메뉴 건너뛰기




Volumn 29, Issue 5, 2004, Pages 871-880

Lysosomal storage diseases: Is impaired apoptosis a pathogenic mechanism?

Author keywords

Apoptosis; Cathepsin; Ceramide; Lysosome; Protease; Sphingosine

Indexed keywords

ANTIINFECTIVE AGENT; CATHEPSIN; CERAMIDE; HYDROLASE; PROTEINASE; SPHINGOLIPID;

EID: 3142734904     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000021232.05175.38     Document Type: Short Survey
Times cited : (19)

References (106)
  • 1
    • 0033982248 scopus 로고    scopus 로고
    • The molecular basis of lysosomal storage diseases and their treatment
    • Winchester, B., Vellodi, A., and Young, E. 2000. The molecular basis of lysosomal storage diseases and their treatment. Biochem. Soc. Trans. 28:150-154.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 150-154
    • Winchester, B.1    Vellodi, A.2    Young, E.3
  • 2
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders
    • Desnick, R. J. and Schuchman, E. H. 2002. Enzyme replacement and enhancement therapies: lessons from lysosomal disorders. Nat. Rev. Genet. 3:954-966.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 4
    • 0036303882 scopus 로고    scopus 로고
    • Lysosomal disorders
    • Wraith, J. E. 2002. Lysosomal disorders. Semin. Neonatol. 7:75-83.
    • (2002) Semin. Neonatol. , vol.7 , pp. 75-83
    • Wraith, J.E.1
  • 6
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb, B. D., Shi, G. P., Chapman, H. A., and Desnick, R. J. 1996. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273:1236-1238.
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 7
    • 0026410287 scopus 로고
    • Biochemical basis of late-onset neurolipidoses
    • Conzelmann, E. and Sandhoff, K. 1991. Biochemical basis of late-onset neurolipidoses. Dev. Neurosci. 13:197-204.
    • (1991) Dev. Neurosci. , vol.13 , pp. 197-204
    • Conzelmann, E.1    Sandhoff, K.2
  • 8
    • 0027932927 scopus 로고
    • Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells
    • Graber, D., Salvayre, R., and Levade, T. 1994. Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells. J. Neurochem. 63:1060-1068.
    • (1994) J. Neurochem. , vol.63 , pp. 1060-1068
    • Graber, D.1    Salvayre, R.2    Levade, T.3
  • 9
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. 2000. The biochemistry of apoptosis. Nature 407:770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 10
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie, A. H. 1980. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284:555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 11
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao, L., Perez, D., and White, E. 1996. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135:1441-1455.
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 12
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch, W. 2001. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ. 8:569-581.
    • (2001) Cell Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 13
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K. F. and Kroemer, G. 2001. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3:E255-263.
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 14
    • 0021040946 scopus 로고
    • Lysosomes revisited
    • de Duve, C. 1983. Lysosomes revisited. Eur. J. Biochem. 137:391-397.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 391-397
    • De Duve, C.1
  • 15
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson, D. E. 2000. Noncaspase proteases in apoptosis. Leukemia 14:1695-1703.
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 16
    • 0034813577 scopus 로고    scopus 로고
    • TNF toxicity - Death from caspase or cathepsin, that is the question
    • Czaja, M. J. 2001. TNF toxicity - death from caspase or cathepsin, that is the question. Hepatology 34:844-846.
    • (2001) Hepatology , vol.34 , pp. 844-846
    • Czaja, M.J.1
  • 17
    • 0035038613 scopus 로고    scopus 로고
    • Triggering of apoptosis by cathepsins
    • Leist, M. and Jaattela, M. 2001. Triggering of apoptosis by cathepsins. Cell Death Differ. 8:324-326.
    • (2001) Cell Death Differ. , vol.8 , pp. 324-326
    • Leist, M.1    Jaattela, M.2
  • 18
    • 0035164416 scopus 로고    scopus 로고
    • A lysosomal protease enters the death scene
    • Salvesen, G. S. 2001. A lysosomal protease enters the death scene. J. Clin. Invest. 107:21-22.
    • (2001) J. Clin. Invest. , vol.107 , pp. 21-22
    • Salvesen, G.S.1
  • 19
    • 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. 1996. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 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
  • 20
    • 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., and Ollinger, K. 1999. 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. 27:1228-1237.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1228-1237
    • Roberg, K.1    Johansson, U.2    Ollinger, K.3
  • 21
    • 0032601582 scopus 로고    scopus 로고
    • Cathepsins as effector proteases in hepatocyte apoptosis
    • Roberts, L. R., Adjei, P. N., and Gores, G. J. 1999. Cathepsins as effector proteases in hepatocyte apoptosis. Cell Biochem. Biophys. 30:71-88.
    • (1999) Cell Biochem. Biophys. , vol.30 , pp. 71-88
    • Roberts, L.R.1    Adjei, P.N.2    Gores, G.J.3
  • 22
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kagedal, K., Johansson, U., and Ollinger, K. 2001. The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J. 15:1592-1594.
    • (2001) FASEB J. , vol.15 , pp. 1592-1594
    • Kagedal, K.1    Johansson, U.2    Ollinger, K.3
  • 23
    • 0035018235 scopus 로고    scopus 로고
    • Evidence of a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukemia HL-60 cells
    • Zang, Y., Beard, R. E., Chandraratna, R. A., and Kang, J. X. 2001. Evidence of a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukemia HL-60 cells. Cell Death Differ. 8:477-485.
    • (2001) Cell Death Differ. , vol.8 , pp. 477-485
    • Zang, Y.1    Beard, R.E.2    Chandraratna, R.A.3    Kang, J.X.4
  • 24
    • 0036660887 scopus 로고    scopus 로고
    • Endosomal-lysosomal proteolysis mediates death signaling by TNFalpha, not by etoposide, in L929 fibrosarcoma cells: Evidence for an active role of cathepsin D
    • Demoz, M., Castino, R., Cesaro, P., Baccino, F. M., Bonelli, G., and Isidoro, C. 2002. Endosomal-lysosomal proteolysis mediates death signaling by TNFalpha, not by etoposide, in L929 fibrosarcoma cells: evidence for an active role of cathepsin D. Biol. Chem. 383:1237-1248.
    • (2002) Biol. Chem. , vol.383 , pp. 1237-1248
    • Demoz, M.1    Castino, R.2    Cesaro, P.3    Baccino, F.M.4    Bonelli, G.5    Isidoro, C.6
  • 25
    • 0037209848 scopus 로고    scopus 로고
    • Roles of cathepsins in reperfusion-induced apoptosis in cultured astrocytes
    • Takuma, K., Kiriu, M., Mori, K., Lee, E., Enomoto, R., Baba, A., and Matsuda, T. 2003. Roles of cathepsins in reperfusion-induced apoptosis in cultured astrocytes. Neurochem. Int. 42:153-159.
    • (2003) Neurochem. Int. , vol.42 , pp. 153-159
    • Takuma, K.1    Kiriu, M.2    Mori, K.3    Lee, E.4    Enomoto, R.5    Baba, A.6    Matsuda, T.7
  • 27
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts
    • Roberg, K., Kagedal, K., and Ollinger, K. 2002. Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161:89-96.
    • (2002) Am. J. Pathol. , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Ollinger, K.3
  • 28
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu, G. S., Saftig, P., Peters, C., and El-Deiry, W. S. 1998. Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity. Oncogene 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
  • 29
    • 0037086662 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate, an agent with in vivo anti-tumor activity, induces apoptosis by causing lysosomal instability
    • Neuzil, J., Zhao, M., Ostermann, G., Sticha, M., Gellert, N., Weber, C., Eaton, J. W., and Brunk, U. T. 2002. Alpha-tocopheryl succinate, an agent with in vivo anti-tumor activity, induces apoptosis by causing lysosomal instability. Biochem. J. 362:709-715.
    • (2002) Biochem. J. , vol.362 , pp. 709-715
    • Neuzil, J.1    Zhao, M.2    Ostermann, G.3    Sticha, M.4    Gellert, N.5    Weber, C.6    Eaton, J.W.7    Brunk, U.T.8
  • 30
    • 0036732169 scopus 로고    scopus 로고
    • Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage
    • Reiners, J. J., Jr., Caruso, J. A., Mathieu, P., Chelladurai, B., Yin, X. M., and Kessel, D. 2002. Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage. Cell Death Differ. 9:934-944.
    • (2002) Cell Death Differ. , vol.9 , pp. 934-944
    • Reiners Jr., J.J.1    Caruso, J.A.2    Mathieu, P.3    Chelladurai, B.4    Yin, X.M.5    Kessel, D.6
  • 32
    • 0037138438 scopus 로고    scopus 로고
    • Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas
    • Castino, R., Pace, D., Demoz, M., Gargiulo, M., Ariatta, C., Raiteri, E., and Isidoro, C. 2002. Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas. Int. J. Cancer 97:775-779.
    • (2002) Int. J. Cancer , vol.97 , pp. 775-779
    • Castino, R.1    Pace, D.2    Demoz, M.3    Gargiulo, M.4    Ariatta, C.5    Raiteri, E.6    Isidoro, C.7
  • 33
    • 0041912315 scopus 로고    scopus 로고
    • Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D
    • in press
    • Tardy, C., Tyynela, J., Hasilik, A., Levade, T., and Andrieu-Abadie, N. 2003. Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D. Cell Death Differ. (in press).
    • (2003) Cell Death Differ.
    • Tardy, C.1    Tyynela, J.2    Hasilik, A.3    Levade, T.4    Andrieu-Abadie, N.5
  • 35
    • 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, M. E., Miyoshi, H., Bronk, S. F., and Gores, G. J. 2001. Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: implications for therapeutic applications. Am. J. Pathol. 159:2045-2054.
    • (2001) Am. J. Pathol. , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 38
    • 0037328905 scopus 로고    scopus 로고
    • Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis
    • Levicar, N., Dewey, R. A., Daley, E., Bates, T. E., Davies, D., Kos, J., Pilkington, G. J., and Lah, T. T. 2003. Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis. Cancer Gene Ther. 10:141-151.
    • (2003) Cancer Gene Ther. , vol.10 , pp. 141-151
    • Levicar, N.1    Dewey, R.A.2    Daley, E.3    Bates, T.E.4    Davies, D.5    Kos, J.6    Pilkington, G.J.7    Lah, T.T.8
  • 40
    • 0034071270 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells
    • Cho, S. and Dawson, G. 2000. Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells. J. Neurochem. 74:1478-1488.
    • (2000) J. Neurochem. , vol.74 , pp. 1478-1488
    • Cho, S.1    Dawson, G.2
  • 41
    • 0034667696 scopus 로고    scopus 로고
    • Antisense palmitoyl protein thioesterase 1 (PPT1) treatment inhibits PPT1 activity and increases cell death in LA-N-5 neuroblastoma cells
    • Cho, S., Dawson, P. E., and Dawson, G. 2000. Antisense palmitoyl protein thioesterase 1 (PPT1) treatment inhibits PPT1 activity and increases cell death in LA-N-5 neuroblastoma cells. J. Neurosci. Res. 62:234-240.
    • (2000) J. Neurosci. Res. , vol.62 , pp. 234-240
    • Cho, S.1    Dawson, P.E.2    Dawson, G.3
  • 43
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • Kolesnick, R. N. and Krönke, M. 1998. Regulation of ceramide production and apoptosis. Annu. Rev. Physiol. 60:643-665.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 643-665
    • Kolesnick, R.N.1    Krönke, M.2
  • 44
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun, Y. A. and Luberto, C. 2000. Ceramide in the eukaryotic stress response. Trends Cell Biol. 10:73-80.
    • (2000) Trends Cell Biol. , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 46
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun, Y. 1996. Functions of ceramide in coordinating cellular responses to stress. Science 274:1855-1859.
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.1
  • 49
    • 0031041448 scopus 로고    scopus 로고
    • Cytokine response modifier a (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-a: CrmA and Bcl-2 target distinct components in the apoptotic pathway
    • Dbaibo, G. S., Perry, D. K., Gamard, C. J., Platt, R., Poirier, G. G., Obeid, L. M., and Hannun, Y. A. 1997. Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-a: CrmA and Bcl-2 target distinct components in the apoptotic pathway. J. Exp. Med. 185:481-490.
    • (1997) J. Exp. Med. , vol.185 , pp. 481-490
    • Dbaibo, G.S.1    Perry, D.K.2    Gamard, C.J.3    Platt, R.4    Poirier, G.G.5    Obeid, L.M.6    Hannun, Y.A.7
  • 50
    • 0344349001 scopus 로고    scopus 로고
    • Signaling sphingomyelinases: Which, where, how and why?
    • Levade, T. and Jaffrézou, J. P. 1999. Signaling sphingomyelinases: which, where, how and why? Biochim. Biophys. Acta 1438:1-17.
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 1-17
    • Levade, T.1    Jaffrézou, J.P.2
  • 51
    • 0021339782 scopus 로고
    • Progressive accumulation of toxic metabolite in a genetic leukodystrophy
    • Igisu, H. and Suzuki, K. 1984. Progressive accumulation of toxic metabolite in a genetic leukodystrophy. Science 224:753-755.
    • (1984) Science , vol.224 , pp. 753-755
    • Igisu, H.1    Suzuki, K.2
  • 52
    • 0022656315 scopus 로고
    • Occurrence of lysoganglioside lyso-GM2 (ll3-Neu5Ac- gangliotriaosylsphingosine) in GM2 gangliosidosis brain
    • Neuenhofer, S., Conzelmann, E., Schwarzmann, G., Egge, H., and Sandhoff, K. 1986. Occurrence of lysoganglioside lyso-GM2 (ll3-Neu5Ac- gangliotriaosylsphingosine) in GM2 gangliosidosis brain. Biol. Chem. Hoppe Seyler 367:241-244.
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 241-244
    • Neuenhofer, S.1    Conzelmann, E.2    Schwarzmann, G.3    Egge, H.4    Sandhoff, K.5
  • 53
    • 0024589780 scopus 로고
    • Lysosulfatide (galactosylsphingosine-3-O-sulfate) from meta-chromatic leukodystrophy and normal human brain
    • Rosengren, B., Fredman, P., Mansson, J. E., and Svennerholm, L. 1989. Lysosulfatide (galactosylsphingosine-3-O-sulfate) from meta-chromatic leukodystrophy and normal human brain. J. Neurochem. 52:1035-1041.
    • (1989) J. Neurochem. , vol.52 , pp. 1035-1041
    • Rosengren, B.1    Fredman, P.2    Mansson, J.E.3    Svennerholm, L.4
  • 54
    • 0025186238 scopus 로고
    • Lysosulfatide (sulfogalactosylsphingosine) accumulation in tissues from patients with metachromatic leukodystrophy
    • Toda, K., Kobayashi, T., Goto, I., Ohno, K., Eto, Y., Inui, K., and Okada, S. 1990. Lysosulfatide (sulfogalactosylsphingosine) accumulation in tissues from patients with metachromatic leukodystrophy. J. Neurochem. 55:1585-1591.
    • (1990) J. Neurochem. , vol.55 , pp. 1585-1591
    • Toda, K.1    Kobayashi, T.2    Goto, I.3    Ohno, K.4    Eto, Y.5    Inui, K.6    Okada, S.7
  • 55
    • 0032934036 scopus 로고    scopus 로고
    • Sphingosylphosphorylcholine in Niemann-Pick disease brain: Accumulation in type A but not in type B
    • Rodriguez-Lafrasse, C. and Valuer, M. T. 1999. Sphingosylphosphorylcholine in Niemann-Pick disease brain: accumulation in type A but not in type B. Neurochem. Res. 24:199-205.
    • (1999) Neurochem. Res. , vol.24 , pp. 199-205
    • Rodriguez-Lafrasse, C.1    Valuer, M.T.2
  • 56
    • 0023138332 scopus 로고
    • Lysosphingolipids inhibit protein kinase C: Implications fot the sphingolipidoses
    • Hannun, Y. A. and Bell, R. M. 1987. Lysosphingolipids inhibit protein kinase C: implications fot the sphingolipidoses. Science 235:670-674.
    • (1987) Science , vol.235 , pp. 670-674
    • Hannun, Y.A.1    Bell, R.M.2
  • 57
    • 0029666484 scopus 로고    scopus 로고
    • Zn2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene
    • Schissel, S. L., Schuchman, E. H., Williams, K. J., and Tabas, I. 1996. Zn2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene. J. Biol. Chem. 271:18431-18436.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18431-18436
    • Schissel, S.L.1    Schuchman, E.H.2    Williams, K.J.3    Tabas, I.4
  • 58
    • 0030971534 scopus 로고    scopus 로고
    • Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides
    • Hiraiwa, M., Taylor, E. M., Campana, W. M., Darin, S. J., and O'Brien, J. S. 1997. Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides. Proc. Natl. Acad. Sci. USA 94:4778-4781.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4778-4781
    • Hiraiwa, M.1    Taylor, E.M.2    Campana, W.M.3    Darin, S.J.4    O'Brien, J.S.5
  • 60
    • 0032190625 scopus 로고    scopus 로고
    • Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture
    • Tsuboi, K., Hiraiwa, M., and O'Brien, J. S. 1998. Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture. Brain Res. Dev. Brain. Res. 110:249-255.
    • (1998) Brain Res. Dev. Brain. Res. , vol.110 , pp. 249-255
    • Tsuboi, K.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 61
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham, C. T. and Ley, T. J. 1999. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. USA 96:8627-8632.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 62
    • 0036899408 scopus 로고    scopus 로고
    • Neuropathological changes in a mouse model of progressive myoclonus epilepsy: Cystatin B deficiency and Unverricht-Lundborg disease
    • Shannon, P., Pennacchio, L. A., Houseweart, M. K., Minassian, B. A., and Myers, R. M. 2002. Neuropathological changes in a mouse model of progressive myoclonus epilepsy: cystatin B deficiency and Unverricht-Lundborg disease. J. Neuropathol. Exp. Neurol. 61:1085-1091.
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 1085-1091
    • Shannon, P.1    Pennacchio, L.A.2    Houseweart, M.K.3    Minassian, B.A.4    Myers, R.M.5
  • 63
    • 0030782030 scopus 로고    scopus 로고
    • Apoptotic cell death in mouse models of GM2 gangliosidosis and observations on human Tay-Sachs and Sandhoff diseases
    • Huang, J. Q., Trasler, J. M., Igdoura, S., Michaud, J., Hanal, N., and Gravel, R. A. 1997. Apoptotic cell death in mouse models of GM2 gangliosidosis and observations on human Tay-Sachs and Sandhoff diseases. Hum. Mol. Genet. 6:1879-1885.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1879-1885
    • Huang, J.Q.1    Trasler, J.M.2    Igdoura, S.3    Michaud, J.4    Hanal, N.5    Gravel, R.A.6
  • 64
    • 0034718598 scopus 로고    scopus 로고
    • Microglial activation precedes acute neurodegeneration in Sandhoff disease and is suppressed by bone marrow transplantation
    • Wada, R., Tifft, C. J., and Proia, R. L. 2000. Microglial activation precedes acute neurodegeneration in Sandhoff disease and is suppressed by bone marrow transplantation. Proc. Natl. Acad. Sci. USA 97:10954-10959.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10954-10959
    • Wada, R.1    Tifft, C.J.2    Proia, R.L.3
  • 65
    • 0033065014 scopus 로고    scopus 로고
    • An apoptotic depletion of oligodendrocytes in the twitcher, a murine model of globoid cell leukodystrophy
    • Taniike, M., Mohri, I., Eguchi, N., Irikura, D., Urade, Y., Okada, S., and Suzuki, K. 1999. An apoptotic depletion of oligodendrocytes in the twitcher, a murine model of globoid cell leukodystrophy. J. Neuropathol. Exp. Neurol. 58:644-653.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 644-653
    • Taniike, M.1    Mohri, I.2    Eguchi, N.3    Irikura, D.4    Urade, Y.5    Okada, S.6    Suzuki, K.7
  • 66
    • 0037144211 scopus 로고    scopus 로고
    • Apoptotic positive cells in Krabbe brain and induction of apoptosis in rat C6 glial cells by psychosine
    • Jatana, M., Giri, S., and Singh, A. K. 2002. Apoptotic positive cells in Krabbe brain and induction of apoptosis in rat C6 glial cells by psychosine. Neurosci. Lett. 330:183-187.
    • (2002) Neurosci. Lett. , vol.330 , pp. 183-187
    • Jatana, M.1    Giri, S.2    Singh, A.K.3
  • 67
    • 0033001660 scopus 로고    scopus 로고
    • Ceramide accumulation is associated with increased apoptotic cell death in cultured fibroblasts of sphingolipid activator protein-deficient mouse but not in fibroblasts of patients with Farber disease
    • Tohyama, J., Oya, Y., Ezoe, T., Vanier, M. T., Nakayasu, H., Fujita, N., and Suzuki, K. 1999. Ceramide accumulation is associated with increased apoptotic cell death in cultured fibroblasts of sphingolipid activator protein-deficient mouse but not in fibroblasts of patients with Farber disease. J. Inherit. Metab. Dis. 22:649-662.
    • (1999) J. Inherit. Metab. Dis. , vol.22 , pp. 649-662
    • Tohyama, J.1    Oya, Y.2    Ezoe, T.3    Vanier, M.T.4    Nakayasu, H.5    Fujita, N.6    Suzuki, K.7
  • 68
    • 0034957276 scopus 로고    scopus 로고
    • Morphological alterations in the inner ear of the arylsulfatase A-deficient mouse
    • Berlin
    • Coenen, R., Gieselmann, V., and Lullmann-Rauch, R. 2001. Morphological alterations in the inner ear of the arylsulfatase A-deficient mouse. Acta Neuropathol. (Berlin) 101:491-498.
    • (2001) Acta Neuropathol. , vol.101 , pp. 491-498
    • Coenen, R.1    Gieselmann, V.2    Lullmann-Rauch, R.3
  • 69
    • 0034891273 scopus 로고    scopus 로고
    • Apoptosis of Neuro2a cells induced by lysosphingolipids with naturally occurring stereochemical configurations
    • Sueyoshi, N., Maehara, T., and Ito, M. 2001. Apoptosis of Neuro2a cells induced by lysosphingolipids with naturally occurring stereochemical configurations. J. Lipid Res. 42:1197-1202.
    • (2001) J. Lipid Res. , vol.42 , pp. 1197-1202
    • Sueyoshi, N.1    Maehara, T.2    Ito, M.3
  • 70
    • 0034886801 scopus 로고    scopus 로고
    • Psychosine is as potent an inducer of cell death as C6-ceramide in cultured fibroblasts and in MOCH-1 cells
    • Tohyama, J., Matsuda, J., and Suzuki, K. 2001. Psychosine is as potent an inducer of cell death as C6-ceramide in cultured fibroblasts and in MOCH-1 cells. Neurochem. Res. 26:667-671.
    • (2001) Neurochem. Res. , vol.26 , pp. 667-671
    • Tohyama, J.1    Matsuda, J.2    Suzuki, K.3
  • 71
    • 0026648695 scopus 로고
    • Type C Niemann-Pick disease: A murine model of the lysosomal cholesterol lipidosis accumulates sphingosine and sphinganine in liver
    • Goldin, E., Roff, C. F., Miller, S. P., Rodriguez-Lafrasse, C., Vanier, M. T., Brady, R. O., and Pentchev, P. G. 1992. Type C Niemann-Pick disease: a murine model of the lysosomal cholesterol lipidosis accumulates sphingosine and sphinganine in liver. Biochim. Biophys. Acta 1127:303-311.
    • (1992) Biochim. Biophys. Acta , vol.1127 , pp. 303-311
    • Goldin, E.1    Roff, C.F.2    Miller, S.P.3    Rodriguez-Lafrasse, C.4    Vanier, M.T.5    Brady, R.O.6    Pentchev, P.G.7
  • 72
    • 0000411490 scopus 로고    scopus 로고
    • Neuronal death and reactive glial changes in the brain of Niemann-Pick disease type C mouse
    • Wu, Y. P., Kubota, A., and Suzuki, K. 1999. Neuronal death and reactive glial changes in the brain of Niemann-Pick disease type C mouse. Soc. Neurosci. Abstr. 25:1118.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 1118
    • Wu, Y.P.1    Kubota, A.2    Suzuki, K.3
  • 74
    • 0032536876 scopus 로고    scopus 로고
    • Acidic sphingomyelinase (ASM) is necessary for Fas-induced GD3 ganglioside accumulation and efficient apoptosis of lymphoid cells
    • de Maria, R., Rippo, M. R., Schuchman, E. H., and Testi, R. 1998. Acidic sphingomyelinase (ASM) is necessary for Fas-induced GD3 ganglioside accumulation and efficient apoptosis of lymphoid cells. J. Exp. Med. 187:897-902.
    • (1998) J. Exp. Med. , vol.187 , pp. 897-902
    • De Maria, R.1    Rippo, M.R.2    Schuchman, E.H.3    Testi, R.4
  • 76
    • 0035968448 scopus 로고    scopus 로고
    • Evidence for the association of ultraviolet-C and H(2)O(2)-induced apoptosis with acid sphingomyelinase activation
    • Komatsu, M., Takahashi, T., Abe, T., Takahashi, I., Ida, H., and Takada, G. 2001. Evidence for the association of ultraviolet-C and H(2)O(2)-induced apoptosis with acid sphingomyelinase activation. Biochim. Biophys. Acta 1533:47-54.
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 47-54
    • Komatsu, M.1    Takahashi, T.2    Abe, T.3    Takahashi, I.4    Ida, H.5    Takada, G.6
  • 79
    • 0037237733 scopus 로고    scopus 로고
    • Defective TNF-alpha-mediated hepatocellular apoptosis and liver damage in acidic sphingomyelinase knockout mice
    • Garcia-Ruiz, C., Colell, A., Mari, M., Morales, A., Calvo, M., Enrich, C., and Fernandez-Checa, J. C. 2003. Defective TNF-alpha-mediated hepatocellular apoptosis and liver damage in acidic sphingomyelinase knockout mice. J. Clin. Invest. 111: 197-208.
    • (2003) J. Clin. Invest. , vol.111 , pp. 197-208
    • Garcia-Ruiz, C.1    Colell, A.2    Mari, M.3    Morales, A.4    Calvo, M.5    Enrich, C.6    Fernandez-Checa, J.C.7
  • 81
    • 0032571251 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase
    • Cock, J. G., Tepper, A. D., de Vries, E., van Blitterswijk, W. J., and Borst, J. 1998. CD95 (Fas/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase. J. Biol. Chem. 273:7560-7565.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7560-7565
    • Cock, J.G.1    Tepper, A.D.2    De Vries, E.3    Van Blitterswijk, W.J.4    Borst, J.5
  • 84
    • 0035807229 scopus 로고    scopus 로고
    • The role of ceramide in receptor- and stress-induced apoptosis studied in acidic ceramidase-deficient Farber disease cells
    • Burek, C., Roth, J., Koch, H. G., Harzer, K., Los, M., and Schulze-Osthoff, K. 2001. The role of ceramide in receptor- and stress-induced apoptosis studied in acidic ceramidase-deficient Farber disease cells. Oncogene 20:6493-6502.
    • (2001) Oncogene , vol.20 , pp. 6493-6502
    • Burek, C.1    Roth, J.2    Koch, H.G.3    Harzer, K.4    Los, M.5    Schulze-Osthoff, K.6
  • 85
    • 0037226939 scopus 로고    scopus 로고
    • The neuronal ceroid-lipofuscinoses
    • Haltia, M. 2003. The neuronal ceroid-lipofuscinoses. J. Neuropathol. Exp. Neurol. 62:1-13.
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 1-13
    • Haltia, M.1
  • 86
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynela, J., Sohar, I., Sleat, D. E., Gin, R. M., Donnelly, R. J., Baumann, M., Haltia, M., and Lobel, P. 2000. A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J. 19:2786-2792.
    • (2000) EMBO J. , vol.19 , pp. 2786-2792
    • Tyynela, J.1    Sohar, I.2    Sleat, D.E.3    Gin, R.M.4    Donnelly, R.J.5    Baumann, M.6    Haltia, M.7    Lobel, P.8
  • 87
    • 0035990974 scopus 로고    scopus 로고
    • Mutated genes in juvenile and valiant late infantile neuronal ceroid lipofuscinoses encode lysosomal proteins
    • Vesa, J. and Peltonen, L. 2002. Mutated genes in juvenile and valiant late infantile neuronal ceroid lipofuscinoses encode lysosomal proteins. Curr. Mol. Med. 2:439-444.
    • (2002) Curr. Mol. Med. , vol.2 , pp. 439-444
    • Vesa, J.1    Peltonen, L.2
  • 88
    • 0030038060 scopus 로고    scopus 로고
    • Apoptosis as the mechanism of neurodegeneration in Batten's disease
    • Lane, S. C., Jolly, R. D., Schmechel, D. E., Alroy, J., and Boustany, R. M. 1996. Apoptosis as the mechanism of neurodegeneration in Batten's disease. J. Neurochem. 67:677-683.
    • (1996) J. Neurochem. , vol.67 , pp. 677-683
    • Lane, S.C.1    Jolly, R.D.2    Schmechel, D.E.3    Alroy, J.4    Boustany, R.M.5
  • 92
    • 0032799217 scopus 로고    scopus 로고
    • CLN3 defines a novel antiapoptotic pathway operative in neurodegeneration and mediated by ceramide
    • Puranam, K. L., Guo, W. X., Qian, W. H., Nikbakht, K., and Boustany, R. M. 1999. CLN3 defines a novel antiapoptotic pathway operative in neurodegeneration and mediated by ceramide. Mol. Genet. Metab. 66:294-308.
    • (1999) Mol. Genet. Metab. , vol.66 , pp. 294-308
    • Puranam, K.L.1    Guo, W.X.2    Qian, W.H.3    Nikbakht, K.4    Boustany, R.M.5
  • 93
    • 0036682881 scopus 로고    scopus 로고
    • TRAM, LAG2 and CLN8: Members of a novel family of lipid-sensing domains?
    • Winter, E. and Ponting, C. P. 2002. TRAM, LAG2 and CLN8: members of a novel family of lipid-sensing domains? Trends Biochem. Sci. 27:381-383.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 381-383
    • Winter, E.1    Ponting, C.P.2
  • 94
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig, P., Hetman, M., Schmahl, W., Weber, K., Heine, L., Mossmann, H., Koster, A., Hess, B., Evers, M., von Figura, K., Peters, C. 1995. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14:3599-3608.
    • (1995) EMBO J. , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6    Koster, A.7    Hess, B.8    Evers, M.9    Von Figura, K.10    Peters, C.11
  • 97
    • 0036349181 scopus 로고    scopus 로고
    • Decreased apoptotic response of inclusion-cell disease fibroblasts: A consequence of lysosomal enzyme missorting?
    • Terman, A., Neuzil, J., Kagedal, K., Ollinger, K., and Brunk, U. T. 2002. Decreased apoptotic response of inclusion-cell disease fibroblasts: a consequence of lysosomal enzyme missorting? Exp. Cell Res. 274:9-15.
    • (2002) Exp. Cell Res. , vol.274 , pp. 9-15
    • Terman, A.1    Neuzil, J.2    Kagedal, K.3    Ollinger, K.4    Brunk, U.T.5
  • 98
    • 0034814719 scopus 로고    scopus 로고
    • Articular chondrocytes from animals with a dermatan sulfate storage disease undergo a high rate of apoptosis and release nitric oxide and inflammatory cytokines: A possible mechanism underlying degenerative joint disease in the mucopolysaccharidoses
    • Simonaro, C. M., Haskins, M. E., and Schuchman, E. H. 2001. Articular chondrocytes from animals with a dermatan sulfate storage disease undergo a high rate of apoptosis and release nitric oxide and inflammatory cytokines: a possible mechanism underlying degenerative joint disease in the mucopolysaccharidoses. Lab. Invest. 81:1319-1328.
    • (2001) Lab. Invest. , vol.81 , pp. 1319-1328
    • Simonaro, C.M.1    Haskins, M.E.2    Schuchman, E.H.3
  • 99
    • 0036891796 scopus 로고    scopus 로고
    • Lysosomal cystine storage augments apoptosis in cultured human fibroblasts and renal tubular epithelial cells
    • Park, M., Helip-Wooley, A., and Thoene, J. 2002. Lysosomal cystine storage augments apoptosis in cultured human fibroblasts and renal tubular epithelial cells. J. Am. Soc. Nephrol. 13:2878-2887.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2878-2887
    • Park, M.1    Helip-Wooley, A.2    Thoene, J.3
  • 101
    • 0037007142 scopus 로고    scopus 로고
    • The Caenorhabditis elegans mucolipin-like gene cup-5 is essential for viability and regulates lysosomes in multiple cell types
    • Hersh, B. M., Hartwieg, E., and Horvitz, H. R. 2002. The Caenorhabditis elegans mucolipin-like gene cup-5 is essential for viability and regulates lysosomes in multiple cell types. Proc. Natl. Acad. Sci. USA 99:4355-4360.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4355-4360
    • Hersh, B.M.1    Hartwieg, E.2    Horvitz, H.R.3
  • 102
    • 0034624913 scopus 로고    scopus 로고
    • CSF insulin-like growth factor-1 in infantile neuronal ceroid lipofuscinosis
    • Riikonen, R., Vanhanen, S. L., Tyynela, J., Santavuori, P., and Tuipeinen, U. 2000. CSF insulin-like growth factor-1 in infantile neuronal ceroid lipofuscinosis. Neurology 54:1828-1832.
    • (2000) Neurology , vol.54 , pp. 1828-1832
    • Riikonen, R.1    Vanhanen, S.L.2    Tyynela, J.3    Santavuori, P.4    Tuipeinen, U.5
  • 103
    • 0035044121 scopus 로고    scopus 로고
    • Lysosomal ceroid depletion by drugs: Therapeutic implications for a hereditary neurodegenerative disease of childhood
    • Zhang, Z., Butler, J. D., Levin, S. W., Wisniewski, K. E., Brooks, S. S., and Mukherjee, A. B. 2001. Lysosomal ceroid depletion by drugs: therapeutic implications for a hereditary neurodegenerative disease of childhood. Nat. Med. 7:478-484.
    • (2001) Nat. Med. , vol.7 , pp. 478-484
    • Zhang, Z.1    Butler, J.D.2    Levin, S.W.3    Wisniewski, K.E.4    Brooks, S.S.5    Mukherjee, A.B.6
  • 104
    • 0036712747 scopus 로고    scopus 로고
    • Motifs within the CLN3 protein: Modulation of cell growth rates and apoptosis
    • Persaud-Sawin, D. A., VanDongen, A., and Boustany, R. M. 2002. Motifs within the CLN3 protein: modulation of cell growth rates and apoptosis. Hum. Mol. Genet. 11:2129-2142.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2129-2142
    • Persaud-Sawin, D.A.1    VanDongen, A.2    Boustany, R.M.3
  • 106
    • 0031764610 scopus 로고    scopus 로고
    • Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice
    • Pennacchio, L. A., Bouley, D. M., Higgins, K. M., Scott, M. P., Noebels, J. L., and Myers, R. M. 1998. Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20:251-258.
    • (1998) Nat. Genet. , vol.20 , pp. 251-258
    • Pennacchio, L.A.1    Bouley, D.M.2    Higgins, K.M.3    Scott, M.P.4    Noebels, J.L.5    Myers, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.