메뉴 건너뛰기




Volumn 42, Issue 9, 2007, Pages 1305-1316

Cathepsin D-Bax death pathway in oxidative stressed neuroblastoma cells

Author keywords

Apoptosis; Caspases; Lysosomes; Mitochondria; Neurodegeneration; Oxidative stress

Indexed keywords

4',6 DIAMIDINO 2 PHENYLINDOLE; CASPASE; CATHEPSIN B; CATHEPSIN D; DEFEROXAMINE; HYDROGEN PEROXIDE; IRON CHELATING AGENT; PROTEIN BAX; SMALL INTERFERING RNA; TUBULIN;

EID: 33947537430     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.12.030     Document Type: Article
Times cited : (82)

References (42)
  • 1
    • 0036298650 scopus 로고    scopus 로고
    • Healty people 2010-leading health indicators for women
    • Malese D.R. Healty people 2010-leading health indicators for women. Womens Health Issues 12 (2002) 155-164
    • (2002) Womens Health Issues , vol.12 , pp. 155-164
    • Malese, D.R.1
  • 2
    • 0029433496 scopus 로고
    • The history of iron in the brain
    • Koeppen A.H. The history of iron in the brain. J. Neurol. Sci. 134 (1995) 1-9
    • (1995) J. Neurol. Sci. , vol.134 , pp. 1-9
    • Koeppen, A.H.1
  • 3
    • 0014878377 scopus 로고
    • Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver
    • Brun A., and Brunk U.T. Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver. J. Histochem. Cytochem. 18 (1970) 820-827
    • (1970) J. Histochem. Cytochem. , vol.18 , pp. 820-827
    • Brun, A.1    Brunk, U.T.2
  • 4
    • 0028360648 scopus 로고
    • Most free-radical injury is iron-related: it is promoted by iron, hemin, holoferritin and vitamin C, and inhibited by desferoxamine and apoferitin
    • Herbert V., Shaw S., Jayatilleke E., and Stopler-Kasdan T. Most free-radical injury is iron-related: it is promoted by iron, hemin, holoferritin and vitamin C, and inhibited by desferoxamine and apoferitin. Stem Cells 12 (1994) 289-303
    • (1994) Stem Cells , vol.12 , pp. 289-303
    • Herbert, V.1    Shaw, S.2    Jayatilleke, E.3    Stopler-Kasdan, T.4
  • 5
    • 0033751421 scopus 로고    scopus 로고
    • Metabolic, metallic, and mitotic sources of oxidatives stress in Alzheimer disease
    • Smith M.A., Nunomura A., Zhu X., Takeda A., and Perry G. Metabolic, metallic, and mitotic sources of oxidatives stress in Alzheimer disease. Antioxid. Redox Signal. 2 (2000) 413-420
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 413-420
    • Smith, M.A.1    Nunomura, A.2    Zhu, X.3    Takeda, A.4    Perry, G.5
  • 6
    • 0023878906 scopus 로고
    • Effects of 6-hydroxydopamine on oxidative phosphorylation of mitochondria from rat striatum, cortex, and liver
    • Thakar J.H., and Hassan M.N. Effects of 6-hydroxydopamine on oxidative phosphorylation of mitochondria from rat striatum, cortex, and liver. Can. J. Physiol. Pharmacol. 66 4 (1988) 376-379
    • (1988) Can. J. Physiol. Pharmacol. , vol.66 , Issue.4 , pp. 376-379
    • Thakar, J.H.1    Hassan, M.N.2
  • 7
    • 0029035056 scopus 로고
    • Differential sensitivity to hydrogen peroxide of dopaminergic and noradrenergic neurotransmission in rat brain slices
    • Langeveld C.H., Schepens E., Stoof J.C., Bast A., and Drukarch B. Differential sensitivity to hydrogen peroxide of dopaminergic and noradrenergic neurotransmission in rat brain slices. Free Radic. Biol. Med. 9 2 (1995) 209-217
    • (1995) Free Radic. Biol. Med. , vol.9 , Issue.2 , pp. 209-217
    • Langeveld, C.H.1    Schepens, E.2    Stoof, J.C.3    Bast, A.4    Drukarch, B.5
  • 8
    • 0031840571 scopus 로고    scopus 로고
    • Roles of lipid peroxidation in modulation of cellular signalling pathways, cell dysfunction, and death in the nervous system
    • Keller J.N., and Mattson M.P. Roles of lipid peroxidation in modulation of cellular signalling pathways, cell dysfunction, and death in the nervous system. Rev. Neurosci. 9 (1998) 105-116
    • (1998) Rev. Neurosci. , vol.9 , pp. 105-116
    • Keller, J.N.1    Mattson, M.P.2
  • 9
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier T.C. Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36 (2001) 1539-1550
    • (2001) Exp. Gerontol. , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 10
    • 0036710886 scopus 로고    scopus 로고
    • Mechanisms of aging: appraisal of the oxidative stress hypothesis
    • Sohal R.S., Mockett R.J., and Orr W.C. Mechanisms of aging: appraisal of the oxidative stress hypothesis. Free Radic. Biol. Med. 33 (2002) 575-586
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 575-586
    • Sohal, R.S.1    Mockett, R.J.2    Orr, W.C.3
  • 11
    • 0344392786 scopus 로고    scopus 로고
    • Antioxidant effect of phenelzine on MPP+-induced cell viability loss in differentiated PC12 cells
    • Lee C.S., Han E.S., and Lee W.B. Antioxidant effect of phenelzine on MPP+-induced cell viability loss in differentiated PC12 cells. Neurochem. Res. 28 12 (2003) 1833-1841
    • (2003) Neurochem. Res. , vol.28 , Issue.12 , pp. 1833-1841
    • Lee, C.S.1    Han, E.S.2    Lee, W.B.3
  • 12
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle J.T., and Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 262 5134 (1993) 689-695
    • (1993) Science , vol.262 , Issue.5134 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 13
    • 0031587950 scopus 로고    scopus 로고
    • Processing of Alzheimer's amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells
    • Zhang L., Zhao B., Yew D.T., Kusiak J.W., and Roth G.S. Processing of Alzheimer's amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells. Biochem. Biophys. Res. Commun. 235 (1997) 845-848
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 845-848
    • Zhang, L.1    Zhao, B.2    Yew, D.T.3    Kusiak, J.W.4    Roth, G.S.5
  • 14
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells
    • Misonou H., Morishima-Kawashima M., and Ihara Y. Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells. Biochemistry 39 23 (2000) 6951-6959
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    Ihara, Y.3
  • 16
    • 28844500817 scopus 로고    scopus 로고
    • High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells
    • Demòz M., Castino R., Follo C., Hasilik A., Sloane B.F., and Isidoro C. High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells. Protein Expr. Purif. 45 1 (2006) 157-167
    • (2006) Protein Expr. Purif. , vol.45 , Issue.1 , pp. 157-167
    • Demòz, M.1    Castino, R.2    Follo, C.3    Hasilik, A.4    Sloane, B.F.5    Isidoro, C.6
  • 17
    • 0141907718 scopus 로고    scopus 로고
    • Destination 'lysosome': a target organelle for tumour cell killing?
    • Castino R., Demòz M., and Isidoro C. Destination 'lysosome': a target organelle for tumour cell killing?. J. Mol. Recognit. 16 (2003) 337-348
    • (2003) J. Mol. Recognit. , vol.16 , pp. 337-348
    • Castino, R.1    Demòz, M.2    Isidoro, C.3
  • 18
    • 0036801288 scopus 로고    scopus 로고
    • Photosensitized oxidation of 2′,7′-dichlorofluorescin: singlet oxygen does not contribute to the formation of fluorescent oxidation product 2′,7′-dichlorofluorescein
    • Bilski P., Belanger A.G., and Chignell C.F. Photosensitized oxidation of 2′,7′-dichlorofluorescin: singlet oxygen does not contribute to the formation of fluorescent oxidation product 2′,7′-dichlorofluorescein. Free Radic. Biol. Med. 33 (2002) 938-946
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 938-946
    • Bilski, P.1    Belanger, A.G.2    Chignell, C.F.3
  • 19
    • 0742289483 scopus 로고    scopus 로고
    • Lysosomes and mitochondria in the commitment to apoptosis: a potential role for cathepsin D and AIF
    • Jaattela M., Cande C., and Kroemer G. Lysosomes and mitochondria in the commitment to apoptosis: a potential role for cathepsin D and AIF. Cell Death Differ. 11 2 (2004) 135-136
    • (2004) Cell Death Differ. , vol.11 , Issue.2 , pp. 135-136
    • Jaattela, M.1    Cande, C.2    Kroemer, G.3
  • 20
    • 0021337104 scopus 로고
    • Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site
    • Graf E., Mahoney J.R., Bryant R.G., and Eaton J.W. Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site. J. Biol. Chem. 259 6 (1984) 3620362-3620364
    • (1984) J. Biol. Chem. , vol.259 , Issue.6 , pp. 3620362-3620364
    • Graf, E.1    Mahoney, J.R.2    Bryant, R.G.3    Eaton, J.W.4
  • 21
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • Brunk U.T., Neuzil J., and Eaton J.W. Lysosomal involvement in apoptosis. Redox Rep. 6 (2001) 91-97
    • (2001) Redox Rep. , vol.6 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 22
    • 0021813287 scopus 로고
    • Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization
    • Laub R., Schneider Y.J., Octave J.N., Trouet A., and Crichton R.R. Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization. Biochem. Pharmacol. 34 8 (1985) 1175-1183
    • (1985) Biochem. Pharmacol. , vol.34 , Issue.8 , pp. 1175-1183
    • Laub, R.1    Schneider, Y.J.2    Octave, J.N.3    Trouet, A.4    Crichton, R.R.5
  • 23
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidative stress is mediated through lysosomal damage
    • Ollinger K., and Brunk U.T. Cellular injury induced by oxidative stress is mediated through lysosomal damage. Free Radic. Biol. Med. 19 5 (1995) 565-574
    • (1995) Free Radic. Biol. Med. , vol.19 , Issue.5 , pp. 565-574
    • Ollinger, K.1    Brunk, U.T.2
  • 24
    • 0033066791 scopus 로고    scopus 로고
    • Cellular uptake and release of two contrasting iron chelators
    • Cable H., and Lioyd J.B. Cellular uptake and release of two contrasting iron chelators. J. Pharm. Pharmacol. 51 (1999) 131-134
    • (1999) J. Pharm. Pharmacol. , vol.51 , pp. 131-134
    • Cable, H.1    Lioyd, J.B.2
  • 25
    • 0037448064 scopus 로고    scopus 로고
    • Prevention of oxidant-induced cell death by lysosomotropic iron chelators
    • Persson H.L., Yu Z., Tirosh O., Eaton J.M., and Brunk U.T. Prevention of oxidant-induced cell death by lysosomotropic iron chelators. Free Radic. Biol. Med. 34 (2003) 1295-1305
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1295-1305
    • Persson, H.L.1    Yu, Z.2    Tirosh, O.3    Eaton, J.M.4    Brunk, U.T.5
  • 26
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 2 (2004) 205-219
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 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 H.K., Carmona S., Laforge M., Harper F., Dumont C., and Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278 (2003) 31401-31411
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 30
    • 0031022255 scopus 로고    scopus 로고
    • Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein
    • Nakanishi H., Amano T., Sastradipura D.F., Yoshimine Y., Tsukuba T., Tanabe K., Hirotsu I., Ohono T., and Yamamoto K. Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein. J. Neurochem. 68 2 (1997) 739-749
    • (1997) J. Neurochem. , vol.68 , Issue.2 , pp. 739-749
    • Nakanishi, H.1    Amano, T.2    Sastradipura, D.F.3    Yoshimine, Y.4    Tsukuba, T.5    Tanabe, K.6    Hirotsu, I.7    Ohono, T.8    Yamamoto, K.9
  • 32
    • 0030865646 scopus 로고    scopus 로고
    • Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis
    • Hampton M.B., and Orrenius S. Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis. FEBS Lett. 414 3 (1997) 552-556
    • (1997) FEBS Lett. , vol.414 , Issue.3 , pp. 552-556
    • Hampton, M.B.1    Orrenius, S.2
  • 33
    • 0027180710 scopus 로고
    • Visualization of iron in cultured macrophages: a cytochemical light and electron microscopic study using autometallography
    • Zdolsek J.M., Roberg K., and Brunk U.T. Visualization of iron in cultured macrophages: a cytochemical light and electron microscopic study using autometallography. Free Radic. Biol. Med. 15 1 (1993) 1-11
    • (1993) Free Radic. Biol. Med. , vol.15 , Issue.1 , pp. 1-11
    • Zdolsek, J.M.1    Roberg, K.2    Brunk, U.T.3
  • 34
    • 0001313069 scopus 로고
    • Lethal hydrogen peroxide toxicity involves lysosomal membranes iron-catalyzed reactions with membrane damage
    • Brunk U.T., Zhang H., Roberg K., and Ollinger K. Lethal hydrogen peroxide toxicity involves lysosomal membranes iron-catalyzed reactions with membrane damage. Redox. Rep. 1 (1995) 267-277
    • (1995) Redox. Rep. , vol.1 , pp. 267-277
    • Brunk, U.T.1    Zhang, H.2    Roberg, K.3    Ollinger, K.4
  • 35
    • 0028032254 scopus 로고
    • Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines
    • Dypbukt J.M., Ankarcrona M., Burkitt M., Sjoholm A., Strom K., Orrenius S., and Nicotera P. Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines. J. Biol. Chem. 269 48 (1994) 30553-30560
    • (1994) J. Biol. Chem. , vol.269 , Issue.48 , pp. 30553-30560
    • Dypbukt, J.M.1    Ankarcrona, M.2    Burkitt, M.3    Sjoholm, A.4    Strom, K.5    Orrenius, S.6    Nicotera, P.7
  • 36
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss L.P., Galinka H., Berissi H., Cohen O., and Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 15 (1996) 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
  • 38
    • 0036660887 scopus 로고    scopus 로고
    • Endosomal-lysosomal proteolysis mediates death signalling by TNFalpha, not by etoposide, in L929 fibrosarcoma cells: evidence for an active role of cathepsin D
    • Demòz M., Castino R., Cesaro P., Baccino F.M., Bonelli G., and Isidoro C. Endosomal-lysosomal proteolysis mediates death signalling by TNFalpha, not by etoposide, in L929 fibrosarcoma cells: evidence for an active role of cathepsin D. Biol. Chem. 383 (2002) 1237-1248
    • (2002) Biol. Chem. , vol.383 , pp. 1237-1248
    • Demòz, M.1    Castino, R.2    Cesaro, P.3    Baccino, F.M.4    Bonelli, G.5    Isidoro, C.6
  • 40
    • 0033436344 scopus 로고    scopus 로고
    • Lysosomal release of cathepsin D precedes relocation of cytocrome c and loss of mitochondrial transmembrane potential during apoptosis by oxdative stress
    • Roberg K., Johansson U., and Ollinger K. Lysosomal release of cathepsin D precedes relocation of cytocrome c and loss of mitochondrial transmembrane potential during apoptosis by oxdative stress. Free Radic. Biol. Med. 27 (1999) 1228-1237
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1228-1237
    • Roberg, K.1    Johansson, U.2    Ollinger, K.3
  • 41
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomiocytes
    • Roberg K., and Ollinger K. Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomiocytes. Am. J. Pathol. 152 (1998) 1151-1156
    • (1998) Am. J. Pathol. , vol.152 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 42
    • 0024286676 scopus 로고
    • Specificity of oxygen radical scavengers and assessment of free radical scavenger efficiency using luminol enhanced chemiluminescence
    • Rao P.S., Luber J.M., Milinowicz J., Lalezari P., and Mueller H.S. Specificity of oxygen radical scavengers and assessment of free radical scavenger efficiency using luminol enhanced chemiluminescence. Biochem. Biophys. Res. Commun. 150 1 (1988) 39-44
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , Issue.1 , pp. 39-44
    • Rao, P.S.1    Luber, J.M.2    Milinowicz, J.3    Lalezari, P.4    Mueller, H.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.