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Volumn 11, Issue 2, 2006, Pages 143-149

Cathepsin-regulated apoptosis

Author keywords

Apoptosis; Cathepsins; Lysosome; Protease

Indexed keywords

BLEOMYCIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN L; ENZYME INHIBITOR; LYSOSOME ENZYME;

EID: 33344457969     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10495-006-3486-y     Document Type: Review
Times cited : (358)

References (67)
  • 1
    • 0028673152 scopus 로고
    • Classification of peptidases
    • Barrett AJ. Classification of peptidases. Methods Enzymol 1994; 244: 1-18.
    • (1994) Methods Enzymol , vol.244 , pp. 1-18
    • Barrett, A.J.1
  • 4
    • 0028923541 scopus 로고
    • Alingment/Phylogeny of the papain superfamily of cysteine proteases
    • Berti PJ, Storer AC. Alingment/Phylogeny of the papain superfamily of cysteine proteases. J Mol Biol 1995; 246: 273-283.
    • (1995) J Mol Biol , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 6
    • 0027238714 scopus 로고
    • Secretion of cathepsin B by human gliomas in vitro
    • McCormick D. Secretion of cathepsin B by human gliomas in vitro. Neuropathol Appl Neurobiol 1993; 19: 146-151.
    • (1993) Neuropathol Appl Neurobiol , vol.19 , pp. 146-151
    • McCormick, D.1
  • 8
    • 0022783474 scopus 로고
    • What is apoptosis?
    • Wyllie AH. What is apoptosis? Histopathology 1986; 10: 995-998.
    • (1986) Histopathology , vol.10 , pp. 995-998
    • Wyllie, A.H.1
  • 9
    • 0034641898 scopus 로고    scopus 로고
    • CD95's deadly mission in the immune system
    • Krammer PH. CD95's deadly mission in the immune system. Nature 2000; 407: 789-795.
    • (2000) Nature , vol.407 , pp. 789-795
    • Krammer, P.H.1
  • 10
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 11
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 12
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 13
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 14
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20: 929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 15
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T. Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog Neurobiol 2000; 62: 273-295.
    • (2000) Prog Neurobiol , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 16
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF, Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 2001; 3: E255-E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 17
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • Brunk UT, Neuzil J, Eaton JW. Lysosomal involvement in apoptosis. Redox Rep 2001; 6: 91-97.
    • (2001) Redox Rep , vol.6 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 18
    • 0033538073 scopus 로고    scopus 로고
    • Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling
    • Schutze S, Machleidt T, Adam D, et al. Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. J Biological Chem 1999; 274: 10203-10212.
    • (1999) J Biological Chem , vol.274 , pp. 10203-10212
    • Schutze, S.1    Machleidt, T.2    Adam, D.3
  • 19
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K, Zhao M, Svensson I, Brunk UT. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem J 2001; 359: 335-343.
    • (2001) Biochem J , vol.359 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 21
    • 0033214095 scopus 로고    scopus 로고
    • Cathepsin D targeted by acid sphingomyelinase-derived ceramide
    • Heinrich M, Wickel M, Schneider-Brachert W, et al. Cathepsin D targeted by acid sphingomyelinase-derived ceramide. EMBO J 1999; 18: 5252-5263.
    • (1999) EMBO J , vol.18 , pp. 5252-5263
    • Heinrich, M.1    Wickel, M.2    Schneider-Brachert, W.3
  • 24
  • 25
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M, Antunes F, Eaton JW, Brunk UT. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur J Biochem 2003; 270: 3778-3786.
    • (2003) Eur J Biochem , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 26
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • Zhao M, Brunk UT, Eaton JW. Delayed oxidant-induced cell death involves activation of phospholipase A2. FEBS Lett 2001; 509: 399-404.
    • (2001) FEBS Lett , vol.509 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3
  • 28
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N, Lorenzo HK, Carmona S, et al. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biological Chem 2003; 278: 31401-31411.
    • (2003) J Biological Chem , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3
  • 29
    • 0037115547 scopus 로고    scopus 로고
    • Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion
    • Nylandsted J, Wick W, Hirt UA, et al. Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion. Cancer Res 2002; 62: 7139-7142.
    • (2002) Cancer Res , vol.62 , pp. 7139-7142
    • Nylandsted, J.1    Wick, W.2    Hirt, U.A.3
  • 30
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis: Cleavage of bid, not Pro-caspases, is the most likely route
    • Stoka V, Turk B, Schendel SL, et al. Lysosomal protease pathways to apoptosis: cleavage of bid, not Pro-caspases, is the most likely route. J Biological Chem 2000; 276: 3149-3157.
    • (2000) J Biological Chem , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3
  • 31
    • 0348038755 scopus 로고    scopus 로고
    • Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
    • Houseweart MK, Vilaythong A, Yin XM, Turk B, Noebels JL, Myers RM. Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1). Cell Death Differ 2003; 10: 1329-1335.
    • (2003) Cell Death Differ , vol.10 , pp. 1329-1335
    • Houseweart, M.K.1    Vilaythong, A.2    Yin, X.M.3    Turk, B.4    Noebels, J.L.5    Myers, R.M.6
  • 32
    • 0141753121 scopus 로고    scopus 로고
    • NF-kappaB protects from the lysosomal pathway of cell death
    • Liu N, Raja SM, Zazzeroni F, et al. NF-kappaB protects from the lysosomal pathway of cell death. EMBO J 2003; 22: 5313-5322.
    • (2003) EMBO J , vol.22 , pp. 5313-5322
    • Liu, N.1    Raja, S.M.2    Zazzeroni, F.3
  • 33
    • 0030862412 scopus 로고    scopus 로고
    • Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes
    • Roberts LR, Kurosawa H, Bronk SF, et al. Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes. Gastroenterology 1997; 113: 1714-1726.
    • (1997) Gastroenterology , vol.113 , pp. 1714-1726
    • Roberts, L.R.1    Kurosawa, H.2    Bronk, S.F.3
  • 34
    • 0031753981 scopus 로고    scopus 로고
    • Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line
    • Jones B, Roberts PJ, Faubion WA, Kominami E, Gores GJ. Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line. Am J Physiol 1998; 275: G723-G730.
    • (1998) Am J Physiol , vol.275
    • Jones, B.1    Roberts, P.J.2    Faubion, W.A.3    Kominami, E.4    Gores, G.J.5
  • 35
    • 0032919402 scopus 로고    scopus 로고
    • Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas
    • Faubion WA, Guicciardi ME, Miyoshi H, et al. Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas. J Clin Invest 1999; 103: 137-145.
    • (1999) J Clin Invest , vol.103 , pp. 137-145
    • Faubion, W.A.1    Guicciardi, M.E.2    Miyoshi, H.3
  • 36
    • 0032899887 scopus 로고    scopus 로고
    • Death receptors in liver biology and pathobiology
    • Faubion WA, Gores GJ. Death receptors in liver biology and pathobiology. Hepatology 1999; 29: 1-4.
    • (1999) Hepatology , vol.29 , pp. 1-4
    • Faubion, W.A.1    Gores, G.J.2
  • 38
    • 0031793017 scopus 로고    scopus 로고
    • Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity
    • Vancompernolle K, Van Herreweghe F, Pynaert G, et al. Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett 1998; 438: 150-158.
    • (1998) FEBS Lett , vol.438 , pp. 150-158
    • Vancompernolle, K.1    Van Herreweghe, F.2    Pynaert, G.3
  • 39
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • Guicciardi ME, Deussing J, Miyoshi H, et al. Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J Clin Infest 2000; 106: 1127-1137.
    • (2000) J Clin Infest , vol.106 , pp. 1127-1137
    • Guicciardi, M.E.1    Deussing, J.2    Miyoshi, H.3
  • 40
    • 0035180207 scopus 로고    scopus 로고
    • Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: Implications for therapeutic applications
    • Guicciardi ME, Miyoshi H, Bronk SF, Gores GJ. Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: Implications for therapeutic applications. American J Pathol 2001; 159: 2045-2054.
    • (2001) American J Pathol , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 41
    • 0042744006 scopus 로고    scopus 로고
    • Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis
    • Canbay A, Guicciardi ME, Higuchi H, et al. Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis. J Clin Invest. 2003; 112: 152-159.
    • (2003) J Clin Invest , vol.112 , pp. 152-159
    • Canbay, A.1    Guicciardi, M.E.2    Higuchi, H.3
  • 42
    • 12344303157 scopus 로고    scopus 로고
    • Cathepsin B inactivation attenuates hepatocyte apoptosis and liver damage in steatotic livers after cold ischemia-warm reperfusion injury
    • Baskin-Bey ES, Canbay A, Bronk SF, et al. Cathepsin B inactivation attenuates hepatocyte apoptosis and liver damage in steatotic livers after cold ischemia-warm reperfusion injury. Am J Physiol Gastrointest. Liver Physiol. 2005; 288: G396-G402.
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.288
    • Baskin-Bey, E.S.1    Canbay, A.2    Bronk, S.F.3
  • 43
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M, Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol 2003; 4: 416-423.
    • (2003) Nat Immunol , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 44
    • 0242579153 scopus 로고    scopus 로고
    • Cathepsin-B-dependent apoptosis triggered by antithymocyte globulins: A novel mechanism of T-cell depletion
    • Michallet MC, Saltel F, Preville X, Flacher M, Revillard JP, Genestier L. Cathepsin-B-dependent apoptosis triggered by antithymocyte globulins: A novel mechanism of T-cell depletion. Blood 2003; 102: 3719-3726.
    • (2003) Blood , vol.102 , pp. 3719-3726
    • Michallet, M.C.1    Saltel, F.2    Preville, X.3    Flacher, M.4    Revillard, J.P.5    Genestier, L.6
  • 45
    • 2142773262 scopus 로고    scopus 로고
    • Cathepsin-dependent apoptosis triggered by supraoptimal activation of T lymphocytes: A possible mechanism of high dose tolerance
    • Michallet MC, Saltel F, Flacher M, Revillard JP, Genestier L. Cathepsin-dependent apoptosis triggered by supraoptimal activation of T lymphocytes: A possible mechanism of high dose tolerance. J Immunol 2004; 172: 5405-5414.
    • (2004) J Immunol , vol.172 , pp. 5405-5414
    • Michallet, M.C.1    Saltel, F.2    Flacher, M.3    Revillard, J.P.4    Genestier, L.5
  • 47
    • 0028215537 scopus 로고
    • T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis
    • Critchfield JM, Racke MK, Zuniga-Pflucker JC, et al. T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis. Science 1994; 263: 1139-1143.
    • (1994) Science , vol.263 , pp. 1139-1143
    • Critchfield, J.M.1    Racke, M.K.2    Zuniga-Pflucker, J.C.3
  • 48
    • 0033566826 scopus 로고    scopus 로고
    • Strong TCR ligation without costimulation causes rapid onset of Fas-dependent apoptosis of naive murine CD4+ T cells
    • Kishimoto H, Sprent J. Strong TCR ligation without costimulation causes rapid onset of Fas-dependent apoptosis of naive murine CD4+ T cells. J Immunol 1999; 163: 1817-1826.
    • (1999) J Immunol , vol.163 , pp. 1817-1826
    • Kishimoto, H.1    Sprent, J.2
  • 49
    • 0029813121 scopus 로고    scopus 로고
    • Role of antigen, CD8, and cytotoxic T lymphocyte (CTL) avidity in high dose antigen induction of apoptosis of effector CTL
    • Alexander-Miller MA, Leggatt GR, Sarin A, Berzofsky JA. Role of antigen, CD8, and cytotoxic T lymphocyte (CTL) avidity in high dose antigen induction of apoptosis of effector CTL. J Experimen Med 1996; 184: 485-492.
    • (1996) J Experimen Med , vol.184 , pp. 485-492
    • Alexander-Miller, M.A.1    Leggatt, G.R.2    Sarin, A.3    Berzofsky, J.A.4
  • 50
    • 0032547813 scopus 로고    scopus 로고
    • Supraoptimal peptide-major histocompatibility complex causes a decrease in bcl-2 levels and allows tumor necrosis factor alpha receptor II-mediated apoptosis of cytotoxic T lymphocytes
    • Alexander-Miller MA, Derby MA, Sarin A, Henkart PA, Berzofsky JA. Supraoptimal peptide-major histocompatibility complex causes a decrease in bcl-2 levels and allows tumor necrosis factor alpha receptor II-mediated apoptosis of cytotoxic T lymphocytes. J Experiment Med 1998; 19; 1391-1399.
    • (1998) J Experiment Med , vol.19 , pp. 1391-1399
    • Alexander-Miller, M.A.1    Derby, M.A.2    Sarin, A.3    Henkart, P.A.4    Berzofsky, J.A.5
  • 51
    • 0141794528 scopus 로고    scopus 로고
    • B cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity
    • Mlinaric-Rascan I, Turk B. B cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity. FEBS Lett 2003; 553: 51-55.
    • (2003) FEBS Lett , vol.553 , pp. 51-55
    • Mlinaric-Rascan, I.1    Turk, B.2
  • 52
    • 0037062449 scopus 로고    scopus 로고
    • Neuronal loss and brain atrophy in mice lacking cathepsins B and L
    • Felbor U, Kessler B, Mothes W, et al. Neuronal loss and brain atrophy in mice lacking cathepsins B and L. Proc Natl Acad Sci USA 2002; 99: 7883-7888.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7883-7888
    • Felbor, U.1    Kessler, B.2    Mothes, W.3
  • 53
    • 0032500842 scopus 로고    scopus 로고
    • Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation
    • Shibata M, Kanamori S, Isahara K, et al. Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation. Biochem Biophys Res Communications 1998; 251: 199-203.
    • (1998) Biochem Biophys Res Communications , vol.251 , pp. 199-203
    • Shibata, M.1    Kanamori, S.2    Isahara, K.3
  • 54
    • 0028924890 scopus 로고
    • Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis
    • Nitatori T, Sato N, Waguri S, et al. Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis. J Neurosci 1995; 15: 1001-1011.
    • (1995) J Neurosci , vol.15 , pp. 1001-1011
    • Nitatori, T.1    Sato, N.2    Waguri, S.3
  • 55
    • 4344699813 scopus 로고    scopus 로고
    • Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells
    • Wille A, Gerber A, Heimburg A, et al. Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells. Biol Chem 2004; 385: 665-670.
    • (2004) Biol Chem , vol.385 , pp. 665-670
    • Wille, A.1    Gerber, A.2    Heimburg, A.3
  • 56
    • 0023943263 scopus 로고
    • Cathepsin D is membrane-associated in macrophage endosomes
    • Diment S, Leech MS, Stahl PD. Cathepsin D is membrane-associated in macrophage endosomes. J Biological Chem 1988; 263: 6901-6907.
    • (1988) J Biological Chem , vol.263 , pp. 6901-6907
    • Diment, S.1    Leech, M.S.2    Stahl, P.D.3
  • 57
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-α
    • Deiss LP, Galinka H, Berissi H, Cohen O, Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-α. EMBO J 1996; 15: 3861-3870.
    • (1996) EMBO J , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 58
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts
    • Roberg K, Kagedal K, Ollinger K. Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. Am J Pathol 2002; 161: 89-96.
    • (2002) Am J Pathol , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Ollinger, K.3
  • 59
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu GS, Saftig P, Peters C, El-Deiry WS. Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity. Oncogene 1998; 16: 2177-2183.
    • (1998) Oncogene , vol.16 , pp. 2177-2183
    • Wu, G.S.1    Saftig, P.2    Peters, C.3    El-Deiry, W.S.4
  • 60
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kagedal K, Johansson U, Ollinger K. The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J 2001; 15: 1592-1594.
    • (2001) FASEB J , vol.15 , pp. 1592-1594
    • Kagedal, K.1    Johansson, U.2    Ollinger, K.3
  • 61
    • 0242609099 scopus 로고    scopus 로고
    • Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine
    • Johansson AC, Steen H, Ollinger K, Roberg K. Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine. Cell Death Differ 2003; 10: 1253-1259.
    • (2003) Cell Death Differ , vol.10 , pp. 1253-1259
    • Johansson, A.C.1    Steen, H.2    Ollinger, K.3    Roberg, K.4
  • 63
    • 0024435378 scopus 로고
    • Acute pulmonary toxicity of bleomycin: DNA scission and matrix protein mRNA levels in bleomycin-sensitive and -resistant strains of mice
    • Harrison JH Jr, Hoyt DG, Lazo JS. Acute pulmonary toxicity of bleomycin: DNA scission and matrix protein mRNA levels in bleomycin-sensitive and -resistant strains of mice. Mol Pharmacol 1989; 36: 231-238.
    • (1989) Mol Pharmacol , vol.36 , pp. 231-238
    • Harrison Jr., J.H.1    Hoyt, D.G.2    Lazo, J.S.3
  • 65
    • 0345707635 scopus 로고    scopus 로고
    • Essential roles for angiotensin receptor AT1a in bleomycin-induced apoptosis and lung fibrosis in mice
    • Li X, Rayford H, Uhal BD. Essential roles for angiotensin receptor AT1a in bleomycin-induced apoptosis and lung fibrosis in mice. Am J Pathol 2003; 163: 2523-2530.
    • (2003) Am J Pathol , vol.163 , pp. 2523-2530
    • Li, X.1    Rayford, H.2    Uhal, B.D.3
  • 66
    • 0242331711 scopus 로고    scopus 로고
    • Silica Induced Caspase Activation in Mouse Alveolar Macrophages Is Dependent upon Mitochondrial Integrity and Aspartic Proteolysis
    • Thibodeau M, Giardina C, Hubbard AK. Silica Induced Caspase Activation in Mouse Alveolar Macrophages Is Dependent upon Mitochondrial Integrity and Aspartic Proteolysis. Toxicol Sci 2003; 76: 91-101.
    • (2003) Toxicol Sci , vol.76 , pp. 91-101
    • Thibodeau, M.1    Giardina, C.2    Hubbard, A.K.3
  • 67
    • 3242808193 scopus 로고    scopus 로고
    • Silica-induced apoptosis in mouse alveolar macrophages is initiated by lysosomal enzyme activity
    • Thibodeau MS, Giardina C, Knecht DA, Helble J, Hubbard AK. Silica-induced apoptosis in mouse alveolar macrophages is initiated by lysosomal enzyme activity. Toxicol Sci 2004; 80: 34-48.
    • (2004) Toxicol Sci , vol.80 , pp. 34-48
    • Thibodeau, M.S.1    Giardina, C.2    Knecht, D.A.3    Helble, J.4    Hubbard, A.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.