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Volumn 10, Issue 9, 2003, Pages 1090-1100

Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D

Author keywords

Apoptosis; Cathepsin D; Ceramide; I cell disease; Lysosome

Indexed keywords

ACYLSPHINGOSINE DEACYLASE; ASPARTIC PROTEINASE; CASPASE; CATHEPSIN D; CERAMIDE; CYTARABINE; CYTOTOXIC AGENT; DOXORUBICIN; LYSOSOME ENZYME; PEPSTATIN; SPHINGOSINE; STAUROSPORINE; TUMOR NECROSIS FACTOR ALPHA; VINBLASTINE;

EID: 0041912315     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401272     Document Type: Review
Times cited : (30)

References (66)
  • 2
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickson AH (1989) Biosynthesis of lysosomal endopeptidases. J. Cell Biochem. 40: 31-41
    • (1989) J. Cell Biochem. , vol.40 , pp. 31-41
    • Erickson, A.H.1
  • 3
    • 0022927903 scopus 로고
    • Immunolocalization of cathepsin D in normal and neoplastic human tissues
    • Reid WA, Valler MJ and Kay J (1986) Immunolocalization of cathepsin D in normal and neoplastic human tissues. J. Clin. Pathol. 39: 1323-1330
    • (1986) J. Clin. Pathol. , vol.39 , pp. 1323-1330
    • Reid, W.A.1    Valler, M.J.2    Kay, J.3
  • 4
    • 0001310293 scopus 로고
    • Cathepsin D and other carboxyl proteinases
    • Barrett AJ (ad)(Amsterdam: Elsevier/North-Holland Biochemical Press)
    • Barrett AJ (1977) Cathepsin D and other carboxyl proteinases. In Proteinases in Mammalian Cells and Tissues, Barrett AJ (ad)(Amsterdam: Elsevier/North-Holland Biochemical Press), pp. 209-248
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 209-248
    • Barrett, A.J.1
  • 6
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb BD, Shi GP, Chapman HA and Desnick RJ (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
  • 12
    • 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 DE, Gin RM, Donnelly RJ, 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
  • 13
    • 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
  • 14
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson DE (2000) Noncaspase proteases in apoptosis. Leukemia 14: 1695-1703
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 15
    • 0035164416 scopus 로고    scopus 로고
    • A lysosomal protease enters the death scene
    • Salvesen GS (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
  • 16
    • 0034813577 scopus 로고    scopus 로고
    • TNF toxicity-death from caspase or cathepsin, that is the question
    • Czaja MJ (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
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu GS, Saftig P, Peters C and El-Deiry WS (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
  • 18
    • 0037086662 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability
    • Noxal J, Zhao M, Ostermann G, Sticha M, Gellert N, Weber C, Eaton JW and Brunk UT (2002) Alpha-tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability. Biochem. J. 362: 709-715
    • (2002) Biochem. J. , vol.362 , pp. 709-715
    • Noxal, 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
  • 19
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/ APO-1 and TNF-alpha
    • Deiss LP, 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
  • 21
    • 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
  • 22
    • 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
    • Demoz M, Castino R, Cesaro P, Baccino FM, Bonelli G and Isidoro C (2002) 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: 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
  • 23
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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 RL, Chandraratna RA and Kang JX (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.L.2    Chandraratna, R.A.3    Kang, J.X.4
  • 28
    • 0036732169 scopus 로고    scopus 로고
    • Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage
    • Reiners Jr JJ, Caruso JA, Mathieu P, Chelladurai B, Yin XM 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 J.J., Jr.1    Caruso, J.A.2    Mathieu, P.3    Chelladurai, B.4    Yin, X.M.5    Kessel, D.6
  • 30
    • 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
  • 31
    • 0034126114 scopus 로고    scopus 로고
    • Transcriptional activation of cathepsin D gene expression by growth factors
    • Wang F, Duan R, Chirgwin J and Safe SH (2000) Transcriptional activation of cathepsin D gene expression by growth factors. J. Mol. Endocrinol. 24: 193-202
    • (2000) J. Mol. Endocrinol. , vol.24 , pp. 193-202
    • Wang, F.1    Duan, R.2    Chirgwin, J.3    Safe, S.H.4
  • 33
    • 0026724311 scopus 로고
    • Structure and function of simian virus 40 large tumor antigen
    • Fanning E and Knippers R (1992) Structure and function of simian virus 40 large tumor antigen. Annu. Rev. Biochem. 61: 55-85
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 55-85
    • Fanning, E.1    Knippers, R.2
  • 34
    • 0028224571 scopus 로고
    • Stabilization of the tumor suppressor p53 during cellular transformation by simian virus 40: Influence of viral and cellular factors and biological consequences
    • Tiemann F and Deppert W (1994) Stabilization of the tumor suppressor p53 during cellular transformation by simian virus 40: influence of viral and cellular factors and biological consequences. J. Virol. 68: 2869-2878
    • (1994) J. Virol. , vol.68 , pp. 2869-2878
    • Tiemann, F.1    Deppert, W.2
  • 35
    • 0027218350 scopus 로고
    • Interactions between SV40 large-tumor antigen and the growth suppressor proteins pRb and p53
    • Ludlow JW (1993) Interactions between SV40 large-tumor antigen and the growth suppressor proteins pRb and p53. FASEB J. 7: 866-871
    • (1993) FASEB J. , vol.7 , pp. 866-871
    • Ludlow, J.W.1
  • 37
    • 0345713153 scopus 로고    scopus 로고
    • L-carnitine prevents doxorubicin-induced apoptosis of cardiac myocytes: Role of inhibition of ceramide generation
    • Andrieu-Abadie N, Jaffrézou JP, Hatem S, Laurent G, Levade T and Mercadier JJ (1999) L-carnitine prevents doxorubicin-induced apoptosis of cardiac myocytes: role of inhibition of ceramide generation. FASEB J. 13: 1501-1510
    • (1999) FASEB J. , vol.13 , pp. 1501-1510
    • Andrieu-Abadie, N.1    Jaffrézou, J.P.2    Hatem, S.3    Laurent, G.4    Levade, T.5    Mercadier, J.J.6
  • 38
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • Roberg K and Ollinger K (1998) Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am. J. Pathol. 152: 1151-1156
    • (1998) Am. J. Pathol. , vol.152 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 39
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K, Zhao M, Svensson I and Brunk UT (2001) Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359: 335-343
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 42
  • 43
    • 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
  • 46
    • 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 and 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
  • 50
    • 0037194598 scopus 로고    scopus 로고
    • Cathepsin-D affects multiple tumor progression steps in vivo: Proliferation, angiogenesis and apoptosis
    • Berchem G, Glondu M, Gleizes M, Brouillet JP, Vignon F, Garcia M and Liaudet-Coopman E (2002) Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis. Oncogene 21: 5951-5955
    • (2002) Oncogene , vol.21 , pp. 5951-5955
    • Berchem, G.1    Glondu, M.2    Gleizes, M.3    Brouillet, J.P.4    Vignon, F.5    Garcia, M.6    Liaudet-Coopman, E.7
  • 51
    • 0033043062 scopus 로고    scopus 로고
    • Cathepsin D in cancer metastasis: A protease and a ligand
    • Rochefort H and Liaudet-Coopman E (1999) Cathepsin D in cancer metastasis: a protease and a ligand. Apmis 107: 86-95
    • (1999) Apmis , vol.107 , pp. 86-95
    • Rochefort, H.1    Liaudet-Coopman, E.2
  • 52
    • 0036676298 scopus 로고    scopus 로고
    • Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells
    • Glondu M, Liaudet-Coopman E, Derocq D, Platet N, Rochefort H and Garcia M (2002) Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells. Oncogene 21: 5127-5134
    • (2002) Oncogene , vol.21 , pp. 5127-5134
    • Glondu, M.1    Liaudet-Coopman, E.2    Derocq, D.3    Platet, N.4    Rochefort, H.5    Garcia, M.6
  • 53
    • 0037266549 scopus 로고    scopus 로고
    • A replacement of the active site aspartic acid residue-293 in mouse cathepsin D affects its intracellular stability, processing, and transport in HEK 293 cells
    • Partanen S, Storch S, Loffler HG, Hasilik A, Tyynela J and Braulke T (2002) A replacement of the active site aspartic acid residue-293 in mouse cathepsin D affects its intracellular stability, processing, and transport in HEK 293 cells. Biochem. J. 369: 55-62
    • (2002) Biochem. J. , vol.369 , pp. 55-62
    • Partanen, S.1    Storch, S.2    Loffler, H.G.3    Hasilik, A.4    Tyynela, J.5    Braulke, T.6
  • 56
    • 0036340284 scopus 로고    scopus 로고
    • Increase in ceramide level alters the lysosomal targeting of cathepsin D prior to onset of apoptosis in HT-29 colon cancer cells
    • De Stefanis D, Reffo P, Bonelli G, Baccino FM, Sala G, Ghidoni R, Codogno P and Isidoro C (2002) Increase in ceramide level alters the lysosomal targeting of cathepsin D prior to onset of apoptosis in HT-29 colon cancer cells. Biol. Chem. 383: 989-999
    • (2002) Biol. Chem. , vol.383 , pp. 989-999
    • De Stefanis, D.1    Reffo, P.2    Bonelli, G.3    Baccino, F.M.4    Sala, G.5    Ghidoni, R.6    Codogno, P.7    Isidoro, C.8
  • 57
    • 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 UT (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
  • 60
    • 0037134774 scopus 로고    scopus 로고
    • Promotion of cathepsin L activity in newt spermatogonial apoptosis induced by prolactin
    • Fujimoto K, Yamamoto T, Kitano T and Abe S (2002) Promotion of cathepsin L activity in newt spermatogonial apoptosis induced by prolactin. FEBS Lett. 521: 43-46
    • (2002) FEBS Lett. , vol.521 , pp. 43-46
    • Fujimoto, K.1    Yamamoto, T.2    Kitano, T.3    Abe, S.4
  • 62
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • Denizot F and Lang R (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89: 271-277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 63
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch J, Lees M and Sloane Stanley GH (1957) A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226: 497-509
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3


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