메뉴 건너뛰기




Volumn 11, Issue 3, 2009, Pages 481-496

Oxidative stress and autophagy in the regulation of lysosome-dependent neuron death

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CATHEPSIN D; CHLOROQUINE; FREE RADICAL; IRON; LIPOFUSCIN; REACTIVE OXYGEN METABOLITE;

EID: 58849163098     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2008.2263     Document Type: Review
Times cited : (106)

References (174)
  • 1
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi V and Chinopoulos C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol Sci 27: 639-645, 2006.
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 2
    • 0034721509 scopus 로고    scopus 로고
    • Up-regulation of the lysosomal system in experimental models of neuronal injury: Implications for Alzheimer's disease
    • Adamec E, Mohan PS, Cataldo AM, Vonsattel JP, and Nixon RA. Up-regulation of the lysosomal system in experimental models of neuronal injury: implications for Alzheimer's disease. Neuroscience 100: 663-675, 2000.
    • (2000) Neuroscience , vol.100 , pp. 663-675
    • Adamec, E.1    Mohan, P.S.2    Cataldo, A.M.3    Vonsattel, J.P.4    Nixon, R.A.5
  • 3
    • 0028886612 scopus 로고
    • Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron
    • Amano T, Nakanishi H, Kondo T, Tanaka T, Oka M, and Yamamoto K. Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron. Mech Ageing Dev 83: 133-141, 1995.
    • (1995) Mech Ageing Dev , vol.83 , pp. 133-141
    • Amano, T.1    Nakanishi, H.2    Kondo, T.3    Tanaka, T.4    Oka, M.5    Yamamoto, K.6
  • 4
    • 0028326741 scopus 로고
    • Chloroquine accumulation and alterations of proteolysis and pinocytosis in the rat conceptus in vitro
    • Ambroso JL and Harris C. Chloroquine accumulation and alterations of proteolysis and pinocytosis in the rat conceptus in vitro. Biochem Pharmacol 47: 679-688, 1994.
    • (1994) Biochem Pharmacol , vol.47 , pp. 679-688
    • Ambroso, J.L.1    Harris, C.2
  • 7
    • 32944481457 scopus 로고    scopus 로고
    • Metallothionein protects against oxidative stress-induced lysosomal destabilization
    • Baird SK, Kurz T, and Brunk UT. Metallothionein protects against oxidative stress-induced lysosomal destabilization. Biochem J 394: 275-283, 2006.
    • (2006) Biochem J , vol.394 , pp. 275-283
    • Baird, S.K.1    Kurz, T.2    Brunk, U.T.3
  • 8
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, and Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77: 817-827, 1994.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 9
    • 0037989761 scopus 로고    scopus 로고
    • Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis: An approach for slowing Alzheimer disease?
    • Bendiske J and Bahr BA. Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis: an approach for slowing Alzheimer disease? J Neuropathol Exp Neurol 62: 451-463, 2003.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 451-463
    • Bendiske, J.1    Bahr, B.A.2
  • 10
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: Selective autophagy of the endoplasmic reticulum
    • Bernales S, Schuck S, and Walter P. ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3: 285-287, 2007.
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 11
    • 0020576115 scopus 로고
    • Effects of chloroquine on lysosomal enzymes, NADPH-induced lipid peroxidation, and antioxidant enzymes of rat retina
    • Bhattacharyya B, Chatterjee TK, and Ghosh JJ. Effects of chloroquine on lysosomal enzymes, NADPH-induced lipid peroxidation, and antioxidant enzymes of rat retina. Biochem Pharmacol 32: 2965-2968, 1983.
    • (1983) Biochem Pharmacol , vol.32 , pp. 2965-2968
    • Bhattacharyya, B.1    Chatterjee, T.K.2    Ghosh, J.J.3
  • 12
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N, Lorenzo HK, Carmona S, Laforge M, Harper F, Dumont C, and Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 278: 31401-31411, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 13
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman EJ, Siebers A, and Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci U S A 85: 7972-7976, 1988.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 14
    • 0038677510 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine
    • Boya P, Gonzalez-Polo RA, Poncet D, Andreau K, Vieira HL, Roumier T, Perfettini JL, and Kroemer G. Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine. Oncogene 22: 3927-3936, 2003.
    • (2003) Oncogene , vol.22 , pp. 3927-3936
    • Boya, P.1    Gonzalez-Polo, R.A.2    Poncet, D.3    Andreau, K.4    Vieira, H.L.5    Roumier, T.6    Perfettini, J.L.7    Kroemer, G.8
  • 15
    • 0014878377 scopus 로고
    • Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver
    • Brun A and Brunk U. Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver. J Histochem Cytochem 18: 820-827, 1970.
    • (1970) J Histochem Cytochem , vol.18 , pp. 820-827
    • Brun, A.1    Brunk, U.2
  • 16
    • 0026663037 scopus 로고
    • A novel hypothesis of lipofuscinogenesis and cellular aging based on interactions between oxidative stress and autophagocytosis
    • Brunk UT, Jones CB, and Sohal RS. A novel hypothesis of lipofuscinogenesis and cellular aging based on interactions between oxidative stress and autophagocytosis. Mutat Res 275: 395-403, 1992.
    • (1992) Mutat Res , vol.275 , pp. 395-403
    • Brunk, U.T.1    Jones, C.B.2    Sohal, R.S.3
  • 17
    • 0036710928 scopus 로고    scopus 로고
    • Lipofuscin: Mechanisms of age-related accumulation and influence on cell function
    • Brunk UT and Terman A. Lipofuscin: mechanisms of age-related accumulation and influence on cell function. Free Radic Biol Med 33: 611-619, 2002.
    • (2002) Free Radic Biol Med , vol.33 , pp. 611-619
    • Brunk, U.T.1    Terman, A.2
  • 19
    • 14844310312 scopus 로고    scopus 로고
    • Role of the autophagic-lysosomal system on low potassium-induced apoptosis in cultured cerebellar granule cells
    • Canu N, Tufi R, Serafino AL, Amadoro G, Ciotti MT, and Calissano P. Role of the autophagic-lysosomal system on low potassium-induced apoptosis in cultured cerebellar granule cells. J Neurochem 92: 1228-1242, 2005.
    • (2005) J Neurochem , vol.92 , pp. 1228-1242
    • Canu, N.1    Tufi, R.2    Serafino, A.L.3    Amadoro, G.4    Ciotti, M.T.5    Calissano, P.6
  • 22
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, and Nixon RA. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system. Neuron 14: 671-680, 1995.
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 23
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased beta-amyloidogenesis
    • Cataldo AM, Barnett JL, Pieroni C, and Nixon RA. Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J Neurosci 17: 6142-6151, 1997.
    • (1997) J Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 24
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, and Nixon RA. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J Neurosci 16: 186-199, 1996.
    • (1996) J Neurosci , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 25
    • 0028220243 scopus 로고
    • Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease
    • Cataldo AM, Hamilton DJ, and Nixon RA. Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease. Brain Res 640: 68-80, 1994.
    • (1994) Brain Res , vol.640 , pp. 68-80
    • Cataldo, A.M.1    Hamilton, D.J.2    Nixon, R.A.3
  • 26
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo AM and Nixon RA. Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc Natl Acad Sci U S A 87: 3861-3865, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 27
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
    • Cataldo AM, Paskevich PA, Kominami E, and Nixon RA. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proc Natl Acad Sci U S A 88: 10998-11002, 1991.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 28
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo AM, Peterhoff CM, Troncoso JC, Gomez-Isla T, Hyman BT, and Nixon RA. Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am J Pathol 157: 277-286, 2000.
    • (2000) Am J Pathol , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 29
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: Evidence for a neuronal origin
    • Cataldo AM, Thayer CY, Bird ED, Wheelock TR, and Nixon RA. Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res 513: 181-192, 1990.
    • (1990) Brain Res , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5
  • 30
    • 0029165212 scopus 로고
    • Inhibition of adenine nucleotide translocator by lipid peroxidation products
    • Chen JJ, Bertrand H, and Yu BP. Inhibition of adenine nucleotide translocator by lipid peroxidation products. Free Radic Biol Med 19: 583-590, 1995.
    • (1995) Free Radic Biol Med , vol.19 , pp. 583-590
    • Chen, J.J.1    Bertrand, H.2    Yu, B.P.3
  • 32
    • 0035890214 scopus 로고    scopus 로고
    • Zinc resistance impairs sensitivity to oxidative stress in HeLa cells: Protection through metallothioneins expression
    • Chimienti F, Jourdan E, Favier A, and Seve M. Zinc resistance impairs sensitivity to oxidative stress in HeLa cells: protection through metallothioneins expression. Free Radic Biol Med 31: 1179-1190, 2001.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1179-1190
    • Chimienti, F.1    Jourdan, E.2    Favier, A.3    Seve, M.4
  • 33
    • 34548598647 scopus 로고    scopus 로고
    • Zaprinast inhibits hydrogen peroxide-induced lysosomal destabilization and cell death in astrocytes
    • Choi JH, Kim DH, Yun IJ, Chang JH, Chun BG, and Choi SH. Zaprinast inhibits hydrogen peroxide-induced lysosomal destabilization and cell death in astrocytes. Eur J Pharmacol 571: 106-115, 2007.
    • (2007) Eur J Pharmacol , vol.571 , pp. 106-115
    • Choi, J.H.1    Kim, D.H.2    Yun, I.J.3    Chang, J.H.4    Chun, B.G.5    Choi, S.H.6
  • 34
    • 0031785364 scopus 로고    scopus 로고
    • Effect of chloroquine and leupeptin on intracellular accumulation of amyloid-beta (A beta) 1-42 peptide in a murine N9 microglial cell line
    • Chu T, Tran T, Yang F, Beech W, Cole GM, and Frautschy SA. Effect of chloroquine and leupeptin on intracellular accumulation of amyloid-beta (A beta) 1-42 peptide in a murine N9 microglial cell line. FEBS Lett 436: 439-444, 1998.
    • (1998) FEBS Lett , vol.436 , pp. 439-444
    • Chu, T.1    Tran, T.2    Yang, F.3    Beech, W.4    Cole, G.M.5    Frautschy, S.A.6
  • 35
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • Cirman T, Oresic K, Mazovec GD, Turk V, Reed JC, Myers RM, Salvesen GS, and Turk B. Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J Biol Chem 279: 3578-3587, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresic, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6    Salvesen, G.S.7    Turk, B.8
  • 36
    • 0029986692 scopus 로고    scopus 로고
    • Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: Immunochemical detection in mitochondria exposed to oxidative stress
    • Cohn JA, Tsai L, Friguet B, and Szweda LI. Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: immunochemical detection in mitochondria exposed to oxidative stress. Arch Biochem Biophys 328: 158-164, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 158-164
    • Cohn, J.A.1    Tsai, L.2    Friguet, B.3    Szweda, L.I.4
  • 37
    • 0018873419 scopus 로고
    • Phagocytosis and degradation of rat liver mitochondria by cultivated human glial cells
    • Collins VP, Arborgh B, Brunk U, and Schellens JP. Phagocytosis and degradation of rat liver mitochondria by cultivated human glial cells. Lab Invest 42: 209-216, 1980.
    • (1980) Lab Invest , vol.42 , pp. 209-216
    • Collins, V.P.1    Arborgh, B.2    Brunk, U.3    Schellens, J.P.4
  • 38
    • 0035877037 scopus 로고    scopus 로고
    • Methylmercury and H(2)O(2) provoke lysosomal damage in human astrocytoma D384 cells followed by apoptosis
    • Dare E, Li W, Zhivotovsky B, Yuan X, and Ceccatelli S. Methylmercury and H(2)O(2) provoke lysosomal damage in human astrocytoma D384 cells followed by apoptosis. Free Radic Biol Med 30: 1347-1356, 2001.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1347-1356
    • Dare, E.1    Li, W.2    Zhivotovsky, B.3    Yuan, X.4    Ceccatelli, S.5
  • 40
    • 0021040946 scopus 로고
    • Lysosomes revisited
    • de Duve C. Lysosomes revisited. Eur J Biochem 137: 391-397, 1983.
    • (1983) Eur J Biochem , vol.137 , pp. 391-397
    • de Duve, C.1
  • 41
    • 26944475263 scopus 로고    scopus 로고
    • The lysosome turns fifty
    • de Duve C. The lysosome turns fifty. Nat Cell Biol 7: 847-849, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 847-849
    • de Duve, C.1
  • 43
    • 0021890911 scopus 로고
    • Responses of cultured cardiac myocytes to lysosomotropic compounds and methylated amino acids
    • Decker RS, Decker ML, Thomas V, and Fuseler JW. Responses of cultured cardiac myocytes to lysosomotropic compounds and methylated amino acids. J Cell Sci 74: 119-135, 1985.
    • (1985) J Cell Sci , vol.74 , pp. 119-135
    • Decker, R.S.1    Decker, M.L.2    Thomas, V.3    Fuseler, J.W.4
  • 44
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A, Mina E, Glabe C, and Busciglio J. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J Neurosci 26: 6011-6018, 2006.
    • (2006) J Neurosci , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 45
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice JF. Chaperone-mediated autophagy. Autophagy 3: 295-299, 2007.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 46
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease
    • Ditaranto K, Tekirian TL, and Yang AJ. Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease. Neurobiol Dis 8: 19-31, 2001.
    • (2001) Neurobiol Dis , vol.8 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 47
    • 0030951610 scopus 로고    scopus 로고
    • Follow-up study of subunit c of mitochondrial ATP synthase (SCMAS) in Batten disease and in unrelated lysosomal disorders
    • Elleder M, Sokolova J, and Hrebicek M. Follow-up study of subunit c of mitochondrial ATP synthase (SCMAS) in Batten disease and in unrelated lysosomal disorders. Acta Neuropathol 93: 379-390, 1997.
    • (1997) Acta Neuropathol , vol.93 , pp. 379-390
    • Elleder, M.1    Sokolova, J.2    Hrebicek, M.3
  • 49
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • Eskelinen EL, Tanaka Y, and Saftig P. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol 13: 137-145, 2003.
    • (2003) Trends Cell Biol , vol.13 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 50
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11: 81-128, 1991.
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 51
    • 1142297431 scopus 로고    scopus 로고
    • Fitch CD. Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs. Life Sci 74: 1957-1972, 2004.
    • Fitch CD. Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs. Life Sci 74: 1957-1972, 2004.
  • 52
    • 0036751954 scopus 로고    scopus 로고
    • Oxidative stress in brain aging: Implications for therapeutics of neurodegenerative diseases
    • Floyd RA and Hensley K. Oxidative stress in brain aging: implications for therapeutics of neurodegenerative diseases. Neurobiol Aging 23: 795-807, 2002.
    • (2002) Neurobiol Aging , vol.23 , pp. 795-807
    • Floyd, R.A.1    Hensley, K.2
  • 53
    • 0018630560 scopus 로고
    • Proteases in cellular slime mold development: Evidence for their involvement
    • Fong D and Bonner JT. Proteases in cellular slime mold development: evidence for their involvement. Proc Natl Acad Sci U S A 76: 6481-6485, 1979.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 6481-6485
    • Fong, D.1    Bonner, J.T.2
  • 54
    • 0027990369 scopus 로고
    • Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal: Formation of cross-linked protein that inhibits the multicatalytic protease
    • Friguet B, Stadtman ER, and Szweda LI. Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal: formation of cross-linked protein that inhibits the multicatalytic protease. J Biol Chem 269: 21639-21643, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 21639-21643
    • Friguet, B.1    Stadtman, E.R.2    Szweda, L.I.3
  • 55
    • 0028340636 scopus 로고
    • Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease
    • Friguet B, Szweda LI, and Stadtman ER. Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease. Arch Biochem Biophys 311: 168-173, 1994.
    • (1994) Arch Biochem Biophys , vol.311 , pp. 168-173
    • Friguet, B.1    Szweda, L.I.2    Stadtman, E.R.3
  • 56
    • 1042265181 scopus 로고    scopus 로고
    • Current state of clinical and morphological features in human NCL
    • Goebel HH and Wisniewski KE. Current state of clinical and morphological features in human NCL. Brain Pathol 14: 61-69, 2004.
    • (2004) Brain Pathol , vol.14 , pp. 61-69
    • Goebel, H.H.1    Wisniewski, K.E.2
  • 57
    • 27644585945 scopus 로고    scopus 로고
    • Redundant cell death mechanisms as relics and backups
    • Golstein P and Kroemer G. Redundant cell death mechanisms as relics and backups. Cell Death Differ 12(suppl 2): 1490-1496, 2005.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1490-1496
    • Golstein, P.1    Kroemer, G.2
  • 58
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling
    • Gonzalez-Noriega A, Grubb JH, Talkad V, and Sly WS. Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling. J Cell Biol 85: 839-852, 1980.
    • (1980) J Cell Biol , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 59
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • Gordon PB and Seglen PO. Prelysosomal convergence of autophagic and endocytic pathways. Biochem Biophys Res Commun 151: 40-47, 1988.
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 62
    • 41149085729 scopus 로고    scopus 로고
    • Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
    • Hamano T, Gendron TF, Causevic E, Yen SH, Lin WL, Isidoro C, Deture M, and Ko LW. Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Eur J Neurosci 27: 1119-1130, 2008.
    • (2008) Eur J Neurosci , vol.27 , pp. 1119-1130
    • Hamano, T.1    Gendron, T.F.2    Causevic, E.3    Yen, S.H.4    Lin, W.L.5    Isidoro, C.6    Deture, M.7    Ko, L.W.8
  • 63
    • 0025074187 scopus 로고
    • Lipofuscin and ceroid formation: The cellular recycling system
    • Harman D. Lipofuscin and ceroid formation: the cellular recycling system. Adv Exp Med Biol 266: 3-15, 1989.
    • (1989) Adv Exp Med Biol , vol.266 , pp. 3-15
    • Harman, D.1
  • 65
    • 0028060607 scopus 로고
    • Inactivation of lysosomal proteases by oxidized low density lipoprotein is partially responsible for its poor degradation by mouse peritoneal macrophages
    • Hoppe G, O'Neil J, and Hoff HF. Inactivation of lysosomal proteases by oxidized low density lipoprotein is partially responsible for its poor degradation by mouse peritoneal macrophages. J Clin Invest 94: 1506-1512, 1994.
    • (1994) J Clin Invest , vol.94 , pp. 1506-1512
    • Hoppe, G.1    O'Neil, J.2    Hoff, H.F.3
  • 67
    • 41149133254 scopus 로고    scopus 로고
    • Zinc and 4-hydroxy-2-nonenal mediate lysosomal membrane permeabilization induced by H2O2 in cultured hippocampal neurons
    • Hwang JJ, Lee SJ, Kim TY, Cho JH, and Koh JY. Zinc and 4-hydroxy-2-nonenal mediate lysosomal membrane permeabilization induced by H2O2 in cultured hippocampal neurons. J Neurosci 28: 3114-3122, 2008.
    • (2008) J Neurosci , vol.28 , pp. 3114-3122
    • Hwang, J.J.1    Lee, S.J.2    Kim, T.Y.3    Cho, J.H.4    Koh, J.Y.5
  • 68
    • 0024400733 scopus 로고
    • A study of the mechanisms of chloroquine retinopathy, I: Chloroquine effect on lipid peroxidation of retina
    • Ivanina TA, Sakina NL, Lebedeva MN, and Borovyagin VL. A study of the mechanisms of chloroquine retinopathy, I: chloroquine effect on lipid peroxidation of retina. Ophthalmic Res 21: 216-220, 1989.
    • (1989) Ophthalmic Res , vol.21 , pp. 216-220
    • Ivanina, T.A.1    Sakina, N.L.2    Lebedeva, M.N.3    Borovyagin, V.L.4
  • 69
    • 0025032215 scopus 로고
    • Lipofuscin-like substances accumulate rapidly in brain, retina and internal organs with cysteine protease inhibition
    • Ivy GO, Kanai S, Ohta M, Smith G, Sato Y, Kobayashi M, and Kitani K. Lipofuscin-like substances accumulate rapidly in brain, retina and internal organs with cysteine protease inhibition. Adv Exp Med Biol 266: 31-45, 1989.
    • (1989) Adv Exp Med Biol , vol.266 , pp. 31-45
    • Ivy, G.O.1    Kanai, S.2    Ohta, M.3    Smith, G.4    Sato, Y.5    Kobayashi, M.6    Kitani, K.7
  • 70
    • 0021675999 scopus 로고
    • Inhibitors of lysosomal enzymes: Accumulation of lipofuscinlike dense bodies in the brain
    • Ivy GO, Schottler F, Wenzel J, Baudry M, and Lynch G. Inhibitors of lysosomal enzymes: accumulation of lipofuscinlike dense bodies in the brain. Science 226: 985-987, 1984.
    • (1984) Science , vol.226 , pp. 985-987
    • Ivy, G.O.1    Schottler, F.2    Wenzel, J.3    Baudry, M.4    Lynch, G.5
  • 71
    • 0029033619 scopus 로고
    • Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and activation of phospholipase A2 in breast carcinoma cells
    • Jaattela M, Benedict M, Tewari M, Shayman JA, and Dixit VM. Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and activation of phospholipase A2 in breast carcinoma cells. Oncogene 10: 2297-2305, 1995.
    • (1995) Oncogene , vol.10 , pp. 2297-2305
    • Jaattela, M.1    Benedict, M.2    Tewari, M.3    Shayman, J.A.4    Dixit, V.M.5
  • 73
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kagedal K, Johansson U, and Ollinger K. The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J 15: 1592-1594, 2001.
    • (2001) FASEB J , vol.15 , pp. 1592-1594
    • Kagedal, K.1    Johansson, U.2    Ollinger, K.3
  • 74
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K, Zhao M, Svensson I, and Brunk UT. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem J 359: 335-343, 2001.
    • (2001) Biochem J , vol.359 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 80
    • 33745205646 scopus 로고    scopus 로고
    • Intralysosomal iron chelation protects against oxidative stress-induced cellular damage
    • Kurz T, Gustafsson B, and Brunk UT. Intralysosomal iron chelation protects against oxidative stress-induced cellular damage. FEBS J 273: 3106-3117, 2006.
    • (2006) FEBS J , vol.273 , pp. 3106-3117
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 81
    • 34249815482 scopus 로고    scopus 로고
    • Autophagy, ageing and apoptosis: The role of oxidative stress and lysosomal iron
    • Kurz T, Terman A, and Brunk UT. Autophagy, ageing and apoptosis: the role of oxidative stress and lysosomal iron. Arch Biochem Biophys 462: 220-230, 2007.
    • (2007) Arch Biochem Biophys , vol.462 , pp. 220-230
    • Kurz, T.1    Terman, A.2    Brunk, U.T.3
  • 82
    • 1642576976 scopus 로고    scopus 로고
    • Examination of the mechanism(s) involved in doxorubicin-mediated iron accumulation in ferritin: Studies using metabolic inhibitors, protein synthesis inhibitors, and lysosomotropic agents
    • Kwok JC and Richardson DR. Examination of the mechanism(s) involved in doxorubicin-mediated iron accumulation in ferritin: studies using metabolic inhibitors, protein synthesis inhibitors, and lysosomotropic agents. Mol Pharmacol 65: 181-195, 2004.
    • (2004) Mol Pharmacol , vol.65 , pp. 181-195
    • Kwok, J.C.1    Richardson, D.R.2
  • 83
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94: 491-501, 1998.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 85
    • 0031031041 scopus 로고    scopus 로고
    • The autophagic and endocytic pathways converge at the nascent autophagic vacuoles
    • Liou W, Geuze HJ, Geelen MJ, and Slot JW. The autophagic and endocytic pathways converge at the nascent autophagic vacuoles. J Cell Biol 136: 61-70, 1997.
    • (1997) J Cell Biol , vol.136 , pp. 61-70
    • Liou, W.1    Geuze, H.J.2    Geelen, M.J.3    Slot, J.W.4
  • 87
    • 0142116349 scopus 로고    scopus 로고
    • Lysosomes and brain aging in mammals
    • Lynch G and Bi X. Lysosomes and brain aging in mammals. Neurochem Res 28: 1725-1734, 2003.
    • (2003) Neurochem Res , vol.28 , pp. 1725-1734
    • Lynch, G.1    Bi, X.2
  • 88
    • 0023432307 scopus 로고
    • Association of the precursor of cathepsin D with coated membranes: Kinetics and carbohydrate processing
    • Marquardt T, Braulke T, Hasilik A, and von Figura K. Association of the precursor of cathepsin D with coated membranes: kinetics and carbohydrate processing. Eur J Biochem 168: 37-42, 1987.
    • (1987) Eur J Biochem , vol.168 , pp. 37-42
    • Marquardt, T.1    Braulke, T.2    Hasilik, A.3    von Figura, K.4
  • 90
    • 0030943654 scopus 로고    scopus 로고
    • Chloroquine administration in mice increases beta-amyloid immunoreactivity and attenuates kainate-induced blood-brain barrier dysfunction
    • Mielke JG, Murphy MP, Maritz J, Bengualid KM, and Ivy GO. Chloroquine administration in mice increases beta-amyloid immunoreactivity and attenuates kainate-induced blood-brain barrier dysfunction. Neurosci Lett 227: 169-172, 1997.
    • (1997) Neurosci Lett , vol.227 , pp. 169-172
    • Mielke, J.G.1    Murphy, M.P.2    Maritz, J.3    Bengualid, K.M.4    Ivy, G.O.5
  • 91
    • 1042299968 scopus 로고    scopus 로고
    • The genetic spectrum of human neuronal ceroid-lipofuscinoses
    • Mole SE. The genetic spectrum of human neuronal ceroid-lipofuscinoses. Brain Pathol 14: 70-76, 2004.
    • (2004) Brain Pathol , vol.14 , pp. 70-76
    • Mole, S.E.1
  • 96
    • 0025826050 scopus 로고
    • Lysosomal storage diseases
    • Neufeld EF. Lysosomal storage diseases. Annu Rev Biochem 60: 257-280, 1991.
    • (1991) Annu Rev Biochem , vol.60 , pp. 257-280
    • Neufeld, E.F.1
  • 97
    • 0020409544 scopus 로고
    • Effect of chloroquine on the stability of rat kidney lysosomes in vivo and in vitro
    • Ngaha EO and Akanji MA. Effect of chloroquine on the stability of rat kidney lysosomes in vivo and in vitro. Comp Biochem Physiol C 73: 109-113, 1982.
    • (1982) Comp Biochem Physiol C , vol.73 , pp. 109-113
    • Ngaha, E.O.1    Akanji, M.A.2
  • 98
    • 33745821268 scopus 로고    scopus 로고
    • Cytosolic acidification and lysosomal alkalinization during TNF-alpha induced apoptosis in U937 cells
    • Nilsson C, Johansson U, Johansson AC, Kagedal K, and Ollinger K. Cytosolic acidification and lysosomal alkalinization during TNF-alpha induced apoptosis in U937 cells. Apoptosis 11: 1149-1159, 2006.
    • (2006) Apoptosis , vol.11 , pp. 1149-1159
    • Nilsson, C.1    Johansson, U.2    Johansson, A.C.3    Kagedal, K.4    Ollinger, K.5
  • 99
    • 17144421250 scopus 로고    scopus 로고
    • Analysis of cytosolic and lysosomal pH in apoptotic cells by flow cytometry
    • Nilsson C, Kagedal K, Johansson U, and Ollinger K. Analysis of cytosolic and lysosomal pH in apoptotic cells by flow cytometry. Methods Cell Sci 25: 185-194, 2003.
    • (2003) Methods Cell Sci , vol.25 , pp. 185-194
    • Nilsson, C.1    Kagedal, K.2    Johansson, U.3    Ollinger, K.4
  • 100
    • 0023890834 scopus 로고
    • Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes
    • Nishimura Y, Amano J, Sato H, Tsuji H, and Kato K. Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes. Arch Biochem Biophys 262: 159-170, 1988.
    • (1988) Arch Biochem Biophys , vol.262 , pp. 159-170
    • Nishimura, Y.1    Amano, J.2    Sato, H.3    Tsuji, H.4    Kato, K.5
  • 101
    • 0029055976 scopus 로고
    • Biosynthesis and processing of lysosomal cathepsin D in primary cultures of rat hepatocytes
    • Nishimura Y, Kato K, Furuno K, and Himeno M. Biosynthesis and processing of lysosomal cathepsin D in primary cultures of rat hepatocytes. Biol Pharm Bull 18: 825-828, 1995.
    • (1995) Biol Pharm Bull , vol.18 , pp. 825-828
    • Nishimura, Y.1    Kato, K.2    Furuno, K.3    Himeno, M.4
  • 102
    • 0034507918 scopus 로고    scopus 로고
    • A "protease activation cascade" in the pathogenesis of Alzheimer's disease
    • Nixon RA. A "protease activation cascade" in the pathogenesis of Alzheimer's disease. Ann N Y Acad Sci 924: 117-131, 2000.
    • (2000) Ann N Y Acad Sci , vol.924 , pp. 117-131
    • Nixon, R.A.1
  • 103
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • Nixon RA. Autophagy, amyloidogenesis and Alzheimer disease. J Cell Sci 120: 4081-4091, 2007.
    • (2007) J Cell Sci , vol.120 , pp. 4081-4091
    • Nixon, R.A.1
  • 105
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: A continuum from development to late age
    • Nixon RA, Yang DS, and Lee JH. Neurodegenerative lysosomal disorders: a continuum from development to late age. Autophagy 4: 590-599, 2008.
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 106
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S and Poole B. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci U S A 75: 3327-3331, 1978.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 107
    • 0019788761 scopus 로고
    • Cytoplasmic vacuolation of mouse peritoneal macrophages and the uptake into lysosomes of weakly basic substances
    • Ohkuma S and Poole B. Cytoplasmic vacuolation of mouse peritoneal macrophages and the uptake into lysosomes of weakly basic substances. J Cell Biol 90: 656-664, 1981.
    • (1981) J Cell Biol , vol.90 , pp. 656-664
    • Ohkuma, S.1    Poole, B.2
  • 109
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidative stress is mediated through lysosomal damage
    • Ollinger K and Brunk UT. Cellular injury induced by oxidative stress is mediated through lysosomal damage. Free Radic Biol Med 19: 565-574, 1995.
    • (1995) Free Radic Biol Med , vol.19 , pp. 565-574
    • Ollinger, K.1    Brunk, U.T.2
  • 110
    • 41749098046 scopus 로고    scopus 로고
    • Chloroquine-induced nitric oxide increase and cell death is dependent on cellular GSH depletion in A172 human glioblastoma cells
    • Park BC, Park SH, Paek SH, Park SY, Kwak MK, Choi HG, Yong CS, Yoo BK, and Kim JA. Chloroquine-induced nitric oxide increase and cell death is dependent on cellular GSH depletion in A172 human glioblastoma cells. Toxicol Lett 178: 52-60, 2008.
    • (2008) Toxicol Lett , vol.178 , pp. 52-60
    • Park, B.C.1    Park, S.H.2    Paek, S.H.3    Park, S.Y.4    Kwak, M.K.5    Choi, H.G.6    Yong, C.S.7    Yoo, B.K.8    Kim, J.A.9
  • 111
    • 0032533549 scopus 로고    scopus 로고
    • Radisky DC and Kaplan J. Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts. Biochem J 336: 201-205, 1998.
    • Radisky DC and Kaplan J. Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts. Biochem J 336: 201-205, 1998.
  • 112
    • 0031440533 scopus 로고    scopus 로고
    • Lysosomotropic agents ameliorate macrophage dysfunction following the phagocytosis of IgG-coated erythrocytes: A role for lipid peroxidation
    • Raley MJ, Schwacha MG, and Loegering DJ. Lysosomotropic agents ameliorate macrophage dysfunction following the phagocytosis of IgG-coated erythrocytes: a role for lipid peroxidation. Inflammation 21: 619-628, 1997.
    • (1997) Inflammation , vol.21 , pp. 619-628
    • Raley, M.J.1    Schwacha, M.G.2    Loegering, D.J.3
  • 113
    • 58849131749 scopus 로고    scopus 로고
    • History and morphology of the lysosome
    • edited by Saftig P. New York: Springer Science Business Media; Landes Bioscience
    • Rauch-Lüllmann Renate. History and morphology of the lysosome. In: Lysosomes, edited by Saftig P. New York: Springer Science Business Media; Landes Bioscience, 2005, pp. 1-16.
    • (2005) Lysosomes , pp. 1-16
    • Renate, R.-L.1
  • 114
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts
    • Roberg K, Kagedal K, and Ollinger K. Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. Am J Pathol 161: 89-96, 2002.
    • (2002) Am J Pathol , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Ollinger, K.3
  • 115
    • 0024238392 scopus 로고
    • Ferritin iron kinetics and protein turnover in K562 cells
    • Roberts S and Bomford A. Ferritin iron kinetics and protein turnover in K562 cells. J Biol Chem 263: 19181-19187, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 19181-19187
    • Roberts, S.1    Bomford, A.2
  • 116
    • 0034830488 scopus 로고    scopus 로고
    • Caspases, apoptosis, and Alzheimer disease: Causation, correlation, and confusion
    • Roth KA. Caspases, apoptosis, and Alzheimer disease: causation, correlation, and confusion. J Neuropathol Exp Neurol 60: 829-838, 2001.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 829-838
    • Roth, K.A.1
  • 117
    • 55749083590 scopus 로고    scopus 로고
    • Lysosomal Membrane Proteins
    • edited by Saftig P. New York: Springer Science Business Media
    • Saftig P. Lysosomal Membrane Proteins. In: Lysosomes, edited by Saftig P. New York: Springer Science Business Media, 2005, pp. 37-49.
    • (2005) Lysosomes , pp. 37-49
    • Saftig, P.1
  • 118
    • 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. 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.
    • (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
  • 119
    • 0029970783 scopus 로고    scopus 로고
    • Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D
    • Saftig P, Peters C, von Figura K, Craessaerts K, Van Leuven F, and De Strooper B. Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D. J Biol Chem 271: 27241-27244, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 27241-27244
    • Saftig, P.1    Peters, C.2    von Figura, K.3    Craessaerts, K.4    Van Leuven, F.5    De Strooper, B.6
  • 120
    • 0024678021 scopus 로고
    • Lysosomal movements during heterophagy and autophagy: With special reference to nematolysosome and wrapping lysosome
    • Sakai M, Araki N, and Ogawa K. Lysosomal movements during heterophagy and autophagy: with special reference to nematolysosome and wrapping lysosome. J Electron Microsc Tech 12: 101-131, 1989.
    • (1989) J Electron Microsc Tech , vol.12 , pp. 101-131
    • Sakai, M.1    Araki, N.2    Ogawa, K.3
  • 121
    • 0025238656 scopus 로고
    • Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress
    • Sakaida I, Kyle ME, and Farber JL. Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress. Mol Pharmacol 37: 435-442, 1990.
    • (1990) Mol Pharmacol , vol.37 , pp. 435-442
    • Sakaida, I.1    Kyle, M.E.2    Farber, J.L.3
  • 122
    • 0024845409 scopus 로고
    • Effects of cysteine protease inhibitors on rabbit cathepsin D maturation
    • Samarel AM, Ferguson AG, Decker RS, and Lesch M. Effects of cysteine protease inhibitors on rabbit cathepsin D maturation. Am J Physiol 257: C1069-C1079, 1989.
    • (1989) Am J Physiol , vol.257
    • Samarel, A.M.1    Ferguson, A.G.2    Decker, R.S.3    Lesch, M.4
  • 123
    • 33746874469 scopus 로고    scopus 로고
    • Ceramide is the key mediator of oxidative stress-induced apoptosis in retinal photoreceptor cells
    • Sanvicens N and Cotter TG. Ceramide is the key mediator of oxidative stress-induced apoptosis in retinal photoreceptor cells. J Neurochem 98: 1432-1444, 2006.
    • (2006) J Neurochem , vol.98 , pp. 1432-1444
    • Sanvicens, N.1    Cotter, T.G.2
  • 124
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, and Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26: 1749-1760, 2007.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 125
    • 3042658542 scopus 로고    scopus 로고
    • Brain iron deposition and the free radical-mitochondrial theory of ageing
    • Schipper HM. Brain iron deposition and the free radical-mitochondrial theory of ageing. Ageing Res Rev 3: 265-301, 2004.
    • (2004) Ageing Res Rev , vol.3 , pp. 265-301
    • Schipper, H.M.1
  • 126
    • 0019209783 scopus 로고
    • Effects of lysosomotropic monoamines, diamines, amino alcohols, and other amino compounds on protein degradation and protein synthesis in isolated rat hepatocytes
    • Seglen PO and Gordon PB. Effects of lysosomotropic monoamines, diamines, amino alcohols, and other amino compounds on protein degradation and protein synthesis in isolated rat hepatocytes. Mol Pharmacol 18: 468-475, 1980.
    • (1980) Mol Pharmacol , vol.18 , pp. 468-475
    • Seglen, P.O.1    Gordon, P.B.2
  • 128
    • 33745859721 scopus 로고    scopus 로고
    • Autophagy, bafilomycin and cell death: The "a-B-cs" of plecomacrolide-induced neuroprotection
    • Shacka JJ, Klocke BJ, and Roth KA. Autophagy, bafilomycin and cell death: the "a-B-cs" of plecomacrolide-induced neuroprotection. Autophagy 2: 228-230, 2006.
    • (2006) Autophagy , vol.2 , pp. 228-230
    • Shacka, J.J.1    Klocke, B.J.2    Roth, K.A.3
  • 131
    • 38449091923 scopus 로고    scopus 로고
    • The autophagy-lysosomal degradation pathway: Role in neurodegenerative disease and therapy
    • Shacka JJ, Roth KA, and Zhang J. The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy. Front Biosci 13: 718-736, 2008.
    • (2008) Front Biosci , vol.13 , pp. 718-736
    • Shacka, J.J.1    Roth, K.A.2    Zhang, J.3
  • 133
    • 0034766880 scopus 로고    scopus 로고
    • Inhibition of RPE lysosomal and antioxidant activity by the age pigment lipofuscin
    • Shamsi FA and Boulton M. Inhibition of RPE lysosomal and antioxidant activity by the age pigment lipofuscin. Invest Ophthalmol Vis Sci 42: 3041-3046, 2001.
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 3041-3046
    • Shamsi, F.A.1    Boulton, M.2
  • 136
    • 0025640126 scopus 로고
    • Age-related changes in antioxidant enzymes and prooxidant generation in tissues of the rat with special reference to parameters in two insect species
    • Sohal RS, Arnold LA, and Sohal BH. Age-related changes in antioxidant enzymes and prooxidant generation in tissues of the rat with special reference to parameters in two insect species. Free Radic Biol Med 9: 495-500, 1990.
    • (1990) Free Radic Biol Med , vol.9 , pp. 495-500
    • Sohal, R.S.1    Arnold, L.A.2    Sohal, B.H.3
  • 137
    • 0024537069 scopus 로고
    • Effect of ambient oxygen concentration on lipofuscin accumulation in cultured rat heart myocytes: A novel in vitro model of lipofuscinogenesis
    • Sohal RS, Marzabadi MR, Galaris D, and Brunk UT. Effect of ambient oxygen concentration on lipofuscin accumulation in cultured rat heart myocytes: a novel in vitro model of lipofuscinogenesis. Free Radic Biol Med 6: 23-30, 1989.
    • (1989) Free Radic Biol Med , vol.6 , pp. 23-30
    • Sohal, R.S.1    Marzabadi, M.R.2    Galaris, D.3    Brunk, U.T.4
  • 138
    • 0021038848 scopus 로고
    • Structural and physical changes in lysosomes from isolated rat hepatocytes treated with methylamine
    • Solheim AE and Seglen PO. Structural and physical changes in lysosomes from isolated rat hepatocytes treated with methylamine. Biochim Biophys Acta 763: 284-291, 1983.
    • (1983) Biochim Biophys Acta , vol.763 , pp. 284-291
    • Solheim, A.E.1    Seglen, P.O.2
  • 139
    • 0022336763 scopus 로고
    • Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide
    • Starke PE, Gilbertson JD, and Farber JL. Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide. Biochem Biophys Res Commun 133: 371-379, 1985.
    • (1985) Biochem Biophys Res Commun , vol.133 , pp. 371-379
    • Starke, P.E.1    Gilbertson, J.D.2    Farber, J.L.3
  • 142
    • 84924252717 scopus 로고    scopus 로고
    • Storch S and Braulke T. Transport of lysosomal enzymes. In Lysosomes, edited by Saftig P. New York: Springer Science+Business Media; Landes Bioscience, 2005, pp. 17-26.
    • Storch S and Braulke T. Transport of lysosomal enzymes. In Lysosomes, edited by Saftig P. New York: Springer Science+Business Media; Landes Bioscience, 2005, pp. 17-26.
  • 143
    • 0023272746 scopus 로고
    • A ferriprotoporphyrin IX-chloroquine complex promotes membrane phospholipid peroxidation: A possible mechanism for antimalarial action
    • Sugioka Y, Suzuki M, Sugioka K, and Nakano M. A ferriprotoporphyrin IX-chloroquine complex promotes membrane phospholipid peroxidation: a possible mechanism for antimalarial action. FEBS Lett 223: 251-254, 1987.
    • (1987) FEBS Lett , vol.223 , pp. 251-254
    • Sugioka, Y.1    Suzuki, M.2    Sugioka, K.3    Nakano, M.4
  • 144
    • 0027535124 scopus 로고
    • Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal: Selective modification of an active-site lysine
    • Szweda LI, Uchida K, Tsai L, and Stadtman ER. Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal: selective modification of an active-site lysine. J Biol Chem 268: 3342-3347, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 3342-3347
    • Szweda, L.I.1    Uchida, K.2    Tsai, L.3    Stadtman, E.R.4
  • 147
    • 0032821609 scopus 로고    scopus 로고
    • Ceroid/lipofuscin-loaded human fibroblasts show increased susceptibility to oxidative stress
    • Terman A, Abrahamsson N, and Brunk UT. Ceroid/lipofuscin-loaded human fibroblasts show increased susceptibility to oxidative stress. Exp Gerontol 34: 755-770, 1999.
    • (1999) Exp Gerontol , vol.34 , pp. 755-770
    • Terman, A.1    Abrahamsson, N.2    Brunk, U.T.3
  • 148
    • 0032169551 scopus 로고    scopus 로고
    • Ceroid/lipofuscin formation in cultured human fibroblasts: The role of oxidative stress and lysosomal proteolysis
    • Terman A and Brunk UT. Ceroid/lipofuscin formation in cultured human fibroblasts: the role of oxidative stress and lysosomal proteolysis. Mech Ageing Dev 104: 277-291, 1998.
    • (1998) Mech Ageing Dev , vol.104 , pp. 277-291
    • Terman, A.1    Brunk, U.T.2
  • 149
    • 0031889998 scopus 로고    scopus 로고
    • Lipofuscin: Mechanisms of formation and increase with age
    • Terman A and Brunk UT. Lipofuscin: mechanisms of formation and increase with age. APMIS 106: 265-276, 1998.
    • (1998) APMIS , vol.106 , pp. 265-276
    • Terman, A.1    Brunk, U.T.2
  • 150
    • 33749656530 scopus 로고    scopus 로고
    • The lysosomal-mitochondrial axis theory of postmitotic aging and cell death
    • Terman A, Gustafsson B, and Brunk UT. The lysosomal-mitochondrial axis theory of postmitotic aging and cell death. Chem Biol Interact 163: 29-37, 2006.
    • (2006) Chem Biol Interact , vol.163 , pp. 29-37
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 151
    • 0021351037 scopus 로고
    • Influence of oxygen tension, pro-oxidants and antioxidants on the formation of lipid peroxidation products (lipofuscin) in individual cultivated human glial cells
    • Thaw HH, Collins VP, and Brunk UT. Influence of oxygen tension, pro-oxidants and antioxidants on the formation of lipid peroxidation products (lipofuscin) in individual cultivated human glial cells. Mech Ageing Dev 24: 211-223, 1984.
    • (1984) Mech Ageing Dev , vol.24 , pp. 211-223
    • Thaw, H.H.1    Collins, V.P.2    Brunk, U.T.3
  • 152
    • 0032493431 scopus 로고    scopus 로고
    • Structural characterization and immunochemical detection of a fluorophore derived from 4-hydroxy-2-nonenal and lysine
    • Tsai L, Szweda PA, Vinogradova O, and Szweda LI. Structural characterization and immunochemical detection of a fluorophore derived from 4-hydroxy-2-nonenal and lysine. Proc Natl Acad Sci U S A 95: 7975-7980, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7975-7980
    • Tsai, L.1    Szweda, P.A.2    Vinogradova, O.3    Szweda, L.I.4
  • 154
    • 0027459566 scopus 로고
    • Kinetics of the pH-induced inactivation of human cathepsin L
    • Turk B, Dolenc I, Turk V, and Bieth JG. Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry 32: 375-380, 1993.
    • (1993) Biochemistry , vol.32 , pp. 375-380
    • Turk, B.1    Dolenc, I.2    Turk, V.3    Bieth, J.G.4
  • 155
    • 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. A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J 19: 2786-2792, 2000.
    • (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
  • 156
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase: A possible involvement of intra- and intermolecular cross-linking reaction
    • Uchida K and Stadtman ER. Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase: a possible involvement of intra- and intermolecular cross-linking reaction. J Biol Chem 268: 6388-6393, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 157
    • 0034849783 scopus 로고    scopus 로고
    • Autophagic cell death and its execution by lysosomal cathepsins
    • Uchiyama Y. Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol 64: 233-246, 2001.
    • (2001) Arch Histol Cytol , vol.64 , pp. 233-246
    • Uchiyama, Y.1
  • 158
    • 84934440405 scopus 로고    scopus 로고
    • Uttenweiler A and Mayer A. Microautophagy in the yeast Saccharomyces cerevisiae. Methods Mol Biol 445: 245-259, 2008.
    • Uttenweiler A and Mayer A. Microautophagy in the yeast Saccharomyces cerevisiae. Methods Mol Biol 445: 245-259, 2008.
  • 159
    • 0029563013 scopus 로고
    • Lipofuscin accumulation and ageing of fibroblasts
    • Von Zglinicki T, Nilsson E, Docke WD, and Brunk UT. Lipofuscin accumulation and ageing of fibroblasts. Gerontology 41(suppl 2): 95-108, 1995.
    • (1995) Gerontology , vol.41 , Issue.SUPPL. 2 , pp. 95-108
    • Von Zglinicki, T.1    Nilsson, E.2    Docke, W.D.3    Brunk, U.T.4
  • 161
    • 0000912176 scopus 로고    scopus 로고
    • Induction of human endothelial cell apoptosis requires both heat shock and oxidative stress responses
    • Wang JH, Redmond HP, Watson RW, and Bouchier-Hayes D. Induction of human endothelial cell apoptosis requires both heat shock and oxidative stress responses. Am J Physiol 272: C1543-C1551, 1997.
    • (1997) Am J Physiol , vol.272
    • Wang, J.H.1    Redmond, H.P.2    Watson, R.W.3    Bouchier-Hayes, D.4
  • 162
    • 35348948380 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand activates a lysosomal pathway of apoptosis that is regulated by Bcl-2 proteins
    • Werneburg NW, Guicciardi ME, Bronk SF, Kaufmann SH, and Gores GJ. Tumor necrosis factor-related apoptosis-inducing ligand activates a lysosomal pathway of apoptosis that is regulated by Bcl-2 proteins. J Biol Chem 282: 28960-28970, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 28960-28970
    • Werneburg, N.W.1    Guicciardi, M.E.2    Bronk, S.F.3    Kaufmann, S.H.4    Gores, G.J.5
  • 163
    • 0016255812 scopus 로고
    • Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B1
    • Wibo M and Poole B. Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B1. J Cell Biol 63: 430-440, 1974.
    • (1974) J Cell Biol , vol.63 , pp. 430-440
    • Wibo, M.1    Poole, B.2
  • 165
    • 33746926747 scopus 로고    scopus 로고
    • Hypochlorous acid induces apoptosis of cultured cortical neurons through activation of calpains and rupture of lysosomes
    • Yap YW, Whiteman M, Bay BH, Li Y, Sheu FS, Qi RZ, Tan CH, and Cheung NS. Hypochlorous acid induces apoptosis of cultured cortical neurons through activation of calpains and rupture of lysosomes. J Neurochem 98: 1597-1609, 2006.
    • (2006) J Neurochem , vol.98 , pp. 1597-1609
    • Yap, Y.W.1    Whiteman, M.2    Bay, B.H.3    Li, Y.4    Sheu, F.S.5    Qi, R.Z.6    Tan, C.H.7    Cheung, N.S.8
  • 167
    • 0037448105 scopus 로고    scopus 로고
    • Intralysosomal iron: A major determinant of oxidant-induced cell death
    • Yu Z, Persson HL, Eaton JW, and Brunk UT. Intralysosomal iron: a major determinant of oxidant-induced cell death. Free Radic Biol Med 34: 1243-1252, 2003.
    • (2003) Free Radic Biol Med , vol.34 , pp. 1243-1252
    • Yu, Z.1    Persson, H.L.2    Eaton, J.W.3    Brunk, U.T.4
  • 170
    • 24144435978 scopus 로고    scopus 로고
    • Chloroquine-mediated radiosensitization is due to the destabilization of the lysosomal membrane and subsequent induction of cell death by necrosis
    • Zhao H, Cai Y, Santi S, Lafrenie R, and Lee H. Chloroquine-mediated radiosensitization is due to the destabilization of the lysosomal membrane and subsequent induction of cell death by necrosis. Radiat Res 164: 250-257, 2005.
    • (2005) Radiat Res , vol.164 , pp. 250-257
    • Zhao, H.1    Cai, Y.2    Santi, S.3    Lafrenie, R.4    Lee, H.5
  • 171
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M, Antunes F, Eaton JW, and Brunk UT. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur J Biochem 270: 3778-3786, 2003.
    • (2003) Eur J Biochem , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 172
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • Zhao M, Brunk UT, and Eaton JW. Delayed oxidant-induced cell death involves activation of phospholipase A2. FEBS Lett 509: 399-404, 2001.
    • (2001) FEBS Lett , vol.509 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3
  • 173
    • 0035861890 scopus 로고    scopus 로고
    • Bcl-2 phosphorylation is required for inhibition of oxidative stress-induced lysosomal leak and ensuing apoptosis
    • Zhao M, Eaton JW, and Brunk UT. Bcl-2 phosphorylation is required for inhibition of oxidative stress-induced lysosomal leak and ensuing apoptosis. FEBS Lett 509: 405-412, 2001.
    • (2001) FEBS Lett , vol.509 , pp. 405-412
    • Zhao, M.1    Eaton, J.W.2    Brunk, U.T.3
  • 174
    • 31344436480 scopus 로고    scopus 로고
    • Autophagy of amyloid beta-protein in differentiated neuroblastoma cells exposed to oxidative stress
    • Zheng L, Roberg K, Jerhammar F, Marcusson J, and Terman A. Autophagy of amyloid beta-protein in differentiated neuroblastoma cells exposed to oxidative stress. Neurosci Lett 394: 184-189, 2006.
    • (2006) Neurosci Lett , vol.394 , pp. 184-189
    • Zheng, L.1    Roberg, K.2    Jerhammar, F.3    Marcusson, J.4    Terman, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.