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Volumn 16, Issue 5, 2003, Pages 337-348

Destination 'Lysosome': A target organelle for tumour cell killing?

Author keywords

Antiblastic drugs; Cancer; Cathepsins; Cell death

Indexed keywords

ANIMALS; CELL DEATH; HUMANS; LYSOSOMES; NEOPLASMS;

EID: 0141907718     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.643     Document Type: Conference Paper
Times cited : (70)

References (181)
  • 2
    • 0032543207 scopus 로고    scopus 로고
    • Defective acidification in human breast tumor cells and implications for chemotherapy
    • Altan N, Chen Y, Schindler M, Simon SM. 1998. Defective acidification in human breast tumor cells and implications for chemotherapy. J. Exp. Med. 187: 1583-98.
    • (1998) J. Exp. Med. , vol.187 , pp. 1583-1598
    • Altan, N.1    Chen, Y.2    Schindler, M.3    Simon, S.M.4
  • 3
    • 0021723696 scopus 로고
    • Control of degradation and growth phase in normal and neoplastic cells
    • Baccino FM, Tessitore L, Bonelli G. 1984. Control of degradation and growth phase in normal and neoplastic cells. Toxicol. Pathol. 12: 281-287.
    • (1984) Toxicol. Pathol. , vol.12 , pp. 281-287
    • Baccino, F.M.1    Tessitore, L.2    Bonelli, G.3
  • 4
    • 0026726492 scopus 로고
    • Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide
    • Ballou LR, Chao CP, Holness MA, Barker SC, Raghow R. 1992. Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide. J. Biol. Chem. 267: 20044-20050.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20044-20050
    • Ballou, L.R.1    Chao, C.P.2    Holness, M.A.3    Barker, S.C.4    Raghow, R.5
  • 5
    • 0028987672 scopus 로고
    • Physiological functions of lysosomal proteolysis
    • Berg T, Gjoen T, Bakke O. 1995. Physiological functions of lysosomal proteolysis. Biochem. J. 307: 313-326.
    • (1995) Biochem. J. , vol.307 , pp. 313-326
    • Berg, T.1    Gjoen, T.2    Bakke, O.3
  • 6
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart EF, Luiken JJ, Blommaart PJ, van Woerkom GM, Meijer AJ. 1995. Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem. 270: 2320-2326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    Van Woerkom, G.M.4    Meijer, A.J.5
  • 7
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • Bohley P, Seglen PO. 1992. Proteases and proteolysis in the lysosome. Experientia 48: 151-157.
    • (1992) Experientia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 9
    • 0033047235 scopus 로고    scopus 로고
    • Apoptosis without caspases: An inefficient molecular guillotine?
    • Borner C, Monney L. 1999. Apoptosis without caspases: an inefficient molecular guillotine? Cell Death Diff. 6: 497-507.
    • (1999) Cell Death Diff. , vol.6 , pp. 497-507
    • Borner, C.1    Monney, L.2
  • 10
    • 0032974475 scopus 로고    scopus 로고
    • Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells
    • Bossi G, Griffiths GM. 1999. Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells. Nat. Med. 5: 90-96.
    • (1999) Nat. Med. , vol.5 , pp. 90-96
    • Bossi, G.1    Griffiths, G.M.2
  • 11
    • 0017711169 scopus 로고
    • Regulation of protein degradation in normal and transformed human cells
    • Bradley MO. 1977. Regulation of protein degradation in normal and transformed human cells. J. Biol. Chem. 252: 5310-5315.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5310-5315
    • Bradley, M.O.1
  • 12
    • 0023784140 scopus 로고
    • In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells
    • Briozzo P, Morisset M, Capony F, Rougeot C, Rochefort H. 1988. In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells. Cancer Res. 48: 3688-3692.
    • (1988) Cancer Res. , vol.48 , pp. 3688-3692
    • Briozzo, P.1    Morisset, M.2    Capony, F.3    Rougeot, C.4    Rochefort, H.5
  • 14
    • 0030978333 scopus 로고    scopus 로고
    • Increased cathepsin D level in the serum of patients with metastatic breast carcinoma detected with a specific pro-cathepsin D immunoassay
    • Brouillet JP, Dufour F, Lemamy G, Garcia M, Schlup N, Grenier J, Mani JC, Rochefort H. 1997. Increased cathepsin D level in the serum of patients with metastatic breast carcinoma detected with a specific pro-cathepsin D immunoassay. Cancer 79: 2132-2136.
    • (1997) Cancer , vol.79 , pp. 2132-2136
    • Brouillet, J.P.1    Dufour, F.2    Lemamy, G.3    Garcia, M.4    Schlup, N.5    Grenier, J.6    Mani, J.C.7    Rochefort, H.8
  • 15
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown WJ, DeWald DB, Emr SD, Plutner H, Balch WE. 1995. Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130: 781-796.
    • (1995) J. Cell Biol. , vol.130 , pp. 781-796
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 16
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk UT, Svensson I. 1999. Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep. 4: 3-11.
    • (1999) Redox Rep. , vol.4 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 17
    • 0032855120 scopus 로고    scopus 로고
    • Cellular uptake, cytotoxicity and DNA-binding studies of the novel imidazoacridinone antineoplastic agent C1311
    • Burger AM, Jenkins TC, Double JA, Bibby MC. 1999. Cellular uptake, cytotoxicity and DNA-binding studies of the novel imidazoacridinone antineoplastic agent C1311. Br. J. Cancer 81: 367-375.
    • (1999) Br. J. Cancer , vol.81 , pp. 367-375
    • Burger, A.M.1    Jenkins, T.C.2    Double, J.A.3    Bibby, M.C.4
  • 18
    • 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
  • 19
    • 0029741890 scopus 로고    scopus 로고
    • Active cell death induced by the anti-estrogens tamoxifen and ICI 164 384 in human mammary carcinoma cells (MCF-7) in culture: The role of autophagy
    • Bursch W, Ellinger A, Kienzl H, Torok L, Pandey S, Sikorska M, Walker R, Hermann RS. 1996. Active cell death induced by the anti-estrogens tamoxifen and ICI 164 384 in human mammary carcinoma cells (MCF-7) in culture: the role of autophagy. Carcinogenesis 17: 1595-607.
    • (1996) Carcinogenesis , vol.17 , pp. 1595-1607
    • Bursch, W.1    Ellinger, A.2    Kienzl, H.3    Torok, L.4    Pandey, S.5    Sikorska, M.6    Walker, R.7    Hermann, R.S.8
  • 21
    • 0024321224 scopus 로고
    • Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells
    • Capony F, Rougeot C, Montcourrier P, Cavailles V, Salazar G, Rochefort H. 1989. Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells. Cancer Res. 49: 3904-3909.
    • (1989) Cancer Res. , vol.49 , pp. 3904-3909
    • Capony, F.1    Rougeot, C.2    Montcourrier, P.3    Cavailles, V.4    Salazar, G.5    Rochefort, H.6
  • 22
    • 0028130332 scopus 로고
    • Specific mannose-6-phosphate receptor-independent sorting of pro-cathepsin D in breast cancer cells
    • Capony F, Braulke T, Rougeot C, Roux S, Montcourrier P, Rochefort H. 1994. Specific mannose-6-phosphate receptor-independent sorting of pro-cathepsin D in breast cancer cells. Exp. Cell Res. 215: 154-163.
    • (1994) Exp. Cell Res. , vol.215 , pp. 154-163
    • Capony, F.1    Braulke, T.2    Rougeot, C.3    Roux, S.4    Montcourrier, P.5    Rochefort, H.6
  • 23
    • 0028267096 scopus 로고
    • Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells
    • Cardone MH, Smith BL, Song W, Mochly-Rosen D, Mostov KE. 1994. Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells. J. Cell Biol. 124: 717-727.
    • (1994) J. Cell Biol. , vol.124 , pp. 717-727
    • Cardone, M.H.1    Smith, B.L.2    Song, W.3    Mochly-Rosen, D.4    Mostov, K.E.5
  • 24
    • 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, 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
  • 27
    • 0028788935 scopus 로고
    • The 70 kDa S6 kinase: Regulation of a kinase with multiple roles in mitogenic signalling
    • Chou MM, Blenis J. 1995. The 70 kDa S6 kinase: regulation of a kinase with multiple roles in mitogenic signalling. Curr. Opin. Cell Biol. 7: 806-814.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 806-814
    • Chou, M.M.1    Blenis, J.2
  • 28
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung J, Kuo CJ, Crabtree GR, Blenis J. 1992. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 69: 1227-1236.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 29
    • 0037189948 scopus 로고    scopus 로고
    • Ceramide generated by acidic sphingomyelinase contributes to tumour necrosis factor-α-mediated apoptosis in human colon HT-29 cells through glycosphingolipid formation. Possible role of ganglioside GD3
    • Colell A, Morales A, Fernadez-Checa J, Garcia-Ruiz C. 2002. Ceramide generated by acidic sphingomyelinase contributes to tumour necrosis factor-α-mediated apoptosis in human colon HT-29 cells through glycosphingolipid formation. Possible role of ganglioside GD3. FEBS Lett. 526: 135-141.
    • (2002) FEBS Lett. , vol.526 , pp. 135-141
    • Colell, A.1    Morales, A.2    Fernadez-Checa, J.3    Garcia-Ruiz, C.4
  • 30
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. 2002. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 31
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo AM, Dice JF. 1998. Lysosomes, a meeting point of proteins, chaperones, and proteases. J. Mol. Med. 76: 6-12.
    • (1998) J. Mol. Med. , vol.76 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 32
    • 0037413688 scopus 로고    scopus 로고
    • Cathepsin a regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor
    • Cuervo AM, Mann L, Bonten EJ, d'Azzo A, Dice JF. 2003. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. EMBO J. 22: 47-59.
    • (2003) EMBO J. , vol.22 , pp. 47-59
    • Cuervo, A.M.1    Mann, L.2    Bonten, E.J.3    D'Azzo, A.4    Dice, J.F.5
  • 33
    • 0032578469 scopus 로고    scopus 로고
    • Cytotoxic agents directed to peptide hormone receptors: Defining the requirements for a successful drug
    • Czerwinski G, Tarasova NI, Michejda CJ. 1998. Cytotoxic agents directed to peptide hormone receptors: defining the requirements for a successful drug. Proc. Natl Acad. Sci. USA 95: 11520-11525.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11520-11525
    • Czerwinski, G.1    Tarasova, N.I.2    Michejda, C.J.3
  • 34
    • 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
  • 35
    • 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, 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
  • 36
    • 0345280022 scopus 로고    scopus 로고
    • Transformation by oncogenic ras-p21 alters the processing and subcellular localization of the lysosomal protease cathepsin D
    • Démoz M, Castino R, Dragonetti A, Raiteri E, Baccino FM, Isidoro C. 1999. Transformation by oncogenic ras-p21 alters the processing and subcellular localization of the lysosomal protease cathepsin D. J. Cell Biochem. 73: 370-378.
    • (1999) J. Cell Biochem. , vol.73 , pp. 370-378
    • Démoz, M.1    Castino, R.2    Dragonetti, A.3    Raiteri, E.4    Baccino, F.M.5    Isidoro, C.6
  • 37
    • 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
    • Démoz M, Castino R, Cesaro P, Baccino FM, Bonelli G, 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
    • Démoz, M.1    Castino, R.2    Cesaro, P.3    Baccino, F.M.4    Bonelli, G.5    Isidoro, C.6
  • 38
    • 0032999830 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): Balancing the opposing forces of protein synthesis and degradation
    • Dennis PB, Fumagalli S, Thomas G. 1999. Target of rapamycin (TOR): balancing the opposing forces of protein synthesis and degradation. Curr. Opin. Genet. Dev. 9: 49-54.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 49-54
    • Dennis, P.B.1    Fumagalli, S.2    Thomas, G.3
  • 39
    • 0030949251 scopus 로고    scopus 로고
    • Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line
    • De Stefanis D, Démoz M, Dragonetti A, Houri JJ, Ogier-Denis, Codogno, Baccino FM, Isidoro C. 1997. Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line. Cell Tissue Res. 289: 109-117.
    • (1997) Cell Tissue Res. , vol.289 , pp. 109-117
    • De Stefanis, D.1    Démoz, M.2    Dragonetti, A.3    Houri, J.J.4    Ogier-Denis5    Codogno6    Baccino, F.M.7    Isidoro, C.8
  • 40
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • Di Cristofano A, Pandolfi PP. 2000. The multiple roles of PTEN in tumor suppression. Cell 100: 387-390.
    • (2000) Cell , vol.100 , pp. 387-390
    • Di Cristofano, A.1    Pandolfi, P.P.2
  • 41
    • 0033785510 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL
    • Dragonetti A, Baldassare M, Castino R, Démoz M, Luini A, Buccione R, Isidoro C. 2000. The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL. J. Cell Sci. 113: 3289-3298.
    • (2000) J. Cell Sci. , vol.113 , pp. 3289-3298
    • Dragonetti, A.1    Baldassare, M.2    Castino, R.3    Démoz, M.4    Luini, A.5    Buccione, R.6    Isidoro, C.7
  • 42
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: Formation of the autophagic vacuole
    • Dunn WA. 1990. Studies on the mechanisms of autophagy: formation of the autophagic vacuole. J. Cell. Biol. 110: 1923-1933.
    • (1990) J. Cell. Biol. , vol.110 , pp. 1923-1933
    • Dunn, W.A.1
  • 43
    • 0028222874 scopus 로고
    • Authophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn WA. 1994. Authophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell. Biol. 4: 139-143.
    • (1994) Trends Cell. Biol. , vol.4 , pp. 139-143
    • Dunn, W.A.1
  • 44
    • 0036226609 scopus 로고    scopus 로고
    • Early endosomes, late endosomes, and lysosomes display distinct partitioning strategies of inheritance with similarities to Golgi-derived membranes
    • Dunster K, Toh BH, Sentry JW. 2002. Early endosomes, late endosomes, and lysosomes display distinct partitioning strategies of inheritance with similarities to Golgi-derived membranes. Eur. J. Cell Biol. 81: 117-124.
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 117-124
    • Dunster, K.1    Toh, B.H.2    Sentry, J.W.3
  • 45
    • 0029585762 scopus 로고
    • Rab 7: An important regulator of late endocytic membrane traffic
    • Feng Y, Press B, Wandinger-Ness A. 1995. Rab 7: an important regulator of late endocytic membrane traffic. J. Cell Biol. 131: 1435-1452.
    • (1995) J. Cell Biol. , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 46
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF, Kroemer G. 2001. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3: E255-E263.
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 48
    • 0028220687 scopus 로고
    • Cell death induced by peroxidized low-density lipoprotein: Endopepsis
    • Fossel ET, Zanella CL, Fletcher JG, Hui KK. 1994. Cell death induced by peroxidized low-density lipoprotein: endopepsis. Cancer Res. 54: 1240-1248.
    • (1994) Cancer Res. , vol.54 , pp. 1240-1248
    • Fossel, E.T.1    Zanella, C.L.2    Fletcher, J.G.3    Hui, K.K.4
  • 49
    • 0036155773 scopus 로고    scopus 로고
    • Defective death receptor signaling as a cause of tumor immune escape
    • French LE, Tschopp J. 2002. Defective death receptor signaling as a cause of tumor immune escape. Semin. Cancer Biol. 12: 51-55.
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 51-55
    • French, L.E.1    Tschopp, J.2
  • 50
    • 0025596963 scopus 로고
    • Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency
    • Garcia M, Derocq D, Pujol P, Rochefort H. 1990. Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency. Oncogene 5: 1809-1814.
    • (1990) Oncogene , vol.5 , pp. 1809-1814
    • Garcia, M.1    Derocq, D.2    Pujol, P.3    Rochefort, H.4
  • 51
    • 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, 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
  • 52
    • 0025413403 scopus 로고
    • The role of cathepsin L in malignant transformation
    • Gottesman MM, Kane SE. 1990. The role of cathepsin L in malignant transformation. Semin. Cancer Biol. 1: 127-136.
    • (1990) Semin. Cancer Biol. , vol.1 , pp. 127-136
    • Gottesman, M.M.1    Kane, S.E.2
  • 53
    • 0018751252 scopus 로고
    • Further studies of the effect of pepstatin on ascites accumulation in tumor-bearing mice
    • Greenbaum LM, Esumi H, Sato S. 1979. Further studies of the effect of pepstatin on ascites accumulation in tumor-bearing mice. Cancer Lett. 7: 91-96.
    • (1979) Cancer Lett. , vol.7 , pp. 91-96
    • Greenbaum, L.M.1    Esumi, H.2    Sato, S.3
  • 54
    • 0033178702 scopus 로고    scopus 로고
    • Regulation of cell growth and cyclin D1 expression by the constitutively active FRAP-p70s6K pathway in human pancreatic cancer cells
    • Grewe M, Gansauge F, Schmid RM, Adler G, Seufferlein T. 1999. Regulation of cell growth and cyclin D1 expression by the constitutively active FRAP-p70s6K pathway in human pancreatic cancer cells. Cancer Res. 59: 3581-3587.
    • (1999) Cancer Res. , vol.59 , pp. 3581-3587
    • Grewe, M.1    Gansauge, F.2    Schmid, R.M.3    Adler, G.4    Seufferlein, T.5
  • 55
    • 0023839303 scopus 로고
    • The mannose 6-phosphate receptor and the biogenesis of lysosomes
    • Griffiths G, Hoflack B, Simons K, Mellman I, Kornfeld S. 1988. The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell 52: 329-341.
    • (1988) Cell , vol.52 , pp. 329-341
    • Griffiths, G.1    Hoflack, B.2    Simons, K.3    Mellman, I.4    Kornfeld, S.5
  • 56
    • 0033030397 scopus 로고    scopus 로고
    • Biogenesis of transport intermediates in the endocytic pathway
    • Gu F, Gruenberg J. 1999. Biogenesis of transport intermediates in the endocytic pathway. FEBS Lett. 452: 61-66.
    • (1999) FEBS Lett. , vol.452 , pp. 61-66
    • Gu, F.1    Gruenberg, J.2
  • 58
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC, Scheller RH. 1997. SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9: 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 60
    • 0028333052 scopus 로고
    • Tumor necrosis factor receptor-mediated signaling pathways
    • Heller RA, Kronke M. 1994. Tumor necrosis factor receptor-mediated signaling pathways. J. Cell Biol. 126: 5-9.
    • (1994) J. Cell Biol. , vol.126 , pp. 5-9
    • Heller, R.A.1    Kronke, M.2
  • 61
    • 0030670626 scopus 로고    scopus 로고
    • Activation of CD95 (APO-1/Fas) signaling by ceramide mediates cancer therapy-induced apoptosis
    • Herr I, Wilhelm D, Bohler T, Angel P, Debatin KM. 1997. Activation of CD95 (APO-1/Fas) signaling by ceramide mediates cancer therapy-induced apoptosis. EMBO J. 16: 6200-6208.
    • (1997) EMBO J. , vol.16 , pp. 6200-6208
    • Herr, I.1    Wilhelm, D.2    Bohler, T.3    Angel, P.4    Debatin, K.M.5
  • 62
    • 0027172110 scopus 로고
    • Serum cathepsin B levels and urinary excretion of cathepsin B in the cancer patients with remote metastasis
    • Hirano T, Manabe T, Takeuchi S. 1993. Serum cathepsin B levels and urinary excretion of cathepsin B in the cancer patients with remote metastasis. Cancer Lett. 70: 41-44.
    • (1993) Cancer Lett. , vol.70 , pp. 41-44
    • Hirano, T.1    Manabe, T.2    Takeuchi, S.3
  • 63
    • 0026645413 scopus 로고
    • Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity
    • Holen I, Gordon PB, Seglen PO. 1992. Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity. Biochem. J. 284: 633-636.
    • (1992) Biochem. J. , vol.284 , pp. 633-636
    • Holen, I.1    Gordon, P.B.2    Seglen, P.O.3
  • 65
    • 0037192768 scopus 로고    scopus 로고
    • PTEN modulates vascular endothelial growth factor-mediated signaling and angiogenic effects
    • Huang J, Kontos CD. 2002. PTEN modulates vascular endothelial growth factor-mediated signaling and angiogenic effects. J. Biol. Chem. 277: 10760-10766.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10760-10766
    • Huang, J.1    Kontos, C.D.2
  • 67
    • 0029642258 scopus 로고
    • Synthesis, maturation and extracellular release of procathepsin D as influenced by cell proliferation or transformation
    • Isidore C, Démoz M, De Stefanis D, Baccino FM, Monelli G. 1995a. Synthesis, maturation and extracellular release of procathepsin D as influenced by cell proliferation or transformation. Int. J. Cancer 63: 866-871.
    • (1995) Int. J. Cancer , vol.63 , pp. 866-871
    • Isidore, C.1    Démoz, M.2    De Stefanis, D.3    Baccino, F.M.4    Monelli, G.5
  • 68
    • 0029549627 scopus 로고
    • High levels of proteolytic enzymes in the ascitic fluid and plasma of rats bearing the Yoshida AH-130 hepatoma
    • Isidoro C, Demoz M, De Stefanis D, Baccino FM, Bonelli G. 1995b. High levels of proteolytic enzymes in the ascitic fluid and plasma of rats bearing the Yoshida AH-130 hepatoma. Invasion Metastasis 15: 116-124.
    • (1995) Invasion Metastasis , vol.15 , pp. 116-124
    • Isidoro, C.1    Demoz, M.2    De Stefanis, D.3    Baccino, F.M.4    Bonelli, G.5
  • 69
    • 0028897623 scopus 로고
    • Altered intracellular processing and enhanced secretion of procathepsin D in a highly deviated rat hepatoma
    • Isidoro C, Demoz M, De Stefanis D, Mainferme F, Wattiaux R, Baccino FM. 1995c. Altered intracellular processing and enhanced secretion of procathepsin D in a highly deviated rat hepatoma. Int. J. Cancer 60: 61-64.
    • (1995) Int. J. Cancer , vol.60 , pp. 61-64
    • Isidoro, C.1    Demoz, M.2    De Stefanis, D.3    Mainferme, F.4    Wattiaux, R.5    Baccino, F.M.6
  • 70
    • 0030931555 scopus 로고    scopus 로고
    • Expression and Posttranslational fate of cathepsin D in HT-29 tumor cells depend on their enterocytic differentiation state
    • Isidoro C, de Stefanis D, Démoz M, Ogier-Denis E, Codogno P, Baccino FM. 1997a. Expression and Posttranslational fate of cathepsin D in HT-29 tumor cells depend on their enterocytic differentiation state. Cell Growth Diff. 8: 1029-1037.
    • (1997) Cell Growth Diff. , vol.8 , pp. 1029-1037
    • Isidoro, C.1    De Stefanis, D.2    Démoz, M.3    Ogier-Denis, E.4    Codogno, P.5    Baccino, F.M.6
  • 71
    • 1842404183 scopus 로고    scopus 로고
    • Differential targeting and processing of procathepsin D in normal and transformed murine 3T3 fibroblasts
    • Isidoro C, Démoz M, De Stefanis D, Baccino FM, Hasilik A, Bonelli G. 1997b. Differential targeting and processing of procathepsin D in normal and transformed murine 3T3 fibroblasts. Int. J. Cancer 70: 310-314.
    • (1997) Int. J. Cancer , vol.70 , pp. 310-314
    • Isidoro, C.1    Démoz, M.2    De Stefanis, D.3    Baccino, F.M.4    Hasilik, A.5    Bonelli, G.6
  • 72
    • 0030896013 scopus 로고    scopus 로고
    • Mis-sorting of procathepsin D in metastogenic tumor cells is not due to impaired synthesis of the phosphomannosyl signal
    • Isidoro C, Baccino FM, Hasilik A. 1997c. Mis-sorting of procathepsin D in metastogenic tumor cells is not due to impaired synthesis of the phosphomannosyl signal. Int. J. Cancer 70: 561-566.
    • (1997) Int. J. Cancer , vol.70 , pp. 561-566
    • Isidoro, C.1    Baccino, F.M.2    Hasilik, A.3
  • 73
    • 0037184909 scopus 로고    scopus 로고
    • Taking the study of cancer cell survival to a new dimension
    • Jacks T, Wienberg RA. 2002. Taking the study of cancer cell survival to a new dimension. Cell 111: 923-925.
    • (2002) Cell , vol.111 , pp. 923-925
    • Jacks, T.1    Wienberg, R.A.2
  • 74
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
    • Jaiswal JK, Andrews NW, Simon SM. 2002. Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol. 25: 625-635.
    • (2002) J. Cell Biol. , vol.25 , pp. 625-635
    • Jaiswal, J.K.1    Andrews, N.W.2    Simon, S.M.3
  • 75
    • 0030883558 scopus 로고    scopus 로고
    • Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells
    • Jia L, Dourmashkin RR, Allen PD, Gray AB, Newland AC, Kelsey SM. 1997. Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells. Br. J. Haematol 98: 673-685.
    • (1997) Br. J. Haematol , vol.98 , pp. 673-685
    • Jia, L.1    Dourmashkin, R.R.2    Allen, P.D.3    Gray, A.B.4    Newland, A.C.5    Kelsey, S.M.6
  • 76
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K, Zhao M, Svensson I, 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
  • 78
    • 0032563130 scopus 로고    scopus 로고
    • Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network
    • Karlsson K, Carlsson SR. 1998. Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network. J. Biol. Chem. 273: 18966-18973.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18966-18973
    • Karlsson, K.1    Carlsson, S.R.2
  • 79
    • 0034987122 scopus 로고    scopus 로고
    • Novel procaspase-3 activating cascade mediated by lysoapoptases and its biological significances in apoptosis
    • Katunuma N, Matsui A, Le QT, Utsumi K, Salvesen G, Ohashi A. 2001. Novel procaspase-3 activating cascade mediated by lysoapoptases and its biological significances in apoptosis. Adv. Enzyme. Regul. 41: 237-250.
    • (2001) Adv. Enzyme. Regul. , vol.41 , pp. 237-250
    • Katunuma, N.1    Matsui, A.2    Le, Q.T.3    Utsumi, K.4    Salvesen, G.5    Ohashi, A.6
  • 81
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26: 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 82
    • 0035032723 scopus 로고    scopus 로고
    • Beclinphosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A, Kabeya Y, Ohsumi Y, Yoshimori T. 2001. Beclinphosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2: 330-335.
    • (2001) EMBO Rep. , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 83
    • 12444332679 scopus 로고    scopus 로고
    • Richardson CC, Abelson JN, Raetz CRH, Thorner JW (eds). Annual Rewiews: Palo Alto CA
    • Kim J, Klionsky DJ. 2000. Annual Review of Biochemistry, Vol. 69, Richardson CC, Abelson JN, Raetz CRH, Thorner JW (eds). Annual Rewiews: Palo Alto CA; 304-336.
    • (2000) Annual Review of Biochemistry , vol.69 , pp. 304-336
    • Kim, J.1    Klionsky, D.J.2
  • 85
    • 0032971161 scopus 로고    scopus 로고
    • Caspase-independent programmed cell death with necrotic morphology
    • Kitanaka C, Kuchino Y. 1999. Caspase-independent programmed cell death with necrotic morphology. Cell Death Diff. 6: 508-515.
    • (1999) Cell Death Diff. , vol.6 , pp. 508-515
    • Kitanaka, C.1    Kuchino, Y.2
  • 86
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD. 2000. Autophagy as a regulated pathway of cellular degradation. Science 290: 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 87
    • 0023785754 scopus 로고
    • The effect of lysosomotropic agents and secretory inhibitors on anthracycline retention and activity in multiple drug-resistant cells
    • Klohs WD, Steinkampf RW. 1988. The effect of lysosomotropic agents and secretory inhibitors on anthracycline retention and activity in multiple drug-resistant cells. Mol. Pharmac. 34: 180-185.
    • (1988) Mol. Pharmac. , vol.34 , pp. 180-185
    • Klohs, W.D.1    Steinkampf, R.W.2
  • 88
    • 0021175877 scopus 로고
    • Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions
    • Knecht E, Hernandez-Yago J, Grisolia S. 1984. Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions. Exp. Cell Res. 154: 224-232.
    • (1984) Exp. Cell Res. , vol.154 , pp. 224-232
    • Knecht, E.1    Hernandez-Yago, J.2    Grisolia, S.3
  • 89
    • 0025051251 scopus 로고
    • Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes
    • Kopitz J, Kisen GO, Gordon PB, Bohley P, Seglen PO. 1990. Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes. J. Cell Biol. 111: 941-953.
    • (1990) J. Cell Biol. , vol.111 , pp. 941-953
    • Kopitz, J.1    Kisen, G.O.2    Gordon, P.B.3    Bohley, P.4    Seglen, P.O.5
  • 92
    • 0029794385 scopus 로고    scopus 로고
    • The ICE family of cysteine proteases as effectors of cell death
    • Kumar S, Lavin MF. 1996. The ICE family of cysteine proteases as effectors of cell death. Cell Death Diff. 3: 255-268.
    • (1996) Cell Death Diff. , vol.3 , pp. 255-268
    • Kumar, S.1    Lavin, M.F.2
  • 95
    • 0028228172 scopus 로고
    • Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis formation in mice with mammary and ovarian tumors
    • Leto G, Pizzolanti G, Tumminello FM, Gebbia N. 1994. Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis formation in mice with mammary and ovarian tumors. In Vivo 8: 231-236.
    • (1994) In Vivo , vol.8 , pp. 231-236
    • Leto, G.1    Pizzolanti, G.2    Tumminello, F.M.3    Gebbia, N.4
  • 99
    • 0028281477 scopus 로고
    • Cathepsin D maturation and its stimulatory effect on metastasis are prevented by addition of KDEL retention signal
    • Liaudet E, Garcia M, Rochefort H. 1994. Cathepsin D maturation and its stimulatory effect on metastasis are prevented by addition of KDEL retention signal. Oncogene 9: 1145-1154.
    • (1994) Oncogene , vol.9 , pp. 1145-1154
    • Liaudet, E.1    Garcia, M.2    Rochefort, H.3
  • 100
    • 0021079540 scopus 로고
    • Tumor invasion and the extracellular matrix
    • Liotta LA, Rao CN, Barsky SH. 1983. Tumor invasion and the extracellular matrix. Lab. Invest. 49: 636-649.
    • (1983) Lab. Invest. , vol.49 , pp. 636-649
    • Liotta, L.A.1    Rao, C.N.2    Barsky, S.H.3
  • 101
    • 0020354209 scopus 로고
    • Protein turnover and proliferation. Failure of SV-3T3 cells to increase lysosomal proteinases, increase protein degradation and cease net protein accumulation
    • Lockwood TD, Minassian IA. 1982. Protein turnover and proliferation. Failure of SV-3T3 cells to increase lysosomal proteinases, increase protein degradation and cease net protein accumulation. Biochem. J. 206: 251-258.
    • (1982) Biochem. J. , vol.206 , pp. 251-258
    • Lockwood, T.D.1    Minassian, I.A.2
  • 102
    • 0017399059 scopus 로고
    • Regulation of acid proteases during growth, quiescence and starvation in normal and transformed cells
    • Lockwood TD, Shier WT. 1977. Regulation of acid proteases during growth, quiescence and starvation in normal and transformed cells. Nature 267: 252-254.
    • (1977) Nature , vol.267 , pp. 252-254
    • Lockwood, T.D.1    Shier, W.T.2
  • 103
    • 0020420797 scopus 로고
    • Protein turnover and proliferation. Turnover kinetics associated with elevation of 3T3-cell acid-proteinase activity and cessation of net protein gain
    • Lockwood TD, Minassian IA, Roux L. 1982. Protein turnover and proliferation. Turnover kinetics associated with elevation of 3T3-cell acid-proteinase activity and cessation of net protein gain. Biochem. J. 206: 239-249.
    • (1982) Biochem. J. , vol.206 , pp. 239-249
    • Lockwood, T.D.1    Minassian, I.A.2    Roux, L.3
  • 104
    • 0033869531 scopus 로고    scopus 로고
    • Invasive properties of murine squamouscarcinoma cells: Secretion of matrix-degrading cathepsins is attributable to a deficiency in the mannose 6-phosphate/insulin-like growth factor II receptor
    • Lorenzo K, Ton P, Clark JL, Coulibaly S, Mach L. 2000. Invasive properties of murine squamouscarcinoma cells: secretion of matrix-degrading cathepsins is attributable to a deficiency in the mannose 6-phosphate/insulin-like growth factor II receptor. Cancer Res. 60: 4070-4076.
    • (2000) Cancer Res. , vol.60 , pp. 4070-4076
    • Lorenzo, K.1    Ton, P.2    Clark, J.L.3    Coulibaly, S.4    Mach, L.5
  • 107
    • 0030036657 scopus 로고    scopus 로고
    • Induction of apoptosis in primary culture of rat hepatocytes by protease inhibitors
    • Maeda S, Lin KH, Inagaki H, Saito T. 1996. Induction of apoptosis in primary culture of rat hepatocytes by protease inhibitors. Biochem. Mol. Biol. Int. 39: 447-453.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 447-453
    • Maeda, S.1    Lin, K.H.2    Inagaki, H.3    Saito, T.4
  • 108
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni R, Kreis TE. 1987. Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105: 1253-1265.
    • (1987) J. Cell Biol. , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 109
    • 0030037845 scopus 로고    scopus 로고
    • Membranes and sorting
    • Mellman I. 1996. Membranes and sorting. Curr. Opin. Cell Biol. 8: 497-498.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 497-498
    • Mellman, I.1
  • 110
    • 0028803110 scopus 로고
    • The rab7 GTPase resides on a vesicular compartment connected to lysosomes
    • Meresse S, Gorvel JP, Chavrier P. 1995. The rab7 GTPase resides on a vesicular compartment connected to lysosomes. J. Cell Sci. 108: 3349-3358.
    • (1995) J. Cell Sci. , vol.108 , pp. 3349-3358
    • Meresse, S.1    Gorvel, J.P.2    Chavrier, P.3
  • 111
    • 0017158118 scopus 로고
    • Cellular autophagocytosis induced by deprivation of serum and amino acids in HeLa cells
    • Mitchener JS, Shelburne JD, Bradford WD, Hawkins HK. 1976. Cellular autophagocytosis induced by deprivation of serum and amino acids in HeLa cells. Am. J. Pathol. 83: 485-498.
    • (1976) Am. J. Pathol. , vol.83 , pp. 485-498
    • Mitchener, J.S.1    Shelburne, J.D.2    Bradford, W.D.3    Hawkins, H.K.4
  • 114
    • 0032518448 scopus 로고    scopus 로고
    • Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis
    • Monney L, Olivier R, Otter I, Jansen B, Poirier GG, Borner C. 1998. Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis. Eur. J. Biochem. 251: 295-303.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 295-303
    • Monney, L.1    Olivier, R.2    Otter, I.3    Jansen, B.4    Poirier, G.G.5    Borner, C.6
  • 117
    • 0025720108 scopus 로고
    • A potent and specific immunotoxin for tumor cells expressing disialoganglioside GD2
    • Mujoo K, Reisfeld RA, Cheung L, Rosenblum MG. 1991. A potent and specific immunotoxin for tumor cells expressing disialoganglioside GD2. Cancer Immunol. Immunother. 34: 198-204.
    • (1991) Cancer Immunol. Immunother. , vol.34 , pp. 198-204
    • Mujoo, K.1    Reisfeld, R.A.2    Cheung, L.3    Rosenblum, M.G.4
  • 118
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafo DB, Colombo MI. 2001. A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation. J. Cell Sci. 114: 3619-3629.
    • (2001) J. Cell Sci. , vol.114 , pp. 3619-3629
    • Munafo, D.B.1    Colombo, M.I.2
  • 119
    • 0033052252 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate-induced apoptosis in Jurkat T cells involves caspase-3 activation, and both lysosomal and mitochondrial destabilisation
    • Neuzil J, Svensson I, Weber T, Weber C, Brunk UT. 1999. Alpha-tocopheryl succinate-induced apoptosis in Jurkat T cells involves caspase-3 activation, and both lysosomal and mitochondrial destabilisation. FEBS Lett. 445: 295-300.
    • (1999) FEBS Lett. , vol.445 , pp. 295-300
    • Neuzil, J.1    Svensson, I.2    Weber, T.3    Weber, C.4    Brunk, U.T.5
  • 120
    • 0037086662 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability
    • Neuzil J, Zhao M, Ostermann G, Sticha M, Gellert N, Weber C, Eaton JW, 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
    • 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
  • 121
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick P, Zerial M. 1997. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9: 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 122
    • 0028239912 scopus 로고
    • GTPases: Multifunctional molecular switches regulating vesicular traffic
    • Nuoffer C, Balch WE. 1994. GTPases: multifunctional molecular switches regulating vesicular traffic. A. Rev. Biochem. 63: 949-990.
    • (1994) A. Rev. Biochem. , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 124
    • 0029905203 scopus 로고    scopus 로고
    • Guanine nucleotide exchange on heterotrimeric Gi3 protein controls autophagic sequestration in HT-29 cells
    • Ogier-Denis E, Houri JJ, Bauvy C, Codogno P. 1996. Guanine nucleotide exchange on heterotrimeric Gi3 protein controls autophagic sequestration in HT-29 cells. J. Biol. Chem. 27: 28593-28600.
    • (1996) J. Biol. Chem. , vol.27 , pp. 28593-28600
    • Ogier-Denis, E.1    Houri, J.J.2    Bauvy, C.3    Codogno, P.4
  • 125
    • 0035744047 scopus 로고    scopus 로고
    • Updates on functions of ceramide in chemotherapy-induced cell death and in multidrug resistance
    • Ogretmen B, Hannun YA. 2001. Updates on functions of ceramide in chemotherapy-induced cell death and in multidrug resistance. Drug Resist. Update 4: 368-377.
    • (2001) Drug Resist. Update , vol.4 , pp. 368-377
    • Ogretmen, B.1    Hannun, Y.A.2
  • 126
    • 0034650786 scopus 로고    scopus 로고
    • Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes
    • Ollinger K. 2000. Inhibition of cathepsin D prevents free-radical-induced apoptosis in rat cardiomyocytes. Arch. Biochem. Biophys. 373: 346-351.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 346-351
    • Ollinger, K.1
  • 127
    • 0034232504 scopus 로고    scopus 로고
    • Endocytic recycling is required for the presentation of an exogenous peptide via MHC class II molecules
    • Pathak SS, Blum JS. 2000. Endocytic recycling is required for the presentation of an exogenous peptide via MHC class II molecules. Traffic 1: 561-569.
    • (2000) Traffic , vol.1 , pp. 561-569
    • Pathak, S.S.1    Blum, J.S.2
  • 128
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. 2000. Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J. Biol. Chem. 14: 992-998.
    • (2000) J. Biol. Chem. , vol.14 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 130
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • Pfeffer SR. 2001. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11: 487-491.
    • (2001) Trends Cell Biol. , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 132
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor PR, Mullock BM, Bright NA, Gray SR, Luzio JP. 2000. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 149: 1053-1062.
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 133
    • 0036377840 scopus 로고    scopus 로고
    • The biological role of the Fas/FasL system during tumor formation and progression
    • Reichmann E. 2002. The biological role of the Fas/FasL system during tumor formation and progression. Semin. Cancer Biol. 12: 309-315.
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 309-315
    • Reichmann, E.1
  • 134
    • 0036732169 scopus 로고    scopus 로고
    • Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage
    • Reiners JJ Jr, Caruso JA, Mathieu P, Chelladurai B, Yin XM, Kessel D. 2002. Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage. Cell Death Diff. 9: 934-944.
    • (2002) Cell Death Diff. , 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
  • 135
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L.
    • Reinheckel T, Deussing J, Roth W, Peters C. 2001. Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem. 382: 735-741.
    • (2001) Biol. Chem. , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 136
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer MA, Soldati T, Shapiro AD, Lin J, Pfeffer SR. 1994. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 125: 573-582.
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.R.5
  • 137
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese RJ, Chapman HA. 2000. Cathepsins and compartmentalization in antigen presentation. Curr. Opin. Immunol. 12: 107-113.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 138
    • 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, 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
  • 139
    • 0025690427 scopus 로고
    • Cathepsin D: A protease involved in breast cancer metastasis
    • Rochefort H, Capony F, Garcia M. 1990. Cathepsin D: a protease involved in breast cancer metastasis. Cancer Metastasis Rev. 9: 321-331.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 321-331
    • Rochefort, H.1    Capony, F.2    Garcia, M.3
  • 140
    • 0037946767 scopus 로고    scopus 로고
    • Messengers of cell death: Apoptotic signaling in health and disease
    • Rossi D, Gaidano G. 2003. Messengers of cell death: apoptotic signaling in health and disease. Haematologica 88: 212-218.
    • (2003) Haematologica , vol.88 , pp. 212-218
    • Rossi, D.1    Gaidano, G.2
  • 141
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. 1994. Mechanisms of intracellular protein transport. Nature 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 142
    • 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, et al. 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
  • 143
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmeizie T, Hall MN. 2000. TOR, a central controller of cell growth. Cell 103: 253-262.
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmeizie, T.1    Hall, M.N.2
  • 145
    • 0032489554 scopus 로고    scopus 로고
    • TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase
    • Schwandner R, Wiegmann K, Bernardo K, Kreder D, Kronke M. 1998. TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase. J. Biol. Chem. 273: 5916-5922.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5916-5922
    • Schwandner, R.1    Wiegmann, K.2    Bernardo, K.3    Kreder, D.4    Kronke, M.5
  • 147
    • 0015880897 scopus 로고
    • The morphology of various types of cell deaths in prenatal tissues
    • Schweichel JU, Merker HJ. 1973. The morphology of various types of cell deaths in prenatal tissues. Teratology 7: 253-266.
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 148
    • 0035437610 scopus 로고    scopus 로고
    • Aminolevulinic acid-based photochemical internalization of the immunotoxin MOC31-gelonin generates synergistic cytotoxic effects in vitro
    • Selbo PK, Kaalhus O, Sivam G, Berg K. 2001. Aminolevulinic acid-based photochemical internalization of the immunotoxin MOC31-gelonin generates synergistic cytotoxic effects in vitro. Photochem. Photobiol. 74: 303-310.
    • (2001) Photochem. Photobiol. , vol.74 , pp. 303-310
    • Selbo, P.K.1    Kaalhus, O.2    Sivam, G.3    Berg, K.4
  • 149
    • 18444380859 scopus 로고    scopus 로고
    • Photochemical internalisation: A novel drug delivery system
    • Selbo PK, Hogset A, Prasmickaite L, Berg K. 2002. Photochemical internalisation: a novel drug delivery system. Tumour Biol. 23: 103-112.
    • (2002) Tumour Biol. , vol.23 , pp. 103-112
    • Selbo, P.K.1    Hogset, A.2    Prasmickaite, L.3    Berg, K.4
  • 150
    • 0037304032 scopus 로고    scopus 로고
    • Cancer and phase II drug-metabolizing enzymes
    • Sheweita SA, Tilmisany AK. 2002. Cancer and phase II drug-metabolizing enzymes. Curr. Drug Metab. 4: 45-58.
    • (2002) Curr. Drug Metab. , vol.4 , pp. 45-58
    • Sheweita, S.A.1    Tilmisany, A.K.2
  • 151
    • 0035835824 scopus 로고    scopus 로고
    • PTEN: Life as a tumor suppressor
    • Simpson L, Parsons R. 2001. PTEN: life as a tumor suppressor. Exp. Cell Res. 264: 29-41.
    • (2001) Exp. Cell Res. , vol.264 , pp. 29-41
    • Simpson, L.1    Parsons, R.2
  • 152
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potential
    • Sloane BF, Dunn JR, Honn KV. 1981. Lysosomal cathepsin B: correlation with metastatic potential. Science 212: 1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 154
    • 0034615555 scopus 로고    scopus 로고
    • Caspases - Controlling intracellular signals by protease zymogen activation
    • Stennicke HR, Salvesen GS. 2000. Caspases - controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477: 299-306.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 155
    • 0033523774 scopus 로고    scopus 로고
    • Regulated secretion from hemopoietic cells
    • Stinchcombe JC, Griffiths GM. 1999. Regulated secretion from hemopoietic cells. J. Cell Biol. 147: 1-6.
    • (1999) J. Cell Biol. , vol.147 , pp. 1-6
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 158
    • 0032516641 scopus 로고    scopus 로고
    • Cathepsin D in tissue and serum of patients with squamous cell carcinoma of the head and neck
    • Strojan P, Budihna M, Smid L, Vrhovec I, Skrk J. 1998. Cathepsin D in tissue and serum of patients with squamous cell carcinoma of the head and neck. Cancer Lett. 130: 49-56.
    • (1998) Cancer Lett. , vol.130 , pp. 49-56
    • Strojan, P.1    Budihna, M.2    Smid, L.3    Vrhovec, I.4    Skrk, J.5
  • 159
    • 0344407444 scopus 로고    scopus 로고
    • Induction of intensive tumor suppression by antiangiogenic photodynamic therapy using polycation-modified liposomal photosensitizer
    • Takeuchi Y, Kurohane K, Ichikawa K, Yonezawa S, Nango M, Oku N. 2003. Induction of intensive tumor suppression by antiangiogenic photodynamic therapy using polycation-modified liposomal photosensitizer. Cancer 97: 2027-2034.
    • (2003) Cancer , vol.97 , pp. 2027-2034
    • Takeuchi, Y.1    Kurohane, K.2    Ichikawa, K.3    Yonezawa, S.4    Nango, M.5    Oku, N.6
  • 160
    • 0033556443 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: Differential involvement of focal adhesion kinase and p130Cas
    • Tamura M, Gu J, Takino T, Yamada KM. 1999. Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas. Cancer Res. 59: 442-449.
    • (1999) Cancer Res. , vol.59 , pp. 442-449
    • Tamura, M.1    Gu, J.2    Takino, T.3    Yamada, K.M.4
  • 161
    • 0035650552 scopus 로고    scopus 로고
    • Multiple lysosomal trafficking phenotypes in metastatic mouse mammary tumor cell lines
    • Tao K, Li J, Warner J, MacLeod K, Miller FR, Sahagian GG. 2001. Multiple lysosomal trafficking phenotypes in metastatic mouse mammary tumor cell lines. Int. J. Oncol. 19: 1333-1339.
    • (2001) Int. J. Oncol. , vol.19 , pp. 1333-1339
    • Tao, K.1    Li, J.2    Warner, J.3    Macleod, K.4    Miller, F.R.5    Sahagian, G.G.6
  • 162
    • 0037093887 scopus 로고    scopus 로고
    • 2+-dependent tyrosine phosphorylation and microtubules
    • 2+-dependent tyrosine phosphorylation and microtubules. J. Immunol. 168: 5287-5296.
    • (2002) J. Immunol. , vol.168 , pp. 5287-5296
    • Tapper, H.1    Furuya, W.2    Grinstein, S.3
  • 163
    • 0023024265 scopus 로고
    • Comparative studies on protein turnover regulations in tumor cells and host tissues: Development and analysis of an experimental model
    • Tessitore L, Bonelli G, Isidoro C, Kazakova O, Baccino FM. 1986. Comparative studies on protein turnover regulations in tumor cells and host tissues: development and analysis of an experimental model. Toxicol. Pathol. 14: 451-456.
    • (1986) Toxicol. Pathol. , vol.14 , pp. 451-456
    • Tessitore, L.1    Bonelli, G.2    Isidoro, C.3    Kazakova, O.4    Baccino, F.M.5
  • 164
    • 0023355738 scopus 로고
    • Regulation of protein turnover versus growth state: Ascites hepatoma as a model for studies both in the animal and in vitro
    • Tessitore L, Bonelli G, Cecchini G, Amenta LS, Baccino FM. 1987. Regulation of protein turnover versus growth state: ascites hepatoma as a model for studies both in the animal and in vitro. Arch. Biochem. Biophys. 255: 372-384.
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 372-384
    • Tessitore, L.1    Bonelli, G.2    Cecchini, G.3    Amenta, L.S.4    Baccino, F.M.5
  • 166
    • 0030707562 scopus 로고    scopus 로고
    • TOR signalling and control of cell growth
    • Thomas G, Hall MN. 1997. TOR signalling and control of cell growth. Curr. Opin. Cell Biol. 9: 782-787.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 782-787
    • Thomas, G.1    Hall, M.N.2
  • 170
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B, Alessi DR. 2000. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346(Pt 3): 561-576.
    • (2000) Biochem. J. , vol.346 , Issue.3 PT , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 171
    • 0029782318 scopus 로고    scopus 로고
    • Receptor-mediated uptake of low-density lipoprotein by B16 melanoma cells in vitro and in vivo in mice
    • Versluis AJ, van Geel PJ, Oppelaar H, van Berkel TJ, Bijsterbosch MK. 1996. Receptor-mediated uptake of low-density lipoprotein by B16 melanoma cells in vitro and in vivo in mice. Br. J. Cancer 74: 525-532.
    • (1996) Br. J. Cancer , vol.74 , pp. 525-532
    • Versluis, A.J.1    Van Geel, P.J.2    Oppelaar, H.3    Van Berkel, T.J.4    Bijsterbosch, M.K.5
  • 172
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant H. 2002. The Fas signaling pathway: more than a paradigm. Science 296: 1635-1636.
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 174
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann K, Schutze S, Machleidt T, Witte D, Kronke M. 1994. Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling. Cell 78: 1005-1015.
    • (1994) Cell , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    Machleidt, T.3    Witte, D.4    Kronke, M.5
  • 175
    • 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. 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
  • 177
    • 0032870475 scopus 로고    scopus 로고
    • Autophagy is activated by apoptotic signalling in sympathetic neurons: An alternative mechanism of death execution
    • Xue L, Fletcher GC, Tolkovsky AM. 1999. Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution. Mol. Cell Neurosci. 14: 180-198.
    • (1999) Mol. Cell Neurosci. , vol.14 , pp. 180-198
    • Xue, L.1    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 178
    • 0034921007 scopus 로고    scopus 로고
    • Tumor suppressor PTEN: Modulator of cell signaling, growth, migration and apoptosis
    • Yamada KM, Araki M. 2001. Tumor suppressor PTEN: modulator of cell signaling, growth, migration and apoptosis. J. Cell Sci. 114: 2375-2382.
    • (2001) J. Cell Sci. , vol.114 , pp. 2375-2382
    • Yamada, K.M.1    Araki, M.2
  • 179
    • 0029011918 scopus 로고
    • Progression of subcellular changes during chemical hypoxia to cultured rat hepatocytes: A laser scanning confocal microscopic study
    • Zahrebelski G, Nieminen AL, al-Ghoul K, Qian T, Herman B, Lemasters JJ. 1995. Progression of subcellular changes during chemical hypoxia to cultured rat hepatocytes: a laser scanning confocal microscopic study. Hepatology 21: 1361-1372.
    • (1995) Hepatology , vol.21 , pp. 1361-1372
    • Zahrebelski, G.1    Nieminen, A.L.2    Al-Ghoul, K.3    Qian, T.4    Herman, B.5    Lemasters, J.J.6
  • 181
    • 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, Kang JX. 2001. Evidence of a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukemia HL-60 cells. Cell Death Diff. 8: 477-485.
    • (2001) Cell Death Diff. , vol.8 , pp. 477-485
    • Zang, Y.1    Beard, R.L.2    Chandraratna, R.A.3    Kang, J.X.4


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