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Volumn 1016, Issue 2, 2004, Pages 163-169

Human neuroblastoma (SH-SY5Y) cells are highly sensitive to the lysosomotropic aldehyde 3-aminopropanal

Author keywords

3 Aminopropanal; Apoptosis; Development and regeneration; Lysosome; Mitochondria; Neuronal death; Oxidative stress; SH SY5Y cell

Indexed keywords

ALDEHYDE DERIVATIVE; ALPHA TOCOPHEROL; AMMONIA; LYSOSOME ENZYME; PROTON PUMP;

EID: 3042777753     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2004.04.075     Document Type: Article
Times cited : (34)

References (39)
  • 2
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • Bonfoco E., Krainc D., Ankarcrona M., Nicotera P., Lipton S.A. Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc. Natl. Acad. Sci. U. S. A. 92:1995;7162-7166
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankarcrona, M.3    Nicotera, P.4    Lipton, S.A.5
  • 3
    • 0023870493 scopus 로고
    • Clastogenic and cytotoxic effects of spermine oxidation products in mouse lymphoma L5178Y cells
    • Bouzyk E., Rosiek O. Clastogenic and cytotoxic effects of spermine oxidation products in mouse lymphoma L5178Y cells. Cancer Lett. 39:1988;93-99
    • (1988) Cancer Lett. , vol.39 , pp. 93-99
    • Bouzyk, E.1    Rosiek, O.2
  • 4
    • 0036728511 scopus 로고    scopus 로고
    • What evidence supports use of erythropoietin as a novel neurotherapeutic?
    • Brines M. What evidence supports use of erythropoietin as a novel neurotherapeutic? Oncology (Huntingt.). 16:2002;79-89
    • (2002) Oncology (Huntingt.) , vol.16 , pp. 79-89
    • Brines, M.1
  • 5
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk U.T., Svensson I. Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep. 4:1999;3-11
    • (1999) Redox Rep. , vol.4 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 6
  • 7
    • 0021164308 scopus 로고
    • Polyamine oxidase-mediated trypanosome killing: The role of hydrogen peroxide and aldehydes
    • Ferrante A., Rzepczyk C.M., Saul A.J. Polyamine oxidase-mediated trypanosome killing: the role of hydrogen peroxide and aldehydes. J. Immunol. 133:1984;2157-2162
    • (1984) J. Immunol. , vol.133 , pp. 2157-2162
    • Ferrante, A.1    Rzepczyk, C.M.2    Saul, A.J.3
  • 8
    • 0033782296 scopus 로고    scopus 로고
    • Mitochondrial participation in ischemic and traumatic neural cell death
    • Fiskum G. Mitochondrial participation in ischemic and traumatic neural cell death. J. Neurotrauma. 17:2000;843-855
    • (2000) J. Neurotrauma , vol.17 , pp. 843-855
    • Fiskum, G.1
  • 9
    • 0036945725 scopus 로고    scopus 로고
    • Pathogenesis of hypoxic-ischemic cerebral injury in the term infant: Current concepts
    • Grow J., Barks J.D. Pathogenesis of hypoxic-ischemic cerebral injury in the term infant: current concepts. Clin. Perinatol. 29:2002;585-602
    • (2002) Clin. Perinatol. , vol.29 , pp. 585-602
    • Grow, J.1    Barks, J.D.2
  • 10
    • 0024352389 scopus 로고
    • Liquid chromatographic determination of common water-soluble antioxidants in biological samples
    • Honegger C.G., Langemann H., Krenger W., Kempf A. Liquid chromatographic determination of common water-soluble antioxidants in biological samples. J. Chromatogr. 487:1989;463-468
    • (1989) J. Chromatogr. , vol.487 , pp. 463-468
    • Honegger, C.G.1    Langemann, H.2    Krenger, W.3    Kempf, A.4
  • 13
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kågedal K., Zhao M., Svensson I., Brunk U.T. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359:2001;335-343
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kågedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 15
    • 0030950904 scopus 로고    scopus 로고
    • Molecular and biochemical events within the brain subjected to cerebral ischemia (targets for therapeutical intervention)
    • Kogure T., Kogure K. Molecular and biochemical events within the brain subjected to cerebral ischemia (targets for therapeutical intervention). Clin. Neurosci. 4:1997;179-183
    • (1997) Clin. Neurosci. , vol.4 , pp. 179-183
    • Kogure, T.1    Kogure, K.2
  • 16
    • 0033789565 scopus 로고    scopus 로고
    • Free radical pathways in CNS injury
    • Lewen A., Matz P., Chan P.H. Free radical pathways in CNS injury. J. Neurotrauma. 17:2000;871-890
    • (2000) J. Neurotrauma , vol.17 , pp. 871-890
    • Lewen, A.1    Matz, P.2    Chan, P.H.3
  • 18
    • 0038641715 scopus 로고    scopus 로고
    • 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin
    • Li W., Yuan X.-M., Ivanova S., Tracey K.J., Eaton J.W., Brunk U.T. 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin. Biochem. J. 371:2003;429-436
    • (2003) Biochem. J. , vol.371 , pp. 429-436
    • Li, W.1    Yuan, X.-M.2    Ivanova, S.3    Tracey, K.J.4    Eaton, J.W.5    Brunk, U.T.6
  • 19
    • 0027501851 scopus 로고
    • Evidence supporting a role for programmed cell death in focal cerebral ischemia in rats
    • Linnik M.D., Zobrist R.H., Hatfield M.D. Evidence supporting a role for programmed cell death in focal cerebral ischemia in rats. Stroke. 24:1993;2002-2008
    • (1993) Stroke , vol.24 , pp. 2002-2008
    • Linnik, M.D.1    Zobrist, R.H.2    Hatfield, M.D.3
  • 21
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S., Poole B. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. U. S. A. 75:1978;3327-3331
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 22
    • 0034650786 scopus 로고    scopus 로고
    • Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes
    • Öllinger K. Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes. Arch. Biochem. Biophys. 373:2000;346-351
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 346-351
    • Öllinger, K.1
  • 23
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidative stress is mediated through lysosomal damage
    • Öllinger K., Brunk U.T. Cellular injury induced by oxidative stress is mediated through lysosomal damage. Free Radic. Biol. Med. 19:1995;565-574
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 565-574
    • Öllinger, K.1    Brunk, U.T.2
  • 25
    • 0034745672 scopus 로고    scopus 로고
    • Relocalization of cathepsin D and cytochrome c early in apoptosis revealed by immunoelectron microscopy
    • Roberg K. Relocalization of cathepsin D and cytochrome c early in apoptosis revealed by immunoelectron microscopy. Lab. Invest. 81:2001;149-158
    • (2001) Lab. Invest. , vol.81 , pp. 149-158
    • Roberg, K.1
  • 26
    • 0033436344 scopus 로고    scopus 로고
    • Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress
    • Roberg K., Johansson U., Öllinger K. Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative 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    Öllinger, K.3
  • 28
    • 0035292649 scopus 로고    scopus 로고
    • 2+ thresholds determine cytochrome c release or permeability transition pore opening in brain mitochondria
    • 2+ thresholds determine cytochrome c release or permeability transition pore opening in brain mitochondria. FASEB J. 15:2001;565-567
    • (2001) FASEB J. , vol.15 , pp. 565-567
    • Schild, L.1    Keilhoff, G.2    Augustin, W.3    Reiser, G.4    Striggow, F.5
  • 29
    • 0034126310 scopus 로고    scopus 로고
    • Oxidation of polyamines and brain injury
    • Seiler N. Oxidation of polyamines and brain injury. Neurochem. Res. 25:2000;471-490
    • (2000) Neurochem. Res. , vol.25 , pp. 471-490
    • Seiler, N.1
  • 33
    • 0029013696 scopus 로고
    • Influence of sample preparation on cellular glutathione recovery from adherent cells in culture
    • Thioudellet C., Oster T., Leroy P., Nicolas A., Wellman M. Influence of sample preparation on cellular glutathione recovery from adherent cells in culture. Cell Biol. Toxicol. 11:1995;103-111
    • (1995) Cell Biol. Toxicol. , vol.11 , pp. 103-111
    • Thioudellet, C.1    Oster, T.2    Leroy, P.3    Nicolas, A.4    Wellman, M.5
  • 34
    • 0141853870 scopus 로고    scopus 로고
    • 3-Aminopropanal is a lysosomotropic aldehyde that causes oxidative stress and apoptosis by rupturing lysosomes
    • Yu Z., Li W., Brunk U.T. 3-Aminopropanal is a lysosomotropic aldehyde that causes oxidative stress and apoptosis by rupturing lysosomes. APMIS. 111:2003;643-652
    • (2003) APMIS , vol.111 , pp. 643-652
    • Yu, Z.1    Li, W.2    Brunk, U.T.3
  • 36
    • 0025070370 scopus 로고
    • Photooxidative damage to lysosomes of cultured macrophages by acridine orange
    • Zdolsek J.M., Olsson G.M., Brunk U.T. Photooxidative damage to lysosomes of cultured macrophages by acridine orange. Photochem. Photobiol. 51:1990;67-76
    • (1990) Photochem. Photobiol. , vol.51 , pp. 67-76
    • Zdolsek, J.M.1    Olsson, G.M.2    Brunk, U.T.3
  • 38
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • Zhao M., Brunk U.T., Eaton J.W. Delayed oxidant-induced cell death involves activation of phospholipase A2. FEBS Lett. 509:2001;399-404
    • (2001) FEBS Lett. , vol.509 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3
  • 39
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M., Antunes F., Eaton J.W., Brunk U.T. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur. J. Biochem. 270:2003;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.