Aubrey FK, Zeldin DA, Michel RN & Noble EG (2006). Slower skeletal muscle phenotypes are critical for constitutive expression of Hsp70 in overloaded rat plantaris muscle. J Appl Physiol 100, 981 987.
    • (2006) J Appl Physiol , vol.100 , pp. 981-987
    • O'Neill, D.E.1    Aubrey, F.K.2    Zeldin, D.A.3    Michel, R.N.4    Noble, E.G.5
  • 41
    • 0026352916 scopus 로고
    • Mechanical and morphological properties of chronically inactive cat tibialis anterior motor units
    • &
    • Pierotti DJ, Roy RR, Bodine-Fowler SC, Hodgson JA & Edgerton VR (1991). Mechanical and morphological properties of chronically inactive cat tibialis anterior motor units. J Physiol 444, 175 192.
    • (1991) J Physiol , vol.444 , pp. 175-192
    • Pierotti, D.J.1    Roy, R.R.2    Bodine-Fowler, S.C.3    Hodgson, J.A.4    Edgerton, V.R.5
  • 42
    • 22344449778 scopus 로고    scopus 로고
    • Anti-apoptotic effects of L-glutamine-mediated transcriptional modulation of the heat shock protein 72 during heat shock
    • &
    • Ropeleski MJ, Riehm J, Baer KA, Musch MW & Chang EB (2005). Anti-apoptotic effects of L-glutamine-mediated transcriptional modulation of the heat shock protein 72 during heat shock. Gastroenterology 129, 170 184.
    • (2005) Gastroenterology , vol.129 , pp. 170-184
    • Ropeleski, M.J.1    Riehm, J.2    Baer, K.A.3    Musch, M.W.4    Chang, E.B.5
  • 43
    • 0026061367 scopus 로고
    • The plasticity of skeletal muscle: Effects of neuromuscular activity
    • &
    • Roy RR, Baldwin KM & Edgerton VR (1991). The plasticity of skeletal muscle: effects of neuromuscular activity. Exer Sport Sci Rev 19, 269 312.
    • (1991) Exer Sport Sci Rev , vol.19 , pp. 269-312
    • Roy, R.R.1    Baldwin, K.M.2    Edgerton, V.R.3
  • 46
    • 0036730503 scopus 로고    scopus 로고
    • Mechanical properties of the electrically silent adult rat soleus muscle
    • &
    • Roy RR, Zhong H, Monti RJ, Vallance KA & Edgerton VR (2002). Mechanical properties of the electrically silent adult rat soleus muscle. Muscle Nerve 26, 404 412.
    • (2002) Muscle Nerve , vol.26 , pp. 404-412
    • Roy, R.R.1    Zhong, H.2    Monti, R.J.3    Vallance, K.A.4    Edgerton, V.R.5
  • 47
    • 21044441687 scopus 로고    scopus 로고
    • Heat treatment reduces oxidative stress and protects muscle mass during immobilization
    • &
    • Selsby JT & Dodd SL (2005). Heat treatment reduces oxidative stress and protects muscle mass during immobilization. Am J Physiol Regul Integr Comp Physiol 289, R134 R139.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.289
    • Selsby, J.T.1    Dodd, S.L.2
  • 48
    • 33744926902 scopus 로고    scopus 로고
    • Caspase activation contributes to endotoxin-induced diaphragm weakness
    • &
    • Supinski GS & Callahan LA (2006). Caspase activation contributes to endotoxin-induced diaphragm weakness. J Appl Physiol 100, 1770 1777.
    • (2006) J Appl Physiol , vol.100 , pp. 1770-1777
    • Supinski, G.S.1    Callahan, L.A.2
  • 49
    • 0034019038 scopus 로고    scopus 로고
    • Myosin heavy chain-isoform expression following reduced neuromuscular activity: Potential regulatory mechanisms
    • Talmadge RJ (2000). Myosin heavy chain-isoform expression following reduced neuromuscular activity: potential regulatory mechanisms. Muscle Nerve 23, 661 679.
    • (2000) Muscle Nerve , vol.23 , pp. 661-679
    • Talmadge, R.J.1
  • 51
    • 0036784999 scopus 로고    scopus 로고
    • Mechanical properties of rat soleus after long-term spinal cord transection
    • &
    • Talmadge RJ, Roy RR, Caiozzo VJ & Edgerton VR (2002). Mechanical properties of rat soleus after long-term spinal cord transection. J Appl Physiol 93, 1487 1497.
    • (2002) J Appl Physiol , vol.93 , pp. 1487-1497
    • Talmadge, R.J.1    Roy, R.R.2    Caiozzo, V.J.3    Edgerton, V.R.4
  • 52
    • 0028935443 scopus 로고
    • Prominence of myosin heavy chain hybrid fibers in soleus muscle of spinal cord-transected rats
    • &
    • Talmadge RJ, Roy RR & Edgerton VR (1995). Prominence of myosin heavy chain hybrid fibers in soleus muscle of spinal cord-transected rats. J Appl Physiol 78, 1256 1265.
    • (1995) J Appl Physiol , vol.78 , pp. 1256-1265
    • Talmadge, R.J.1    Roy, R.R.2    Edgerton, V.R.3
  • 53
    • 26844582185 scopus 로고    scopus 로고
    • Molecular pathways leading to cancer cachexia
    • Tisdale MJ (2005). Molecular pathways leading to cancer cachexia. Physiology (Bethesda) 20, 340 348.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 340-348
    • Tisdale, M.J.1
  • 54
    • 0037423661 scopus 로고    scopus 로고
    • Serine phosphorylation and suppression of apoptosis by the small heat shock protein αb-crystallin
    • Webster KA (2003). Serine phosphorylation and suppression of apoptosis by the small heat shock protein αB-crystallin. Circ Res 92, 130 132.
    • (2003) Circ Res , vol.92 , pp. 130-132
    • Webster, K.A.1
  • 55
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch WJ (1992). Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 72, 1063 1081.
    • (1992) Physiol Rev , vol.72 , pp. 1063-1081
    • Welch, W.J.1


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