메뉴 건너뛰기




Volumn 24, Issue 1, 2003, Pages 33-53

Delineation of signalling pathway leading to antioxidant-dependent inhibition of dexamethasone-mediated muscle cell death

Author keywords

[No Author keywords available]

Indexed keywords

1 (5 ISOQUINOLINESULFONYL) 2 METHYLPIPERAZINE; 1 [[6 (3 METHOXYESTRA 1,3,5(10) TRIEN 17BETA YL)AMINO]HEXYL] 1H PYRROLE 2,5 DIONE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 7 AMINODACTINOMYCIN; ACETYLCYSTEINE; ANTIOXIDANT; ASCORBIC ACID; CALCIMYCIN; CALCIUM ION; CALPAIN; CALPASTATIN; CREATINE KINASE; CYCLIC AMP; DACTINOMYCIN; DEXAMETHASONE; DNA FRAGMENT; GENOMIC DNA; GLUCOCORTICOID; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; PROTEIN KINASE C;

EID: 0041928098     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024887431768     Document Type: Conference Paper
Times cited : (22)

References (75)
  • 1
    • 0034737602 scopus 로고    scopus 로고
    • Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton JM and Steinhardt RA (2000) Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. J Biol Chem 275: 9452-9460.
    • (2000) J Biol Chem , vol.275 , pp. 9452-9460
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 2
    • 0033779795 scopus 로고    scopus 로고
    • Deflazacort increases laminin expression and myogenic repair, and induces early persistent functional gain in mdx mouse muscular dystrophy
    • Anderson JE, Weber M and Vargas C (2000) Deflazacort increases laminin expression and myogenic repair, and induces early persistent functional gain in mdx mouse muscular dystrophy. Cell Transplant 9: 551-564.
    • (2000) Cell Transplant , vol.9 , pp. 551-564
    • Anderson, J.E.1    Weber, M.2    Vargas, C.3
  • 3
    • 0028238953 scopus 로고
    • Dexamethasone-mediated induction of mMTV-myf5 in DD3 myoblasts increases endogenous myogenin expression but does not transactivate myf5
    • Arnold TE, Worrell RA, Barth JL, Morris J and Ivarie R (1994) Dexamethasone-mediated induction of mMTV-myf5 in DD3 myoblasts increases endogenous myogenin expression but does not transactivate myf5. Exp Cell Res 212: 321-328.
    • (1994) Exp Cell Res , vol.212 , pp. 321-328
    • Arnold, T.E.1    Worrell, R.A.2    Barth, J.L.3    Morris, J.4    Ivarie, R.5
  • 4
    • 0029998009 scopus 로고    scopus 로고
    • Decreased antioxidant defence and increased oxidant stress during dexamethasone-induced apoptosis: bcl-2 prevents the loss of antioxidant enzyme activity
    • Baker AF, Briehl MM, Dorr R and Powis P (1996) Decreased antioxidant defence and increased oxidant stress during dexamethasone-induced apoptosis: bcl-2 prevents the loss of antioxidant enzyme activity. Cell Death Diff 3: 207-213.
    • (1996) Cell Death Diff , vol.3 , pp. 207-213
    • Baker, A.F.1    Briehl, M.M.2    Dorr, R.3    Powis, P.4
  • 6
    • 0018865567 scopus 로고
    • A synergistic effect of glucocorticoids and insulin on the differentiation of myoblasts
    • Ball EH and Sanwall BD (1980) A synergistic effect of glucocorticoids and insulin on the differentiation of myoblasts. J Cell Physiol 102: 27-36.
    • (1980) J Cell Physiol , vol.102 , pp. 27-36
    • Ball, E.H.1    Sanwall, B.D.2
  • 7
    • 0030851194 scopus 로고    scopus 로고
    • Calpain and calpastatin in myoblast differentiation and fusion: Effects of inhibitors
    • Barnoy S, Glaser T and Kosower NS (1997) Calpain and calpastatin in myoblast differentiation and fusion: effects of inhibitors. Biochem Biophys Acta 1358: 181-188.
    • (1997) Biochem Biophys Acta , vol.1358 , pp. 181-188
    • Barnoy, S.1    Glaser, T.2    Kosower, N.S.3
  • 8
    • 0032510276 scopus 로고    scopus 로고
    • The calpain-calpastatin system and protein degradation in fusing myoblasts
    • Barnoy S, Glaser T and Kosower NS (1998) The calpain-calpastatin system and protein degradation in fusing myoblasts. Biochem Biophys Acta 1402: 52-60.
    • (1998) Biochem Biophys Acta , vol.1402 , pp. 52-60
    • Barnoy, S.1    Glaser, T.2    Kosower, N.S.3
  • 10
    • 0025915530 scopus 로고
    • Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation
    • Bechet DM, Ferrara MJ, Mordier SB, Roux MP, Deval CD and Obled A (1991) Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. J Biol Chem 266: 14,104-14,112.
    • (1991) J Biol Chem , vol.266 , pp. 14104-14112
    • Bechet, D.M.1    Ferrara, M.J.2    Mordier, S.B.3    Roux, M.P.4    Deval, C.D.5    Obled, A.6
  • 11
    • 0032418502 scopus 로고    scopus 로고
    • Effects of glucocorticoids on oxidative stress-induced hippocampal cell death: Implications for the pathogenesis of Alzheimer's disease
    • Behl C (1998) Effects of glucocorticoids on oxidative stress-induced hippocampal cell death: implications for the pathogenesis of Alzheimer's disease. Exp Gerontol 33: 689-696.
    • (1998) Exp Gerontol , vol.33 , pp. 689-696
    • Behl, C.1
  • 12
    • 0033767375 scopus 로고    scopus 로고
    • Calcium-mediated proteolytic damage in white matter of hypothalamic rats?
    • Bigio MRD (2000) Calcium-mediated proteolytic damage in white matter of hypothalamic rats? J Neuropathol Exp Neurol 59: 946-954.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 946-954
    • Bigio, M.R.D.1
  • 14
    • 0030051802 scopus 로고    scopus 로고
    • Modulation of the antioxidant defence as a factor in apoptosis
    • Briehl MM and Baker AF (1996) Modulation of the antioxidant defence as a factor in apoptosis. Cell Death Diff 3: 63-70.
    • (1996) Cell Death Diff , vol.3 , pp. 63-70
    • Briehl, M.M.1    Baker, A.F.2
  • 16
    • 0029141988 scopus 로고
    • Downregulation of the antioxidant defence during glucocorticoid-mediated apoptosis
    • Briehl MM, Cotgrave IA and Powis P (1995) Downregulation of the antioxidant defence during glucocorticoid-mediated apoptosis. Cell Death Diff 2: 41-46.
    • (1995) Cell Death Diff , vol.2 , pp. 41-46
    • Briehl, M.M.1    Cotgrave, I.A.2    Powis, P.3
  • 18
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • Chua BT, Guo K and Li P (2000) Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J Biol Chem 275: 5131-5135.
    • (2000) J Biol Chem , vol.275 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 20
    • 0034733634 scopus 로고    scopus 로고
    • Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-κB
    • Du J, Mitch E, Wang X and Price SR (2000) Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-κB. J Biol Chem 275: 196,661-19,666.
    • (2000) J Biol Chem , vol.275 , pp. 196661-19666
    • Du, J.1    Mitch, E.2    Wang, X.3    Price, S.R.4
  • 21
    • 0032549222 scopus 로고    scopus 로고
    • Dexamethasone stimulates the expression of GLUT1 and GLUT4 proteins via different signalling pathways in L6 skeletal muscle cells
    • Ewart HS, Somwar R and Klip A (1998) Dexamethasone stimulates the expression of GLUT1 and GLUT4 proteins via different signalling pathways in L6 skeletal muscle cells. FEBS Lett 425: 179-183.
    • (1998) FEBS Lett , vol.425 , pp. 179-183
    • Ewart, H.S.1    Somwar, R.2    Klip, A.3
  • 22
    • 0034685026 scopus 로고    scopus 로고
    • The gene expression of ubiquitin ligase E3α is upregulated in skeletal muscle during sepsis in rats - Potential role of glucocorticoids
    • Fischer D, Sun X, Gang G, Pritts T and Hasselgren P-O (2000) The gene expression of ubiquitin ligase E3α is upregulated in skeletal muscle during sepsis in rats - potential role of glucocorticoids. Biochem Biophys Res Commun 267: 504-508.
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 504-508
    • Fischer, D.1    Sun, X.2    Gang, G.3    Pritts, T.4    Hasselgren, P.-O.5
  • 23
    • 0034193421 scopus 로고    scopus 로고
    • Calcineurin activity is required for the initiation of skeletal muscle differentiation
    • Friday BB, Horsley V and Pavlath GK (2000) Calcineurin activity is required for the initiation of skeletal muscle differentiation. J Cell Biol 149: 657-665.
    • (2000) J Cell Biol , vol.149 , pp. 657-665
    • Friday, B.B.1    Horsley, V.2    Pavlath, G.K.3
  • 24
    • 0033758751 scopus 로고    scopus 로고
    • N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome C release and apoptotic cell death
    • Gao G and Dou QP (2000) N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome C release and apoptotic cell death. J Cell Biochem 80: 53-70.
    • (2000) J Cell Biochem , vol.80 , pp. 53-70
    • Gao, G.1    Dou, Q.P.2
  • 26
    • 0028219361 scopus 로고
    • Thymocyte apoptosis induced by elevated endogenous corticosterone levels
    • Gruber J, Sgonc R, Hu YH, Beug H and Eick G (1994) Thymocyte apoptosis induced by elevated endogenous corticosterone levels. Eur J Immunol 24: 1115-1121.
    • (1994) Eur J Immunol , vol.24 , pp. 1115-1121
    • Gruber, J.1    Sgonc, R.2    Hu, Y.H.3    Beug, H.4    Eick, G.5
  • 27
    • 0032879088 scopus 로고    scopus 로고
    • Alanine or pyruvate is required for the development of myotubes from myoblasts and cortisol satisfies this requirement
    • Haba G, Khatami M, Cooper GW, Backlund P and Flaks JG (1999) Alanine or pyruvate is required for the development of myotubes from myoblasts and cortisol satisfies this requirement. Mol Cell Biochem 198: 163-170.
    • (1999) Mol Cell Biochem , vol.198 , pp. 163-170
    • Haba, G.1    Khatami, M.2    Cooper, G.W.3    Backlund, P.4    Flaks, J.G.5
  • 28
    • 0030921207 scopus 로고    scopus 로고
    • Relationship of dihydroepiandrosterone and cortisol in disease
    • Hechter O, Grossman A and Chatterton Jr RT (1997) Relationship of dihydroepiandrosterone and cortisol in disease. Med Hypoth 49: 85-91.
    • (1997) Med Hypoth , vol.49 , pp. 85-91
    • Hechter, O.1    Grossman, A.2    Chatterton R.T., Jr.3
  • 31
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson MD, Burne JF and Raff MC (1994) Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J 13: 1899-1910.
    • (1994) EMBO J , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burne, J.F.2    Raff, M.C.3
  • 32
    • 0035104587 scopus 로고    scopus 로고
    • Caspase 3 inhibition attenuates hydrogen peroxide-induced DNA fragmentation but not cell death in neuronal PC12 cells
    • Jiang D, Iha N, Boonplueang R and Andersen JK (2001) Caspase 3 inhibition attenuates hydrogen peroxide-induced DNA fragmentation but not cell death in neuronal PC12 cells. J Neurochem 76: 1745-1755.
    • (2001) J Neurochem , vol.76 , pp. 1745-1755
    • Jiang, D.1    Iha, N.2    Boonplueang, R.3    Andersen, J.K.4
  • 33
    • 0033869961 scopus 로고    scopus 로고
    • m-calpain levels increase during fusion of myoblasts in the mutant muscular dysgenesis (mdg) mouse
    • Joffroy S, Dourdin N, Delage J-P, Cottin P, Koenig J and Brustis J-J (2000) m-calpain levels increase during fusion of myoblasts in the mutant muscular dysgenesis (mdg) mouse. Int J Dev Biol 44: 421-428.
    • (2000) Int J Dev Biol , vol.44 , pp. 421-428
    • Joffroy, S.1    Dourdin, N.2    Delage, J.-P.3    Cottin, P.4    Koenig, J.5    Brustis, J.-J.6
  • 36
    • 0023261107 scopus 로고
    • Sensitivity of myofibryllar proteins to glucocorticoid-induced muscle proteolysis
    • Endocrinol. Metab. 15
    • Kayali AG, Young VR and Goodman MN (1987) Sensitivity of myofibryllar proteins to glucocorticoid-induced muscle proteolysis. Am J Physiol 252 (Endocrinol. Metab. 15): E621-E626.
    • (1987) Am J Physiol , vol.252
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 37
    • 0035104229 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid-mediated, caspase-independent dendritic cell death by CD40 activation
    • Kim KD, Choe Y-K, Choe IS and Lim J-S (2001) Inhibition of glucocorticoid-mediated, caspase-independent dendritic cell death by CD40 activation. J Leukoc Biol 69: 426-434.
    • (2001) J Leukoc Biol , vol.69 , pp. 426-434
    • Kim, K.D.1    Choe, Y.-K.2    Choe, I.S.3    Lim, J.-S.4
  • 38
    • 0035917828 scopus 로고    scopus 로고
    • Insulin-like growth factor 1 inhibits glucocorticoid-induced glutamine synthetase activity in cultured L6 rat skeletal muscle cells
    • Kimura K, Kanda F, Okuda S and Chihara K (2001) Insulin-like growth factor 1 inhibits glucocorticoid-induced glutamine synthetase activity in cultured L6 rat skeletal muscle cells. Neurosci Lett 302: 154-156.
    • (2001) Neurosci Lett , vol.302 , pp. 154-156
    • Kimura, K.1    Kanda, F.2    Okuda, S.3    Chihara, K.4
  • 41
    • 0028032677 scopus 로고
    • Regulatory mechanisms that coordinate skeletal muscle differentiation and cell cycle withdrawal
    • Lassar AB, Skapek SX and Novitch B (1994) Regulatory mechanisms that coordinate skeletal muscle differentiation and cell cycle withdrawal. Curr Opin Cell Biol 6: 788-794.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 788-794
    • Lassar, A.B.1    Skapek, S.X.2    Novitch, B.3
  • 42
    • 0034638844 scopus 로고    scopus 로고
    • Coordinate control of muscle cell survival by distinct insulin-like growth factor activated signaling pathways
    • Lawlor MA and Rotwein P (2000) Coordinate control of muscle cell survival by distinct insulin-like growth factor activated signaling pathways. J Cell Biol 151: 1131-1140.
    • (2000) J Cell Biol , vol.151 , pp. 1131-1140
    • Lawlor, M.A.1    Rotwein, P.2
  • 43
    • 0002903773 scopus 로고    scopus 로고
    • Degradation of methoxysuccinyl-phe-leu-phe-7-amido-4-trifluoromethyl coumarin (FLF) in cultured myotubes and HepG2 cells is proteasome- and calpain/calcium-dependent
    • Li BG, Fang CH and Hasselgren P-O (2000) Degradation of methoxysuccinyl-phe-leu-phe-7-amido-4-trifluoromethyl coumarin (FLF) in cultured myotubes and HepG2 cells is proteasome- and calpain/calcium-dependent. Int J Biochem Cell Biol 32: 677-686.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 677-686
    • Li, B.G.1    Fang, C.H.2    Hasselgren, P.-O.3
  • 44
    • 0033007118 scopus 로고    scopus 로고
    • Redox-dependent and redox-independent subcomponents of protein degradation in perfused myocardium
    • Lockwood TD (1999) Redox-dependent and redox-independent subcomponents of protein degradation in perfused myocardium. Am J Physiol Endocrinol Metab 276: E945-E954.
    • (1999) Am J Physiol Endocrinol Metab , vol.276
    • Lockwood, T.D.1
  • 45
    • 0034464839 scopus 로고    scopus 로고
    • A Delineation of the signaling pathways involved in glucocorticoid-induced and spontaneous apoptosis of rat thymocytes
    • Mann CL, Hughes FM and Cidlowski J (2000) A Delineation of the signaling pathways involved in glucocorticoid-induced and spontaneous apoptosis of rat thymocytes. Endocrinol 141: 528-538.
    • (2000) Endocrinol , vol.141 , pp. 528-538
    • Mann, C.L.1    Hughes, F.M.2    Cidlowski, J.3
  • 47
    • 0029972142 scopus 로고    scopus 로고
    • Opposing effects of glucocorticoids on the rate of apoptosis in neutrophilic and eosinophilic granulocytes
    • Meagher LC, Cousin JM, Seckl JR and Haslett C (1996) Opposing effects of glucocorticoids on the rate of apoptosis in neutrophilic and eosinophilic granulocytes. J Immunol 156: 4422-4428.
    • (1996) J Immunol , vol.156 , pp. 4422-4428
    • Meagher, L.C.1    Cousin, J.M.2    Seckl, J.R.3    Haslett, C.4
  • 48
    • 0018414849 scopus 로고
    • Calcium and the control of muscle specific creatine kinase accumulation during skeletal muscle differentiation in vitro
    • Morris GE and Cole RJ (1979) Calcium and the control of muscle specific creatine kinase accumulation during skeletal muscle differentiation in vitro. Dev Biol 69: 146-158.
    • (1979) Dev Biol , vol.69 , pp. 146-158
    • Morris, G.E.1    Cole, R.J.2
  • 50
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson DW (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Diff 6: 1028-1042.
    • (1999) Cell Death Diff , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 51
    • 0032540136 scopus 로고    scopus 로고
    • Structure and physiology of calpain, an enigmatic protease
    • Ono Y, Sorimachi H and Suzuki K (1998) Structure and physiology of calpain, an enigmatic protease. Biochem Biophys Res Commun 245: 289-294.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 289-294
    • Ono, Y.1    Sorimachi, H.2    Suzuki, K.3
  • 53
    • 0033755109 scopus 로고    scopus 로고
    • Glucocorticoid inhibition of C2C12 proliferation rate and differentiation capacity in relation to mRNA levels of the MRF gene family
    • Pas MFW, de Jong PR and Verburg FJ (2000) Glucocorticoid inhibition of C2C12 proliferation rate and differentiation capacity in relation to mRNA levels of the MRF gene family. Mol Biol Rep 27: 87-98.
    • (2000) Mol Biol Rep , vol.27 , pp. 87-98
    • Pas, M.F.W.1    De Jong, P.R.2    Verburg, F.J.3
  • 56
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy Type 2A
    • Richard I, Broux O and Allamand V (1995) Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy Type 2A. Cell 81: 27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3
  • 57
    • 0032845245 scopus 로고    scopus 로고
    • Melatonin regulates glucocorticoid receptor: An answer to its antiapoptotic action in thymus
    • Sainz RM, Mayo JC, Reiter RJ, Antolin I, Esteban MM and Rodriguez C (1999) Melatonin regulates glucocorticoid receptor: an answer to its antiapoptotic action in thymus. FASEB J 13: 1547-1556.
    • (1999) FASEB J , vol.13 , pp. 1547-1556
    • Sainz, R.M.1    Mayo, J.C.2    Reiter, R.J.3    Antolin, I.4    Esteban, M.M.5    Rodriguez, C.6
  • 58
    • 0032701375 scopus 로고    scopus 로고
    • Apoptosis of skeletal muscles during development and disease
    • Sandri M and Carraro U (1999) Apoptosis of skeletal muscles during development and disease. Int J Biochem Cell Biol 31: 1373-1390.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1373-1390
    • Sandri, M.1    Carraro, U.2
  • 59
    • 0030833040 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase-1 and -2 respond differently to mitogenic and differentiative signaling pathways in myoblasts
    • Sarbassov DD, Jones LG and Petersen CA (1997) Extracellular signal-regulated kinase-1 and -2 respond differently to mitogenic and differentiative signaling pathways in myoblasts. Mol Endocrinol 11: 2038-2047.
    • (1997) Mol Endocrinol , vol.11 , pp. 2038-2047
    • Sarbassov, D.D.1    Jones, L.G.2    Petersen, C.A.3
  • 60
    • 0031756168 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation
    • Sarbassov DD and Petersen CA (1998) Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation. Mol Endocrinol 12: 1870-1878.
    • (1998) Mol Endocrinol , vol.12 , pp. 1870-1878
    • Sarbassov, D.D.1    Petersen, C.A.2
  • 61
    • 0033512552 scopus 로고    scopus 로고
    • Effects of serum deprivation, insulin and dexamethasone on polysome percentages in C2C12 myoblasts and differentiating myoblasts
    • Smith CW, Klaasmeyer JG, Edeal JB, Woods TL and Jones SJ (1999) Effects of serum deprivation, insulin and dexamethasone on polysome percentages in C2C12 myoblasts and differentiating myoblasts. Tissue Cell 31: 451-458.
    • (1999) Tissue Cell , vol.31 , pp. 451-458
    • Smith, C.W.1    Klaasmeyer, J.G.2    Edeal, J.B.3    Woods, T.L.4    Jones, S.J.5
  • 62
    • 0029916919 scopus 로고    scopus 로고
    • Regulation of calcium binding proteins calreticulin and calsequestrin during differentiation in the myogenic cell line L6
    • Tharin S, Hamel PA, Conway EM, Michalak M and Opas M (1996) Regulation of calcium binding proteins calreticulin and calsequestrin during differentiation in the myogenic cell line L6. J Cell Physiol 166: 547-560.
    • (1996) J Cell Physiol , vol.166 , pp. 547-560
    • Tharin, S.1    Hamel, P.A.2    Conway, E.M.3    Michalak, M.4    Opas, M.5
  • 63
    • 0028362689 scopus 로고
    • Apoptosis and steroid hormones
    • Thompson EB (1994) Apoptosis and steroid hormones. Mol Endocrinol 8: 665-673.
    • (1994) Mol Endocrinol , vol.8 , pp. 665-673
    • Thompson, E.B.1
  • 64
    • 0032694911 scopus 로고    scopus 로고
    • Stimulation of myofobrillar protein degradation and expression of mRNA encoding the ubiquitin-proteasome system in C2C12 myotubes by dexamethasone: Effect of the proteasome inhibitor MG-132
    • Thompson MG, Thom A, Partridge K, Garden K, Campbell GP, Calder G and Palmer RM (1999) Stimulation of myofobrillar protein degradation and expression of mRNA encoding the ubiquitin-proteasome system in C2C12 myotubes by dexamethasone: effect of the proteasome inhibitor MG-132. J Cell Physiol 181: 455-461.
    • (1999) J Cell Physiol , vol.181 , pp. 455-461
    • Thompson, M.G.1    Thom, A.2    Partridge, K.3    Garden, K.4    Campbell, G.P.5    Calder, G.6    Palmer, R.M.7
  • 65
    • 0031967414 scopus 로고    scopus 로고
    • The anti-catabolic efficacy of insulin-like growth factor-I is enhanced by its early administration to rats receiving dexamethasone
    • Tomas FM (1998) The anti-catabolic efficacy of insulin-like growth factor-I is enhanced by its early administration to rats receiving dexamethasone. J Endocrinol 157: 89-97.
    • (1998) J Endocrinol , vol.157 , pp. 89-97
    • Tomas, F.M.1
  • 66
    • 0035866773 scopus 로고    scopus 로고
    • Catalase-overexpressing thymocytes are resistant to glucocorticoid-induced apoptosis and exhibit increased net tumor growth
    • Tome ME, Baker AF, Powis G, Payne CM and Briehl MM (2001) Catalase-overexpressing thymocytes are resistant to glucocorticoid-induced apoptosis and exhibit increased net tumor growth. Cancer Res 61: 2766-2773.
    • (2001) Cancer Res , vol.61 , pp. 2766-2773
    • Tome, M.E.1    Baker, A.F.2    Powis, G.3    Payne, C.M.4    Briehl, M.M.5
  • 68
    • 0031969695 scopus 로고    scopus 로고
    • Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis
    • Villa PG, Henzel WJ, Sensebrenner M, Henderson CE and Pettmann B (1998) Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis. J Cell Sci 111: 713-722.
    • (1998) J Cell Sci , vol.111 , pp. 713-722
    • Villa, P.G.1    Henzel, W.J.2    Sensebrenner, M.3    Henderson, C.E.4    Pettmann, B.5
  • 69
    • 0032185015 scopus 로고    scopus 로고
    • Dexamethasone stimulates proteasome-, and calcium-dependent proteolysis in cultured L6 myotubes
    • Wang L, Luo G-J, Wang J-J and Hasselgren P-O (1998) Dexamethasone stimulates proteasome-, and calcium-dependent proteolysis in cultured L6 myotubes. Shock 10: 298-306.
    • (1998) Shock , vol.10 , pp. 298-306
    • Wang, L.1    Luo, G.-J.2    Wang, J.-J.3    Hasselgren, P.-O.4
  • 70
    • 0031443677 scopus 로고    scopus 로고
    • Calpains mediate calcium and chloride influx during the late phase of cell injury
    • Waters SL, Sarang SS, Wang KKW and Schnellmann RG (1997) Calpains mediate calcium and chloride influx during the late phase of cell injury. J Pharmacol Exp Therap 283: 1177-1184.
    • (1997) J Pharmacol Exp Therap , vol.283 , pp. 1177-1184
    • Waters, S.L.1    Sarang, S.S.2    Wang, K.K.W.3    Schnellmann, R.G.4
  • 71
    • 0032528180 scopus 로고    scopus 로고
    • Inhibition of osteoblastogenesis and promotion of apoptosis of osteoblasts and osteocytes by glucocorticoids. Potential mechanisms of their deleterious effects on bone
    • Weinstein RS, Jilka RL, Parfitt AM and Manolagas SC (1998) Inhibition of osteoblastogenesis and promotion of apoptosis of osteoblasts and osteocytes by glucocorticoids. Potential mechanisms of their deleterious effects on bone. J Clin Invest 102: 274-282.
    • (1998) J Clin Invest , vol.102 , pp. 274-282
    • Weinstein, R.S.1    Jilka, R.L.2    Parfitt, A.M.3    Manolagas, S.C.4
  • 72
    • 0027214875 scopus 로고
    • cAMP-dependent protein kinase represses myogenic differentiation and the activity of the muscle-specific helix-loop-helix transcription factors Myf-5 and MyoD
    • Winter B, Braun T and Arnold HH (1993) cAMP-dependent protein kinase represses myogenic differentiation and the activity of the muscle-specific helix-loop-helix transcription factors Myf-5 and MyoD. J Biol Chem 268: 9869-9878.
    • (1993) J Biol Chem , vol.268 , pp. 9869-9878
    • Winter, B.1    Braun, T.2    Arnold, H.H.3
  • 73
    • 0034739734 scopus 로고    scopus 로고
    • Implications of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T (2000) Implications of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog Neurobiol 62: 273-295.
    • (2000) Prog Neurobiol , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 74
    • 0028292562 scopus 로고
    • Effects of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits
    • Yeh J-Y, Ou B-R and Forsberg NE (1994) Effects of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits. J Endocrinol 141: 209-217.
    • (1994) J Endocrinol , vol.141 , pp. 209-217
    • Yeh, J.-Y.1    Ou, B.-R.2    Forsberg, N.E.3
  • 75
    • 0025613973 scopus 로고
    • Programmed T lymphocyte death. Cell activation- and steroid-induced pathways are mutually antagonistic
    • Zacharchuk CM, Mercep M, Chakraborti PK, Simons Jr SS and Ashwell JD (1990) Programmed T lymphocyte death. Cell activation- and steroid-induced pathways are mutually antagonistic. J Immunol 145: 4037-4045.
    • (1990) J Immunol , vol.145 , pp. 4037-4045
    • Zacharchuk, C.M.1    Mercep, M.2    Chakraborti, P.K.3    Simons S.S., Jr.4    Ashwell, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.