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Volumn 111, Issue 20, 2014, Pages

Hypochlorite-induced structural modifications enhance the chaperone activity of human ?2-macroglobulin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 MACROGLOBULIN; AMYLOID BETA PROTEIN[1-42]; CHAPERONE; CITRATE SYNTHASE; CREATINE KINASE; DIMER; FIBRINOGEN; HYPOCHLORITE; LIPOPROTEIN RECEPTOR; OXIDIZED LOW DENSITY LIPOPROTEIN; TETRAMER;

EID: 84901052763     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1403379111     Document Type: Article
Times cited : (62)

References (82)
  • 1
    • 55449092300 scopus 로고    scopus 로고
    • Bleach activates a redox-regulated chaperone by oxidative protein unfolding
    • Winter J, Ilbert M, Graf PC, Ozcelik D, Jakob U (2008) Bleach activates a redox-regulated chaperone by oxidative protein unfolding. Cell 135(4):691-701.
    • (2008) Cell , vol.135 , Issue.4 , pp. 691-701
    • Winter, J.1    Ilbert, M.2    Graf, P.C.3    Ozcelik, D.4    Jakob, U.5
  • 2
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ (1989) Tissue destruction by neutrophils. N Engl J Med 320(6):365-376.
    • (1989) N Engl J Med , vol.320 , Issue.6 , pp. 365-376
    • Weiss, S.J.1
  • 3
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff SJ (2005) Myeloperoxidase: Friend and foe. J Leukoc Biol 77(5):598-625.
    • (2005) J Leukoc Biol , vol.77 , Issue.5 , pp. 598-625
    • Klebanoff, S.J.1
  • 4
    • 0345148809 scopus 로고    scopus 로고
    • Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro
    • Yang CY, et al. (1999) Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro. J Lipid Res 40(4):686-698.
    • (1999) J Lipid Res , vol.40 , Issue.4 , pp. 686-698
    • Yang, C.Y.1
  • 5
    • 3343003470 scopus 로고    scopus 로고
    • Neuronal expression of myeloperoxidase is increased in Alzheimers disease
    • Green PS, et al. (2004) Neuronal expression of myeloperoxidase is increased in Alzheimers disease. J Neurochem 90(3):724-733.
    • (2004) J Neurochem , vol.90 , Issue.3 , pp. 724-733
    • Green, P.S.1
  • 7
    • 79960671469 scopus 로고    scopus 로고
    • Age related macular degeneration and drusen: Neuroinflammation in the retina
    • Buschini E, Piras A, Nuzzi R, Vercelli A (2011) Age related macular degeneration and drusen: Neuroinflammation in the retina. Prog Neurobiol 95(1):14-25.
    • (2011) Prog Neurobiol , vol.95 , Issue.1 , pp. 14-25
    • Buschini, E.1    Piras, A.2    Nuzzi, R.3    Vercelli, A.4
  • 8
    • 0020614308 scopus 로고
    • Generation of IgG aggregates by the myeloperoxidase-hydrogen peroxide system
    • Jasin HE (1983) Generation of IgG aggregates by the myeloperoxidase- hydrogen peroxide system. J Immunol 130(4):1918-1923.
    • (1983) J Immunol , vol.130 , Issue.4 , pp. 1918-1923
    • Jasin, H.E.1
  • 9
    • 0015896128 scopus 로고
    • The interaction of α2-macroglobulin with proteinases Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
    • Barrett AJ, Starkey PM (1973) The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochem J 133(4):709-724.
    • (1973) Biochem J , vol.133 , Issue.4 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 10
    • 0027076834 scopus 로고
    • α 2-macroglobulin, a multifunctional binding protein with targeting characteristics
    • Borth W (1992) α2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J 6(15):3345-3353.
    • (1992) FASEB J , vol.6 , Issue.15 , pp. 3345-3353
    • Borth, W.1
  • 13
    • 84874192917 scopus 로고    scopus 로고
    • Protease-Activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms
    • Wyatt AR, et al. (2013) Protease-Activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. FEBS Lett 587(5):398-403.
    • (2013) FEBS Lett , vol.587 , Issue.5 , pp. 398-403
    • Wyatt, A.R.1
  • 14
    • 63249134826 scopus 로고    scopus 로고
    • α 2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species
    • Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR (2009) α2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J Biol Chem 284(7):4246-4254.
    • (2009) J Biol Chem , vol.284 , Issue.7 , pp. 4246-4254
    • Yerbury, J.J.1    Kumita, J.R.2    Meehan, S.3    Dobson, C.M.4    Wilson, M.R.5
  • 15
    • 0032539723 scopus 로고    scopus 로고
    • α 2-macroglobulin associates with β-Amyloid peptide and prevents fibril formation
    • Hughes SR, et al. (1998) α2-macroglobulin associates with β-Amyloid peptide and prevents fibril formation. Proc Natl Acad Sci USA 95(6):3275-3280.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.6 , pp. 3275-3280
    • Hughes, S.R.1
  • 16
    • 79953208604 scopus 로고    scopus 로고
    • Inhibition of β2-microglobulin amyloid fibril formation by α2- macroglobulin
    • Ozawa D, et al. (2011) Inhibition of β2-microglobulin amyloid fibril formation by α2- macroglobulin. J Biol Chem 286(11):9668-9676.
    • (2011) J Biol Chem , vol.286 , Issue.11 , pp. 9668-9676
    • Ozawa, D.1
  • 17
    • 38549152772 scopus 로고    scopus 로고
    • Protease activation of α2-macroglobulin modulates a chaperone-like action with broad specificity
    • French K, Yerbury JJ, Wilson MR (2008) Protease activation of α2-macroglobulin modulates a chaperone-like action with broad specificity. Biochemistry 47(4):1176-1185.
    • (2008) Biochemistry , vol.47 , Issue.4 , pp. 1176-1185
    • French, K.1    Yerbury, J.J.2    Wilson, M.R.3
  • 18
    • 84864515731 scopus 로고    scopus 로고
    • Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
    • Mannini B, et al. (2012) Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc Natl Acad Sci USA 109(31):12479-12484.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.31 , pp. 12479-12484
    • Mannini, B.1
  • 19
    • 84877353475 scopus 로고    scopus 로고
    • Extracellular chaperones prevent Aβ42-induced toxicity in rat brains
    • Cascella R, et al. (2013) Extracellular chaperones prevent Aβ42-induced toxicity in rat brains. Biochim Biophys Acta 1832(8):1217-1226.
    • (2013) Biochim Biophys Acta , Issue.8 , pp. 1217-1226
    • Cascella, R.1
  • 20
    • 0031589609 scopus 로고    scopus 로고
    • The subunits of α2-macroglobulin receptor/low density lipoprotein receptor-related protein, native and transformed α2-macroglobulin and interleukin 6 in Alzheimers disease
    • Thal DR, Schober R, Birkenmeier G (1997) The subunits of α2-macroglobulin receptor/low density lipoprotein receptor-related protein, native and transformed α2-macroglobulin and interleukin 6 in Alzheimers disease. Brain Res 777(1-2):223-227.
    • (1997) Brain Res , vol.777 , Issue.1-2 , pp. 223-227
    • Thal, D.R.1    Schober, R.2    Birkenmeier, G.3
  • 21
    • 34547751817 scopus 로고    scopus 로고
    • Serum macroglobulin induces prion protein transition
    • Adler V, Kryukov V (2007) Serum macroglobulin induces prion protein transition. Neurochem J 1(1):43-52.
    • (2007) Neurochem J , vol.1 , Issue.1 , pp. 43-52
    • Adler, V.1    Kryukov, V.2
  • 22
    • 0018571222 scopus 로고
    • Soluble proteins in the human atherosclerotic plaque with spectral reference to immunoglobulins, C3- complement component, alpha 1-Antitrypsin and alpha 2-macroglobulin
    • Hollander W, Colombo MA, Kirkpatrick B, Paddock J (1979) Soluble proteins in the human atherosclerotic plaque. With spectral reference to immunoglobulins, C3- complement component, alpha 1-Antitrypsin and alpha 2-macroglobulin. Atherosclerosis 34(4):391-405.
    • (1979) Atherosclerosis , vol.34 , Issue.4 , pp. 391-405
    • Hollander, W.1    Colombo, M.A.2    Kirkpatrick, B.3    Paddock, J.4
  • 23
    • 0020002162 scopus 로고
    • Deposits of α2M in the rheumatoid synovial membrane
    • Flory ED, Clarris BJ, Muirden KD (1982) Deposits of α2M in the rheumatoid synovial membrane. Ann Rheum Dis 41(5):520-526.
    • (1982) Ann Rheum Dis , vol.41 , Issue.5 , pp. 520-526
    • Flory, E.D.1    Clarris, B.J.2    Muirden, K.D.3
  • 24
    • 0024333351 scopus 로고
    • α-Macroglobulins: Structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen L (1989) α-Macroglobulins: Structure, shape, and mechanism of proteinase complex formation. J Biol Chem 264(20):11539-11542.
    • (1989) J Biol Chem , vol.264 , Issue.20 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 25
    • 0028060243 scopus 로고
    • Oxidative dissociation of human α2-macroglobulin tetramers into dysfunctional dimers
    • Reddy VY, et al. (1994) Oxidative dissociation of human α2-macroglobulin tetramers into dysfunctional dimers. J Biol Chem 269(6):4683-4691.
    • (1994) J Biol Chem , vol.269 , Issue.6 , pp. 4683-4691
    • Reddy, V.Y.1
  • 26
    • 0024410109 scopus 로고
    • Functional inactivation and structural disruption of human α2-macroglobulin by neutrophils and eosinophils
    • Reddy VY, Pizzo SV, Weiss SJ (1989) Functional inactivation and structural disruption of human α2-macroglobulin by neutrophils and eosinophils. J Biol Chem 264(23): 13801-13809.
    • (1989) J Biol Chem , vol.264 , Issue.23 , pp. 13801-13809
    • Reddy, V.Y.1    Pizzo, S.V.2    Weiss, S.J.3
  • 27
    • 0344564123 scopus 로고    scopus 로고
    • Mechanism of hypochlorite-mediated inactivation of proteinase inhibition by α2-macroglobulin
    • Wu SM, Pizzo SV (1999) Mechanism of hypochlorite-mediated inactivation of proteinase inhibition by α2-macroglobulin. Biochemistry 38(42):13983-13990.
    • (1999) Biochemistry , vol.38 , Issue.42 , pp. 13983-13990
    • Wu, S.M.1    Pizzo, S.V.2
  • 28
    • 0030860903 scopus 로고    scopus 로고
    • The binding of receptor-recognized α2-macroglobulin to the low density lipoprotein receptor-related protein and the α2M signaling receptor is decoupled by oxidation
    • Wu SM, Boyer CM, Pizzo SV (1997) The binding of receptor-recognized α2-macroglobulin to the low density lipoprotein receptor-related protein and the α2M signaling receptor is decoupled by oxidation. J Biol Chem 272(33):20627-20635.
    • (1997) J Biol Chem , vol.272 , Issue.33 , pp. 20627-20635
    • Wu, S.M.1    Boyer, C.M.2    Pizzo, S.V.3
  • 29
    • 0032531422 scopus 로고    scopus 로고
    • Oxidized α2-macroglobulin (α2M) differentially regulates receptor binding by cytokines/growth factors: Implications for tissue injury and repair mechanisms in inflammation
    • Wu SM, Patel DD, Pizzo SV (1998) Oxidized α2-macroglobulin (α2M) differentially regulates receptor binding by cytokines/growth factors: Implications for tissue injury and repair mechanisms in inflammation. J Immunol 161(8):4356-4365.
    • (1998) J Immunol , vol.161 , Issue.8 , pp. 4356-4365
    • Wu, S.M.1    Patel, D.D.2    Pizzo, S.V.3
  • 30
    • 0019784199 scopus 로고
    • Clearance and binding of two electrophoreticfast forms of human α2-macroglobulin
    • Imber MJ, Pizzo SV (1981) Clearance and binding of two electrophoretic fast forms of human α2-macroglobulin. J Biol Chem 256(15):8134-8139.
    • (1981) J Biol Chem , vol.256 , Issue.15 , pp. 8134-8139
    • Imber, M.J.1    Pizzo, S.V.2
  • 31
    • 79959400821 scopus 로고    scopus 로고
    • Peroxidase-induced degradation of single-walled carbon nanotubes: Hypochlorite is a major oxidant capable of in vivo degradation of carbon nanotubes
    • Vlasova II, et al. (2011) Peroxidase-induced degradation of single-walled carbon nanotubes: Hypochlorite is a major oxidant capable of in vivo degradation of carbon nanotubes. J Phys Conf Ser 291(1):012056.
    • (2011) J Phys Conf ser , vol.291 , Issue.1 , pp. 012056
    • Vlasova, I.I.1
  • 32
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • Hawkins CL, Pattison DI, Davies MJ (2003) Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 25(3-4):259-274.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 33
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton MB, Kettle AJ, Winterbourn CC (1998) Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing. Blood 92(9):3007-3017.
    • (1998) Blood , vol.92 , Issue.9 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 34
    • 0026027712 scopus 로고
    • The oxidant hypochlorite (OCl-), a product of the myeloperoxidase system, degrades articular cartilage proteoglycan aggregate
    • Katrantzis M, Baker MS, Handley CJ, Lowther DA (1991) The oxidant hypochlorite (OCl-), a product of the myeloperoxidase system, degrades articular cartilage proteoglycan aggregate. Free Radic Biol Med 10(2):101-109.
    • (1991) Free Radic Biol Med , vol.10 , Issue.2 , pp. 101-109
    • Katrantzis, M.1    Baker, M.S.2    Handley, C.J.3    Lowther, D.A.4
  • 35
    • 0030966334 scopus 로고    scopus 로고
    • The contact zones in human α2-macroglobulin- functional domains important for the regulation of the trapping mechanism
    • Shanbhag VP, Stigbrand T, Jensen PE (1997) The contact zones in human α2-macroglobulin- functional domains important for the regulation of the trapping mechanism. Eur J Biochem 244(3):694-699.
    • (1997) Eur J Biochem , vol.244 , Issue.3 , pp. 694-699
    • Shanbhag, V.P.1    Stigbrand, T.2    Jensen, P.E.3
  • 36
    • 0026637215 scopus 로고
    • Temperature dependence of the kinetics of the urea-induced dissociation of human plasma α2-macroglobulin into half-molecules. A minimum rate at 15 degrees C indicates hydrophobic interaction between the subunits
    • Sjöberg B, Pap S, Mortensen K (1992) Temperature dependence of the kinetics of the urea-induced dissociation of human plasma α2-macroglobulin into half-molecules. A minimum rate at 15 degrees C indicates hydrophobic interaction between the subunits. J Mol Biol 225(2):551-556.
    • (1992) J Mol Biol , vol.225 , Issue.2 , pp. 551-556
    • Sjöberg, B.1    Pap, S.2    Mortensen, K.3
  • 37
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine RL, Moskovitz J, Stadtman ER (2000) Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation. IUBMB Life 50(4-5):301-307.
    • (2000) IUBMB Life , vol.50 , Issue.4-5 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 38
    • 84870485110 scopus 로고    scopus 로고
    • Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen
    • Weigandt KM, et al. (2012) Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen. Biophys J 103(11):2399-2407.
    • (2012) Biophys J , vol.103 , Issue.11 , pp. 2399-2407
    • Weigandt, K.M.1
  • 39
    • 0141905917 scopus 로고    scopus 로고
    • Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
    • Chapman AL, Winterbourn CC, Brennan SO, Jordan TW, Kettle AJ (2003) Characterization of non-covalent oligomers of proteins treated with hypochlorous acid. Biochem J 375(Pt 1):33-40.
    • (2003) Biochem J , vol.375 , Issue.PART 1 , pp. 33-40
    • Chapman, A.L.1    Winterbourn, C.C.2    Brennan, S.O.3    Jordan, T.W.4    Kettle, A.J.5
  • 40
    • 0028030788 scopus 로고
    • Oxidation of low-density lipoprotein by hypochlorite causes aggregation that is mediated by modification of lysine residues rather than lipid oxidation
    • Hazell LJ, van den Berg JJ, Stocker R (1994) Oxidation of low-density lipoprotein by hypochlorite causes aggregation that is mediated by modification of lysine residues rather than lipid oxidation. Biochem J 302(Pt 1):297-304.
    • (1994) Biochem J , vol.302 , Issue.PART 1 , pp. 297-304
    • Hazell, L.J.1    Van Den Berg, J.J.2    Stocker, R.3
  • 41
    • 0018690723 scopus 로고
    • Heat-induced fragmentation of human α2- macroglobulin
    • Harpel PC, Hayes MB, Hugli TE (1979) Heat-induced fragmentation of human α2- macroglobulin. J Biol Chem 254(17):8669-8678.
    • (1979) J Biol Chem , vol.254 , Issue.17 , pp. 8669-8678
    • Harpel, P.C.1    Hayes, M.B.2    Hugli, T.E.3
  • 42
    • 0037066773 scopus 로고    scopus 로고
    • Distinct binding sites in the structure of α 2-macroglobulin mediate the interaction with β-Amyloid peptide and growth factors
    • Mettenburg JM, Webb DJ, Gonias SL (2002) Distinct binding sites in the structure of α 2-macroglobulin mediate the interaction with β-Amyloid peptide and growth factors. J Biol Chem 277(15):13338-13345.
    • (2002) J Biol Chem , vol.277 , Issue.15 , pp. 13338-13345
    • Mettenburg, J.M.1    Webb, D.J.2    Gonias, S.L.3
  • 43
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms
    • Deane R, et al. (2004) LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. Neuron 43(3):333-344.
    • (2004) Neuron , vol.43 , Issue.3 , pp. 333-344
    • Deane, R.1
  • 44
    • 84867392697 scopus 로고    scopus 로고
    • Decreased expression and increased oxidation of plasma haptoglobin in Alzheimer disease: Insights from redox proteomics
    • Cocciolo A, et al. (2012) Decreased expression and increased oxidation of plasma haptoglobin in Alzheimer disease: Insights from redox proteomics. Free Radic Biol Med 53(10):1868-1876.
    • (2012) Free Radic Biol Med , vol.53 , Issue.10 , pp. 1868-1876
    • Cocciolo, A.1
  • 45
    • 84867132934 scopus 로고    scopus 로고
    • Myeloperoxidase and oxidative stress in rheumatoid arthritis
    • Stamp LK, et al. (2012) Myeloperoxidase and oxidative stress in rheumatoid arthritis. Rheumatology (Oxford) 51(10):1796-1803.
    • (2012) Rheumatology (Oxford) , vol.51 , Issue.10 , pp. 1796-1803
    • Stamp, L.K.1
  • 46
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 47
    • 0021825352 scopus 로고
    • Generation of free radical intermediates from foreign compounds by neutrophil-derived oxidants
    • Kalyanaraman B, Sohnle PG (1985) Generation of free radical intermediates from foreign compounds by neutrophil-derived oxidants. J Clin Invest 75(5):1618-1622.
    • (1985) J Clin Invest , vol.75 , Issue.5 , pp. 1618-1622
    • Kalyanaraman, B.1    Sohnle, P.G.2
  • 48
    • 0025304539 scopus 로고
    • Rheumatoid arthritis. Pathophysiology and implications for therapy
    • Harris ED, Jr. (1990) Rheumatoid arthritis. Pathophysiology and implications for therapy. N Engl J Med 322(18):1277-1289.
    • (1990) N Engl J Med , vol.322 , Issue.18 , pp. 1277-1289
    • Harris Jr., E.D.1
  • 49
    • 0031024294 scopus 로고    scopus 로고
    • Immunological evidence for hypochlorite-modified proteins in human kidney
    • Malle E, et al. (1997) Immunological evidence for hypochlorite-modified proteins in human kidney. Am J Pathol 150(2):603-615.
    • (1997) Am J Pathol , vol.150 , Issue.2 , pp. 603-615
    • Malle, E.1
  • 50
    • 34548414670 scopus 로고    scopus 로고
    • Myeloperoxidase and chlorinated peptides in osteoarthritis: Potential biomarkers of the disease
    • Steinbeck MJ, Nesti LJ, Sharkey PF, Parvizi J (2007) Myeloperoxidase and chlorinated peptides in osteoarthritis: Potential biomarkers of the disease. J Orthop Res 25(9): 1128-1135.
    • (2007) J Orthop Res , vol.25 , Issue.9 , pp. 1128-1135
    • Steinbeck, M.J.1    Nesti, L.J.2    Sharkey, P.F.3    Parvizi, J.4
  • 51
    • 0037372157 scopus 로고    scopus 로고
    • 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: Association with adverse respiratory outcome
    • Buss IH, et al. (2003) 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: Association with adverse respiratory outcome. Pediatr Res 53(3):455-462.
    • (2003) Pediatr Res , vol.53 , Issue.3 , pp. 455-462
    • Buss, I.H.1
  • 53
    • 79951669207 scopus 로고    scopus 로고
    • The immune system in atherosclerosis
    • Hansson GK, Hermansson A (2011) The immune system in atherosclerosis. Nat Immunol 12(3):204-212.
    • (2011) Nat Immunol , vol.12 , Issue.3 , pp. 204-212
    • Hansson, G.K.1    Hermansson, A.2
  • 54
  • 55
    • 23844458614 scopus 로고    scopus 로고
    • The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin
    • Yerbury JJ, Rybchyn MS, Easterbrook-Smith SB, Henriques C, Wilson MR (2005) The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin. Biochemistry 44(32):10914-10925.
    • (2005) Biochemistry , vol.44 , Issue.32 , pp. 10914-10925
    • Yerbury, J.J.1    Rybchyn, M.S.2    Easterbrook-Smith, S.B.3    Henriques, C.4    Wilson, M.R.5
  • 56
    • 0028981330 scopus 로고
    • α-Crystallin can act as a chaperone under conditions of oxidative stress
    • Wang K, Spector A (1995) α-Crystallin can act as a chaperone under conditions of oxidative stress. Invest Ophthalmol Vis Sci 36(2):311-321.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , Issue.2 , pp. 311-321
    • Wang, K.1    Spector, A.2
  • 57
    • 1942423136 scopus 로고    scopus 로고
    • Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone
    • Hoppe G, Chai YC, Crabb JW, Sears J (2004) Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. Exp Eye Res 78(6):1085-1092.
    • (2004) Exp Eye Res , vol.78 , Issue.6 , pp. 1085-1092
    • Hoppe, G.1    Chai, Y.C.2    Crabb, J.W.3    Sears, J.4
  • 58
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redoxdependent molecular chaperone that inhibits alpha-synuclein aggregate formation
    • Shendelman S, Jonason A, Martinat C, Leete T, Abeliovich A (2004) DJ-1 is a redoxdependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol 2(11):e362.
    • (2004) PLoS Biol , vol.2 , Issue.11
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 59
    • 84862907646 scopus 로고    scopus 로고
    • Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a
    • Wang C, et al. (2012) Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a. J Biol Chem 287(2):1139-1149.
    • (2012) J Biol Chem , vol.287 , Issue.2 , pp. 1139-1149
    • Wang, C.1
  • 60
    • 39849097748 scopus 로고    scopus 로고
    • Redox regulation in the extracellular environment
    • Ottaviano FG, Handy DE, Loscalzo J (2008) Redox regulation in the extracellular environment. Circ J 72(1):1-16.
    • (2008) Circ J , vol.72 , Issue.1 , pp. 1-16
    • Ottaviano, F.G.1    Handy, D.E.2    Loscalzo, J.3
  • 61
    • 22144433040 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases B1 B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells
    • Marchetti MA, et al. (2005) Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells. Invest Ophthalmol Vis Sci 46(6):2107-2112.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , Issue.6 , pp. 2107-2112
    • Marchetti, M.A.1
  • 62
    • 38149134449 scopus 로고    scopus 로고
    • Neutrophil granulocytes uniquely express, among human blood cells, high levels of Methionine-sulfoxidereductase enzymes
    • Achilli C, Ciana A, Rossi A, Balduini C, Minetti G (2008) Neutrophil granulocytes uniquely express, among human blood cells, high levels of Methionine-sulfoxidereductase enzymes. J Leukoc Biol 83(1):181-189.
    • (2008) J Leukoc Biol , vol.83 , Issue.1 , pp. 181-189
    • Achilli, C.1    Ciana, A.2    Rossi, A.3    Balduini, C.4    Minetti, G.5
  • 63
    • 0031915142 scopus 로고    scopus 로고
    • Bait region involvement in the dimer-dimer interface of human α2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides
    • Bowen ME, Gettins PGW (1998) Bait region involvement in the dimer-dimer interface of human α2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides. J Biol Chem 273(3):1825-1831.
    • (1998) J Biol Chem , vol.273 , Issue.3 , pp. 1825-1831
    • Bowen, M.E.1    Pgw, G.2
  • 64
    • 84859258162 scopus 로고    scopus 로고
    • The crystal structure of human α2-macroglobulin reveals a unique molecular cage
    • Marrero A, et al. (2012) The crystal structure of human α2-macroglobulin reveals a unique molecular cage. Angew Chem Int Ed Engl 51(14):3340-3344.
    • (2012) Angew Chem Int Ed Engl , vol.51 , Issue.14 , pp. 3340-3344
    • Marrero, A.1
  • 65
    • 84858972803 scopus 로고    scopus 로고
    • Therapeutic effects of systemic administration of chaperone alpha;B -crystallin associated with binding proinflammatory plasma proteins
    • Rothbard JB, et al. (2012) Therapeutic effects of systemic administration of chaperone alpha;B-crystallin associated with binding proinflammatory plasma proteins. J Biol Chem 287(13):9708-9721.
    • (2012) J Biol Chem , vol.287 , Issue.13 , pp. 9708-9721
    • Rothbard, J.B.1
  • 66
    • 84878880617 scopus 로고    scopus 로고
    • Acute phase proteins are major clients for the chaperone action of ?-macroglobulin in human plasma
    • Wyatt AR, Zammit NW, Wilson MR (2013) Acute phase proteins are major clients for the chaperone action of α-macroglobulin in human plasma. Cell Stress Chaperones 18(2):161-170.
    • (2013) Cell Stress Chaperones , vol.18 , Issue.2 , pp. 161-170
    • Wyatt, A.R.1    Zammit, N.W.2    Wilson, M.R.3
  • 67
    • 77949292454 scopus 로고    scopus 로고
    • Identification of human plasma proteins as major clients for the extracellular chaperone clusterin
    • Wyatt AR, Wilson MR (2010) Identification of human plasma proteins as major clients for the extracellular chaperone clusterin. J Biol Chem 285(6):3532-3539.
    • (2010) J Biol Chem , vol.285 , Issue.6 , pp. 3532-3539
    • Wyatt, A.R.1    Wilson, M.R.2
  • 68
    • 84873442839 scopus 로고    scopus 로고
    • Widespread regulation of translation by elongation pausing in heat shock
    • Shalgi R, et al. (2013) Widespread regulation of translation by elongation pausing in heat shock. Mol Cell 49(3):439-452.
    • (2013) Mol Cell , vol.49 , Issue.3 , pp. 439-452
    • Shalgi, R.1
  • 69
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • Morimoto RI (1993) Cells in stress: Transcriptional activation of heat shock genes. Science 259(5100):1409-1410.
    • (1993) Science , vol.259 , Issue.5100 , pp. 1409-1410
    • Morimoto, R.I.1
  • 72
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: An ancient damage-Associated molecular pattern that initiates innate immune responses
    • Seong SY, Matzinger P (2004) Hydrophobicity: An ancient damage-Associated molecular pattern that initiates innate immune responses. Nat Rev Immunol 4(6): 469-478.
    • (2004) Nat Rev Immunol , vol.4 , Issue.6 , pp. 469-478
    • Seong, S.Y.1    Matzinger, P.2
  • 73
    • 0022337471 scopus 로고
    • Self-perpetuating mechanisms of immunoglobulin G aggregation in rheumatoid inflammation
    • Lunec J, Blake DR, McCleary SJ, Brailsford S, Bacon PA (1985) Self-perpetuating mechanisms of immunoglobulin G aggregation in rheumatoid inflammation. J Clin Invest 76(6):2084-2090.
    • (1985) J Clin Invest , vol.76 , Issue.6 , pp. 2084-2090
    • Lunec, J.1    Blake, D.R.2    McCleary, S.J.3    Brailsford, S.4    Bacon, P.A.5
  • 74
    • 18844471606 scopus 로고    scopus 로고
    • Advanced oxidation protein products as novel mediators of inflammation and monocyte activation in chronic renal failure
    • Witko-Sarsat V, et al. (1998) Advanced oxidation protein products as novel mediators of inflammation and monocyte activation in chronic renal failure. J Immunol 161(5): 2524-2532.
    • (1998) J Immunol , vol.161 , Issue.5 , pp. 2524-2532
    • Witko-Sarsat, V.1
  • 75
    • 0033527446 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein induces macrophage respiratory burst via its protein moiety: A novel pathway in atherogenesis?
    • Nguyen-Khoa T, et al. (1999) Oxidized low-density lipoprotein induces macrophage respiratory burst via its protein moiety: A novel pathway in atherogenesis? Biochem Biophys Res Commun 263(3):804-809.
    • (1999) Biochem Biophys Res Commun , vol.263 , Issue.3 , pp. 804-809
    • Nguyen-Khoa, T.1
  • 76
    • 77953077457 scopus 로고    scopus 로고
    • Aggregates of denatured proteins stimulate nitric oxide and superoxide production in macrophages
    • Jozefowski S, Marcinkiewicz J (2010) Aggregates of denatured proteins stimulate nitric oxide and superoxide production in macrophages. Inflamm Res 59(4):277-289.
    • (2010) Inflamm Res , vol.59 , Issue.4 , pp. 277-289
    • Jozefowski, S.1    Marcinkiewicz, J.2
  • 77
    • 61349088546 scopus 로고    scopus 로고
    • Inflammation in Alzheimers disease: Amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors
    • Salminen A, Ojala J, Kauppinen A, Kaarniranta K, Suuronen T (2009) Inflammation in Alzheimers disease: Amyloid-beta oligomers trigger innate immunity defence via pattern recognition receptors. Prog Neurobiol 87(3):181-194.
    • (2009) Prog Neurobiol , vol.87 , Issue.3 , pp. 181-194
    • Salminen, A.1    Ojala, J.2    Kauppinen, A.3    Kaarniranta, K.4    Suuronen, T.5
  • 78
    • 65949116826 scopus 로고    scopus 로고
    • Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate
    • Yanamandra K, et al. (2009) Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate. PLoS ONE 4(5):e5562.
    • (2009) PLoS ONE , vol.4 , Issue.5
    • Yanamandra, K.1
  • 79
    • 55249087467 scopus 로고    scopus 로고
    • Immunological features of alphasynuclein in Parkinsons disease
    • Roodveldt C, Christodoulou J, Dobson CM (2008) Immunological features of alphasynuclein in Parkinsons disease. J Cell Mol Med 12(5B):1820-1829.
    • (2008) J Cell Mol Med , vol.12 , Issue.5 , pp. 1820-1829
    • Roodveldt, C.1    Christodoulou, J.2    Dobson, C.M.3
  • 80
    • 79955156438 scopus 로고    scopus 로고
    • Disease-Associated amyloid and misfolded protein aggregates activate the inflammasome
    • Masters SL, ONeill LA (2011) Disease-Associated amyloid and misfolded protein aggregates activate the inflammasome. Trends Mol Med 17(5):276-282.
    • (2011) Trends Mol Med , vol.17 , Issue.5 , pp. 276-282
    • Masters, S.L.1    Oneill, L.A.2
  • 81
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5 to 35
    • Morris JC (1966) The acid ionization constant of HOCl from 5 to 35. J Phys Chem 70(12):3798-3805.
    • (1966) J Phys Chem , vol.70 , Issue.12 , pp. 3798-3805
    • Morris, J.C.1
  • 82
    • 0025786502 scopus 로고
    • 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/α2-macroglobulin receptor
    • Herz J, Goldstein JL, Strickland DK, Ho YK, Brown MS (1991) 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/α2-macroglobulin receptor. J Biol Chem 266(31):21232-21238.
    • (1991) J Biol Chem , vol.266 , Issue.31 , pp. 21232-21238
    • Herz, J.1    Goldstein, J.L.2    Strickland, D.K.3    Ho, Y.K.4    Brown, M.S.5


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