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Volumn 15, Issue 26, 2009, Pages 3043-3051

Protein pool maintenance during oxidative stress

Author keywords

Oxidative stress; Proteasome; Protein oxidation; Proteolysis; Reactive species

Indexed keywords

4 HYDROXYNONENAL; BORTEZOMIB; CALPAIN; CASPASE; HEXANAL; LACTACYSTIN; MALONALDEHYDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEASOME; UBIQUITIN PROTEIN LIGASE;

EID: 70449458038     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209789058129     Document Type: Review
Times cited : (18)

References (113)
  • 3
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T, Reinheckel T, Davies KJA. Degradation of oxidized proteins in mammalian cells. FASEB J 1997; 11: 526-534 (Pubitemid 27274426)
    • (1997) FASEB Journal , vol.11 , Issue.7 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 4
    • 0034571026 scopus 로고    scopus 로고
    • Oxidative stress, aging and the proteasomal system
    • Grune T. Oxidative stress, aging and the proteasomal system. Biogerontology 2000; 1: 31-40.
    • (2000) Biogerontology , vol.1 , pp. 31-40
    • Grune, T.1
  • 5
    • 0037564169 scopus 로고    scopus 로고
    • Singlet-oxygen mediated damage to proteins and its consequences
    • Davies MJ. Singlet-oxygen mediated damage to proteins and its consequences. Biochem Biophys Res Commun 2003; 305: 761-770
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 761-770
    • Davies, M.J.1
  • 6
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • DOI 10.1016/S0891-5849(02)00765-7, PII S0891584902007657
    • Levine RL. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic Biol Med 2002; 32: 790-796 (Pubitemid 34439249)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 7
    • 0035371095 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis by the nonradical oxidants singlet oxygen or peroxynitrite
    • DOI 10.1016/S0891-5849(01)00515-9, PII S0891584901005159
    • Grune T, Klotz LO, Gieche J, Rudeck M, Sies H. Protein oxidation and proteolysis by the nonradical oxidants singlet oxygen or peroxynitrite. Free Radic Biol Med 2001; 30: 1243-1253 (Pubitemid 32463935)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.11 , pp. 1243-1253
    • Grune, T.1    Klotz, L.-O.2    Gieche, J.3    Rudeck, M.4    Sies, H.5
  • 9
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean RT, Shanlin FU, Stocker R, Davies MJ. Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 1997; 324: 1-18. (Pubitemid 27229359)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 10
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals I. General aspects
    • Davies KJA. Protein damage and degradation by oxygen radicals I. General aspects. J Biol Chem 1987; 262: 9895-9901
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 11
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals II. Modification of amino acids
    • Davies KJA, Delsignore ME, Lin SW. Protein damage and degradation by oxygen radicals II. Modification of amino acids. J Biol Chem 1987; 262: 9902-9907
    • (1987) J Biol Chem , vol.262 , pp. 9902-9907
    • Davies, K.J.A.1    Delsignore, M.E.2    Lin, S.W.3
  • 12
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure
    • Davies KJA, Delsignore ME. Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure. J Biol Chem 1987; 262: 9908-9913
    • (1987) J Biol Chem , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 13
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals IV. Degradation of denatured protein
    • Davies KJA, Lin SW, Pacifici RE. Protein damage and degradation by oxygen radicals IV. Degradation of denatured protein. J Biol Chem 1987; 262: 9914-9920
    • (1987) J Biol Chem , vol.262 , pp. 9914-9920
    • Davies, K.J.A.1    Lin, S.W.2    Pacifici, R.E.3
  • 14
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993; 62: 797-821. (Pubitemid 23237888)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 15
    • 0027414020 scopus 로고
    • Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome
    • Giulivi C, Davies KJA. Dityrosine and tyrosine oxidation products are endogenous markers for selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19S) proteasome. J Biol Chem 1993; 268: 8752-8759 (Pubitemid 23118663)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.12 , pp. 8752-8759
    • Giulivi, C.1    Davies, K.J.A.2
  • 16
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • DOI 10.1016/S0891-5849(02)00824-9, PII S0891584902008249
    • Shringarpure R, Davies KJA. Protein turnover by the proteasome in aging and disease. Free Radic Biol Med 2002; 32: 1084-1089 (Pubitemid 34603346)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1084-1089
    • Shringarpure, R.1    Davies, K.J.A.2
  • 17
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • DOI 10.1016/j.biocel.2004.04.020, PII S1357272504001670
    • Grune T, Jung T, Merker K, Davies KJA. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol 2004; 36: 2519-2530 (Pubitemid 39119763)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.A.4
  • 18
    • 0029972278 scopus 로고    scopus 로고
    • Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores
    • DOI 10.1016/0891-5849(96)00175-X
    • Yin D. Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores. Free Radic Biol Med 1996; 21: 871-888 (Pubitemid 26365282)
    • (1996) Free Radical Biology and Medicine , vol.21 , Issue.6 , pp. 871-888
    • Yin, D.1
  • 19
    • 0026515974 scopus 로고
    • Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonylprotein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes
    • Yin D. Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonylprotein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes. Mech Aging Dev 1992; 62: 35-46.
    • (1992) Mech Aging Dev , vol.62 , pp. 35-46
    • Yin, D.1
  • 21
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • DOI 10.1016/S0076-6879(94)33040-9
    • Levine RL, Williams JA, Stadtman ER, Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 1994; 233: 346-357 (Pubitemid 24177560)
    • (1994) Methods in Enzymology , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 23
    • 27544511969 scopus 로고    scopus 로고
    • High sensitivity enzyme-linked immunosorbent assay (ELISA) method for measuring protein carbonyl in samples with low amounts of protein
    • Alamdari DH, Kostidou E, Paletas K, Sarigianni M, Konstas AG, Karapiperidou A, et al. High sensitivity enzyme-linked immunosorbent assay (ELISA) method for measuring protein carbonyl in samples with low amounts of protein. Free Radic Biol Med 2005; 39: 1362-1367
    • (2005) Free Radic Biol Med , vol.39 , pp. 1362-1367
    • Alamdari, D.H.1    Kostidou, E.2    Paletas, K.3    Sarigianni, M.4    Konstas, A.G.5    Karapiperidou, A.6
  • 24
    • 0028242667 scopus 로고
    • Quantitation of 4-hydroxynonenal protein adducts
    • Uchida K, Stadtman ER. Quantitation of 4-hydroxynonenal protein adducts. Methods Enzymol 1994; 233: 371-380
    • (1994) Methods Enzymol , vol.233 , pp. 371-380
    • Uchida, K.1    Stadtman, E.R.2
  • 25
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert HF. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem 1994; 269: 7764-7771 (Pubitemid 24217992)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 26
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 1989; 264: 13963-13966
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 29
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med 1995; 18: 93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 31
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • Bader N, Grune T. Protein oxidation and proteolysis. Biol Chem 2006; 387: 1351-1355
    • (2006) Biol Chem , vol.387 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 32
    • 0036254702 scopus 로고    scopus 로고
    • Proteolytic response to oxidative stress in mammalian cells
    • Mehlhase J, Grune T. Proteolytic response to oxidative stress in mammalian cells. Biol Chem 2002; 383: 559-567
    • (2002) Biol Chem , vol.383 , pp. 559-567
    • Mehlhase, J.1    Grune, T.2
  • 33
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • Bohley P, Seglen PO. Proteases and proteolysis in the lysosome. Experentia 1992; 48: 151-157
    • (1992) Experentia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 34
    • 0023546546 scopus 로고
    • Calcium-dependent proteases: An enzyme system active at cellular membranes?
    • Mellgren RL. Calcium-dependent proteases: an enzyme system active at cellular membranes? FASEB J 1987; 1: 110-115
    • (1987) FASEB J , vol.1 , pp. 110-115
    • Mellgren, R.L.1
  • 35
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress cause relocation of lysosomal enzymes cathepsin D with ensuing apoptosis in neuronal rat cardiomyocytes
    • Roberg K, Ollinger K. Oxidative stress cause relocation of lysosomal enzymes cathepsin D with ensuing apoptosis in neuronal rat cardiomyocytes. Am J Pathol 1998; 152: 1151-1156
    • (1998) Am J Pathol , vol.152 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 36
    • 0026748405 scopus 로고
    • The intracellular storage and turnover of apolipoprotein B of oxidized LDL in macrophages
    • Jessup W, Mander EL, Dean RT. The intracellular storage and turnover of apolipoprotein B of oxidized LDL in macrophages. Biochem Biophys Acta 1992; 1126: 167-177
    • (1992) Biochem Biophys Acta , vol.1126 , pp. 167-177
    • Jessup, W.1    Mander, E.L.2    Dean, R.T.3
  • 37
    • 0027358327 scopus 로고
    • Inefficient degradation of oxidized regions of protein molecules
    • Grant AJ, Jessup W, Dean RT. Inefficient degradation of oxidized regions of protein molecules. Free Radic Res Commun 1993; 18: 259-267
    • (1993) Free Radic Res Commun , vol.18 , pp. 259-267
    • Grant, A.J.1    Jessup, W.2    Dean, R.T.3
  • 38
    • 0032169551 scopus 로고    scopus 로고
    • Ceroid/lipofuscin formation in cultured human fibroblasts: The role of oxidative stress and lysosomal proteolysis
    • Terman A, Brunk UT. Ceroid/lipofuscin formation in cultured human fibroblasts: the role of oxidative stress and lysosomal proteolysis. Mech Ageing Dev 1998; 104: 277-291
    • (1998) Mech Ageing Dev , vol.104 , pp. 277-291
    • Terman, A.1    Brunk, U.T.2
  • 39
    • 0033870001 scopus 로고    scopus 로고
    • Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
    • Sitte N, Huber M, Grune T, Ladhoff A, Doecke WD, Von Zglinicki T, et al. Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. FASEB J 2000; 14: 1490-1498
    • (2000) FASEB J , vol.14 , pp. 1490-1498
    • Sitte, N.1    Huber, M.2    Grune, T.3    Ladhoff, A.4    Doecke, W.D.5    Von Zglinicki, T.6
  • 40
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation system
    • Hofmann K, Falquet L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation system. Trends Biochem Sci 2001; 26: 347-350
    • (2001) Trends Biochem Sci , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 41
    • 0022996157 scopus 로고
    • Free radical mediated fragmentation of monoamine oxidase in the mitochondrial membrane
    • Dean RT, Thomas SM, Garner A. Free radical mediated fragmentation of monoamine oxidase in the mitochondrial membrane. Biochem J 1986; 240: 489-494
    • (1986) Biochem J , vol.240 , pp. 489-494
    • Dean, R.T.1    Thomas, S.M.2    Garner, A.3
  • 42
    • 0027352990 scopus 로고
    • Enhanced enzymatic degradation of radical damaged mitochondrial membrane components
    • Grant AJ, Jessup W, Dean RT. Enhanced enzymatic degradation of radical damaged mitochondrial membrane components. Free Radical Res Commun 1993; 19: 125-134
    • (1993) Free Radical Res Commun , vol.19 , pp. 125-134
    • Grant, A.J.1    Jessup, W.2    Dean, R.T.3
  • 43
    • 0026052529 scopus 로고
    • Enhanced proteolysis and changes in membrane-associated calpain following phenylhydrazine insult to human red cells
    • Mortensen AM, Novack RF. Enhanced proteolysis and changes in membrane-associated calpain following phenylhydrazine insult to human red cells. Toxicol Appl Pharmacol 1991; 110: 435-449
    • (1991) Toxicol Appl Pharmacol , vol.110 , pp. 435-449
    • Mortensen, A.M.1    Novack, R.F.2
  • 44
    • 0028109433 scopus 로고
    • Presence of membrane- Bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense
    • Beppu M, Inoue M, Ishikawa T, Kikugawa K. Presence of membrane- bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense. Biochim Biophys Acta 1994; 1196: 81-87
    • (1994) Biochim Biophys Acta , vol.1196 , pp. 81-87
    • Beppu, M.1    Inoue, M.2    Ishikawa, T.3    Kikugawa, K.4
  • 45
    • 0027257647 scopus 로고
    • Regulation of selective protein degradation in the endoplasmic reticulum by redox potential
    • Young J, Kane LP, Exley M, Wileman T. Regulation of selective protein degradation in the endoplasmic reticulum by redox potential. J Biol Chem 1993; 268: 19810-19818
    • (1993) J Biol Chem , vol.268 , pp. 19810-19818
    • Young, J.1    Kane, L.P.2    Exley, M.3    Wileman, T.4
  • 46
    • 0033594745 scopus 로고    scopus 로고
    • Diverse stimuli induce calpain overexpression and apoptosis in C6 glioma cells
    • Ray SK, Wilford GG, Crosby CV, Hogan EL, Banik NL. Diverse stimuli induce calpain overexpression and apoptosis in C6 glioma cells. Brain Res 1999; 829: 18-27.
    • (1999) Brain Res , vol.829 , pp. 18-27
    • Ray, S.K.1    Wilford, G.G.2    Crosby, C.V.3    Hogan, E.L.4    Banik, N.L.5
  • 47
    • 0029996607 scopus 로고    scopus 로고
    • Calpain activation in plasma membrane bleb formation during tert-butyl-hydroperoxide-induced rat hepatocyte injury
    • Miyoshi H, Umeshita K, Sakon M, Imajoh-Ohmi S, Fujitani K, Gotoh M, et al. Calpain activation in plasma membrane bleb formation during tert-butyl-hydroperoxide-induced rat hepatocyte injury. Gastroenterology 1996; 110: 1897-1904
    • (1996) Gastroenterology , vol.110 , pp. 1897-1904
    • Miyoshi, H.1    Umeshita, K.2    Sakon, M.3    Imajoh-Ohmi, S.4    Fujitani, K.5    Gotoh, M.6
  • 48
    • 0035936965 scopus 로고    scopus 로고
    • White matter damage following systemic injection oft he mitochondrial inhibitor 3-nitropropionic acid in rat
    • McCracken E, Dewar D, Hunter AJ. White matter damage following systemic injection oft he mitochondrial inhibitor 3-nitropropionic acid in rat. Brain Res 2001; 892: 329-335
    • (2001) Brain Res , vol.892 , pp. 329-335
    • McCracken, E.1    Dewar, D.2    Hunter, A.J.3
  • 49
    • 0029439509 scopus 로고
    • Oxidative stress: The paradox of aerobic life
    • Davies KJA. Oxidative stress: the paradox of aerobic life. Biochem Soc Symp 1995: 61: 1-31.
    • (1995) Biochem Soc Symp , vol.61 , pp. 1-31
    • Davies, K.J.A.1
  • 50
    • 0016772784 scopus 로고
    • Relationship between in vivo degradative rates and isoelectric points of proteins
    • Dice JF, Goldberg AL. Relationship between in vivo degradative rates and isoelectric points of proteins. Proc Natl Acad Sci USA 1975; 72: 3893-3897
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3893-3897
    • Dice, J.F.1    Goldberg, A.L.2
  • 51
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota DA, Davies KJA. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002; 4: 674-680
    • (2002) Nat Cell Biol , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.A.2
  • 52
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota DA, Remmen HV, Davies KJA. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett 2002; 532: 103-106
    • (2002) FEBS Lett , vol.532 , pp. 103-106
    • Bota, D.A.1    Remmen, H.V.2    Davies, K.J.A.3
  • 53
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell death
    • Chan SL, Mattson MP. Caspase and calpain substrates: roles in synaptic plasticity and cell death. J Neurosci Res 1999; 58: 167-190
    • (1999) J Neurosci Res , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 54
    • 0033817520 scopus 로고    scopus 로고
    • Early caspase activation in leukemic cells subject to etoposide-induced G2-M arrest: Evidence of commitment to apoptosis rather than mitochondrial cell death
    • Sleiman RJ, Stewart BW. Early caspase activation in leukemic cells subject to etoposide-induced G2-M arrest: evidence of commitment to apoptosis rather than mitochondrial cell death. Clin Cancer Res 2000; 6: 3756-3765
    • (2000) Clin Cancer Res , vol.6 , pp. 3756-3765
    • Sleiman, R.J.1    Stewart, B.W.2
  • 55
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G, Davies KJA. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003; 305: 709-718
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.A.4
  • 56
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T, Reinheckel T, Davies KJA. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem 1996; 271: 15504-15509
    • (1996) J Biol Chem , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 57
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress
    • Grune T, Reinheckel T, Joshi M, Davies KJA. Proteolysis in cultured liver epithelial cells during oxidative stress. J Biol Chem 1995; 270: 2344-2351
    • (1995) J Biol Chem , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 58
    • 0032080117 scopus 로고    scopus 로고
    • Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome
    • Grune T, Blasig IE, Sitte N, Roloff B, Haseloff R, Davies KJA. Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome. J Biol Chem 1998; 273: 10857-10862
    • (1998) J Biol Chem , vol.273 , pp. 10857-10862
    • Grune, T.1    Blasig, I.E.2    Sitte, N.3    Roloff, B.4    Haseloff, R.5    Davies, K.J.A.6
  • 59
    • 0032438035 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts
    • Sitte N, Merker K, Grune T. Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts. FEBS Lett 1998; 440: 399-402.
    • (1998) FEBS Lett , vol.440 , pp. 399-402
    • Sitte, N.1    Merker, K.2    Grune, T.3
  • 60
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79: 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 61
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg A. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996; 65: 801-807
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-807
    • Coux, O.1    Tanaka, K.2    Goldberg, A.3
  • 62
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett AJ. Proteasomes: multicatalytic proteinase complexes. Biochem J 1993; 291: 1-10.
    • (1993) Biochem J , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 63
    • 0032006110 scopus 로고    scopus 로고
    • Intracellular distribution of proteasomes
    • Rivett AJ. Intracellular distribution of proteasomes. Curr Opin Immunol 1998; 10: 110-114
    • (1998) Curr Opin Immunol , vol.10 , pp. 110-114
    • Rivett, A.J.1
  • 64
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 65
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jensch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999; 96: 635-644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jensch, S.6
  • 66
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • DOI 10.1146/annurev.biochem.68.1.1015
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015-1068 (Pubitemid 29449214)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 67
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson KD. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin Cell Dev Biol 2000; 11: 141-148
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 68
    • 0028365076 scopus 로고
    • Activation of the multicatalytic protease
    • Hoffmann L, Rechsteiner M. Activation of the multicatalytic protease. J Biol Chem 1994; 269: 16890-16895
    • (1994) J Biol Chem , vol.269 , pp. 16890-16895
    • Hoffmann, L.1    Rechsteiner, M.2
  • 69
    • 0028872057 scopus 로고
    • Human lymphoblast and erythrocyte multicatalytic proteases: Differential peptidase activities and responses to the 11S regulator
    • Ustrell V, Realini C, Pratt G, Rechneister M. Human lymphoblast and erythrocyte multicatalytic proteases: differential peptidase activities and responses to the 11S regulator. FEBS Lett 1995; 376: 155-158
    • (1995) FEBS Lett , vol.376 , pp. 155-158
    • Ustrell, V.1    Realini, C.2    Pratt, G.3    Rechneister, M.4
  • 70
    • 0029874055 scopus 로고    scopus 로고
    • The proteasome subunit, C2, contains an important site for binding of the PA28 (11S) activator
    • Kania MA, DeMartino GN, Baumeister W, Goldberg AL. The proteasome subunit, C2, contains an important site for binding of the PA28 (11S) activator. Eur J Biochem 1996; 236: 510-516
    • (1996) Eur J Biochem , vol.236 , pp. 510-516
    • Kania, M.A.1    DeMartino, G.N.2    Baumeister, W.3    Goldberg, A.L.4
  • 71
    • 0024843661 scopus 로고
    • Maxroxyproteinase (M.O.P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells
    • Pacifici RE, Salo DC, Davies KJA. Maxroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radic Biol Med 1989; 7: 521-536
    • (1989) Free Radic Biol Med , vol.7 , pp. 521-536
    • Pacifici, R.E.1    Salo, D.C.2    Davies, K.J.A.3
  • 72
    • 0027324284 scopus 로고
    • Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Pacifici RE, Kono Y, Davies KJA. Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. J Biol Chem 1993; 268: 15405-15411
    • (1993) J Biol Chem , vol.268 , pp. 15405-15411
    • Pacifici, R.E.1    Kono, Y.2    Davies, K.J.A.3
  • 73
    • 0028245961 scopus 로고
    • Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Guilivi C, Pacifici RE, Davies KJA. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Arc Biochem Biophys 1994; 311: 329-341
    • (1994) Arc Biochem Biophys , vol.311 , pp. 329-341
    • Guilivi, C.1    Pacifici, R.E.2    Davies, K.J.A.3
  • 74
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJA. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83: 301-310
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.A.1
  • 75
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein
    • Friguet B, Szweda LI. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett 1997; 405: 21-25
    • (1997) FEBS Lett , vol.405 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 76
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R, Grune T, Davies KJA. Protein oxidation and 20S proteasome dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001; 58: 1442-1450 (Pubitemid 32964414)
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.10 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.A.3
  • 77
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure R, Grune T, Mehlhase J, Davies KJA. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003; 278: 311-318
    • (2003) J Biol Chem , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 78
    • 0030598901 scopus 로고    scopus 로고
    • Phosphorylation of the proteasome activator PA28 is required for proteasome activation
    • Li N, Lerea KM, Etlinger JD. Phosphorylation of the proteasome activator PA28 is required for proteasome activation. Biochem Biophys Res Commun 1996; 225: 855-860
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 855-860
    • Li, N.1    Lerea, K.M.2    Etlinger, J.D.3
  • 79
    • 0029892643 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells
    • Mason GG, Hendil KB, Rivett AJ. Phosphorylation of proteasomes in mammalian cells. Eur J Biochem 1996; 238: 453-462
    • (1996) Eur J Biochem , vol.238 , pp. 453-462
    • Mason, G.G.1    Hendil, K.B.2    Rivett, A.J.3
  • 80
    • 1342294159 scopus 로고    scopus 로고
    • Stability of the nuclear protein turnover during cellular senescence of human fibroblasts
    • Merker K, Ullrich O, Schmidt H, Sitte N, Grune T. Stability of the nuclear protein turnover during cellular senescence of human fibroblasts. FASEB J 2003; 17: 1963-1965
    • (2003) FASEB J , vol.17 , pp. 1963-1965
    • Merker, K.1    Ullrich, O.2    Schmidt, H.3    Sitte, N.4    Grune, T.5
  • 81
    • 0036844724 scopus 로고    scopus 로고
    • PARP-mediated proteasome activation: A coordination of DNA repair and protein degradation?
    • Arnold J, Grune T. PARP-mediated proteasome activation: a coordination of DNA repair and protein degradation? Bioessays 2002; 24: 1060-1065
    • (2002) Bioessays , vol.24 , pp. 1060-1065
    • Arnold, J.1    Grune, T.2
  • 82
  • 84
    • 0035478982 scopus 로고    scopus 로고
    • Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells
    • Ullrich O, Grune T. Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells. Free Radic Biol Med 2001; 31: 887-893
    • (2001) Free Radic Biol Med , vol.31 , pp. 887-893
    • Ullrich, O.1    Grune, T.2
  • 85
    • 57449113835 scopus 로고    scopus 로고
    • Turnover of oxidatively modified proteins: The usage of in vitro and metabolic labeling
    • Catalgol B, Grune T. Turnover of oxidatively modified proteins: the usage of in vitro and metabolic labeling. Free Rad Biol Med 2009; 46: 8-13.
    • (2009) Free Rad Biol Med , vol.46 , pp. 8-13
    • Catalgol, B.1    Grune, T.2
  • 86
    • 0025358959 scopus 로고
    • Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo DC, Pacifici RE, Lin SW, Giulivi C, Davies KJA. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. J Biol Chem 1990; 265: 11919-11927 (Pubitemid 120013349)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.20 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Lin, S.W.3    Giulivi, C.4    Davies, K.J.A.5
  • 87
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev AF, Goldberg AL. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001; 8: 739-758
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 89
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A, Michaud C, Powers JC, Orlowski M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 1992; 31: 9421-9428
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 90
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    • Bogyo M, McMaster JS, Gaczynska M, Tortorella D, Goldberg AL, Ploegh H. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc Natl Acad Sci USA 1997; 94: 6629-6634
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 92
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995; 268: 726-731
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 93
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for clasto-lactacystin beta-lactone
    • Dick LR, Cruikshank AA, Grenier L, Melandri FD, Nunes SL, Stein RL. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. J Biol Chem 1996; 271: 7273-7276
    • (1996) J Biol Chem , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 94
    • 0343262654 scopus 로고    scopus 로고
    • Crystal structure of epoxomicin: 20s proteasome reveals a molecular basis for selectivity of α',β'-epoxyketone proteasome inhibitors
    • Groll M, Kim KB, Kairies N, Huber R, Crews CM. Crystal structure of epoxomicin: 20s proteasome reveals a molecular basis for selectivity of α',β'-epoxyketone proteasome inhibitors. J Am Chem Soc 2000; 122: 1237-1238
    • (2000) J Am Chem Soc , vol.122 , pp. 1237-1238
    • Groll, M.1    Kim, K.B.2    Kairies, N.3    Huber, R.4    Crews, C.M.5
  • 95
    • 48349087467 scopus 로고    scopus 로고
    • Induction of autophagy by proteasome inhibitor is associated with proliferative arrest in colon cancer cells
    • Wu WK, Wu YC, Yu L, Li ZJ, Sung JJ, Cho CH. Induction of autophagy by proteasome inhibitor is associated with proliferative arrest in colon cancer cells. Biochem Biophys Res Commun 2008; 374: 258-263
    • (2008) Biochem Biophys Res Commun , vol.374 , pp. 258-263
    • Wu, W.K.1    Wu, Y.C.2    Yu, L.3    Li, Z.J.4    Sung, J.J.5    Cho, C.H.6
  • 97
    • 50149093848 scopus 로고    scopus 로고
    • Targeted therapeutic approach for an anaplastic thyroid cancer in vitro and in vivo
    • Stenner F, Liewen H, Zweifel M, Weber A, Tchinda J, Bode B, et al. Targeted therapeutic approach for an anaplastic thyroid cancer in vitro and in vivo. Cancer Sci 2008; 99: 1847-1852
    • (2008) Cancer Sci , vol.99 , pp. 1847-1852
    • Stenner, F.1    Liewen, H.2    Zweifel, M.3    Weber, A.4    Tchinda, J.5    Bode, B.6
  • 99
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T, Richardson P, Chauhan D, Palombella VJ, Elliott PJ, et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 2001; 61: 3071-3076
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5
  • 100
    • 0034722897 scopus 로고    scopus 로고
    • New agents in cancer clinical trials
    • Adams J, Elliott PJ. New agents in cancer clinical trials. Oncogene 2000; 19: 6687-6692
    • (2000) Oncogene , vol.19 , pp. 6687-6692
    • Adams, J.1    Elliott, P.J.2
  • 103
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T, Ullrich O, Sitte N, Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000; 377: 65-68
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 104
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress
    • Shang F, Gong X, Taylor A. Activity of ubiquitin-dependent pathway in response to oxidative stress. J Biol Chem 1997; 272: 23086-23093
    • (1997) J Biol Chem , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 105
    • 0030724889 scopus 로고    scopus 로고
    • Regulation of ubiquitin conjugating enzymes by glutathione following oxidative stress
    • Jahngen-Hodge J, Obin MS, Gong X, Shang F, Nowell TR Jr, Gong J, et al. Regulation of ubiquitin conjugating enzymes by glutathione following oxidative stress. J Biol Chem 1997; 272: 28218-28226
    • (1997) J Biol Chem , vol.272 , pp. 28218-28226
    • Jahngen-Hodge, J.1    Obin, M.S.2    Gong, X.3    Shang, F.4    Nowell Jr., T.R.5    Gong, J.6
  • 106
    • 0029952689 scopus 로고    scopus 로고
    • Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure
    • Strack PR, Waxman L, Fagan JM. Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure. Biochemistry 1996; 35: 7142-7149
    • (1996) Biochemistry , vol.35 , pp. 7142-7149
    • Strack, P.R.1    Waxman, L.2    Fagan, J.M.3
  • 107
    • 0027359174 scopus 로고
    • Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis
    • Davies JM, Horwitz DA, Davies KJA. Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis. Free Radic Biol Med 1993; 15: 637-643
    • (1993) Free Radic Biol Med , vol.15 , pp. 637-643
    • Davies, J.M.1    Horwitz, D.A.2    Davies, K.J.A.3
  • 108
    • 0037082124 scopus 로고    scopus 로고
    • Age dependent declines in proteasome activity in the heart
    • Bulteau AL, Szweda LI, Friguet B. Age dependent declines in proteasome activity in the heart. Arch Biochem Biophys 2002; 397: 298-304.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 298-304
    • Bulteau, A.L.1    Szweda, L.I.2    Friguet, B.3
  • 109
    • 33750720268 scopus 로고    scopus 로고
    • Protein oxidation and degradation during aging: Role in skin aging and neurodegeneration
    • Widmer R, Ziaja I, Grune T. Protein oxidation and degradation during aging: role in skin aging and neurodegeneration. Free Radic Res 2006; 40: 1259-1268
    • (2006) Free Radic Res , vol.40 , pp. 1259-1268
    • Widmer, R.1    Ziaja, I.2    Grune, T.3
  • 110
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • Friguet B. Oxidized protein degradation and repair in ageing and oxidative stress. FEBS Lett 2006; 580: 2910-2916
    • (2006) FEBS Lett , vol.580 , pp. 2910-2916
    • Friguet, B.1
  • 111
    • 47249125823 scopus 로고    scopus 로고
    • Life under stress: The probiotic stress response and how it may be manipulated
    • Corcoran BM, Stanton C, Fitzgerald G, Ross RP. Life under stress: the probiotic stress response and how it may be manipulated. Curr Pharm Des 2008; 14(14): 1382-1399
    • (2008) Curr Pharm des , vol.14 , Issue.14 , pp. 1382-1399
    • Corcoran, B.M.1    Stanton, C.2    Fitzgerald, G.3    Ross, R.P.4
  • 112
    • 57349089167 scopus 로고    scopus 로고
    • Physiological basis for contractile dysfunction in heart failure
    • Dalla Libera L, Vescovo G, Volterrani M. Physiological basis for contractile dysfunction in heart failure. Curr Pharm Des 2008; 14(25): 2572-2581
    • (2008) Curr Pharm des , vol.14 , Issue.25 , pp. 2572-2581
    • Dalla Libera, L.1    Vescovo, G.2    Volterrani, M.3
  • 113
    • 44449172015 scopus 로고    scopus 로고
    • Role of advanced glycation end products in diabetic neuropathy
    • Sugimoto K, Yasujima M, Yagihashi S. Role of advanced glycation end products in diabetic neuropathy. Curr Pharm Des 2008; 14(10): 953-961
    • (2008) Curr Pharm des , vol.14 , Issue.10 , pp. 953-961
    • Sugimoto, K.1    Yasujima, M.2    Yagihashi, S.3


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