메뉴 건너뛰기




Volumn 184, Issue 2, 2010, Pages 824-835

Hypochlorous acid: A natural adjuvant that facilitates antigen processing, cross-priming, and the induction of adaptive immunity

Author keywords

[No Author keywords available]

Indexed keywords

ADJUVANT; ALDEHYDE; CARBOHYDRATE; CD161 ANTIGEN; CHLORAMINE DERIVATIVE; GLYCOPROTEIN; HYPOCHLOROUS ACID; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OVALBUMIN; TOLL LIKE RECEPTOR; TYROSINASE RELATED PROTEIN 2; HLA ANTIGEN CLASS 2; IMMUNOLOGICAL ADJUVANT; LOW DENSITY LIPOPROTEIN RECEPTOR;

EID: 76249105638     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0902606     Document Type: Article
Times cited : (301)

References (48)
  • 1
    • 0029987839 scopus 로고    scopus 로고
    • The instructive role of innate immunity in the acquired immune response
    • Fearon, D. T., and R. M. Locksley. 1996. The instructive role of innate immunity in the acquired immune response. Science 272: 50-53.
    • (1996) Science , vol.272 , pp. 50-53
    • Fearon, D.T.1    Locksley, R.M.2
  • 2
    • 27844541797 scopus 로고    scopus 로고
    • Control of B-cell responses by Toll-like receptors
    • Pasare, C., and R. Medzhitov. 2005. Control of B-cell responses by Toll-like receptors. Nature 438: 364-368.
    • (2005) Nature , vol.438 , pp. 364-368
    • Pasare, C.1    Medzhitov, R.2
  • 3
    • 45749111446 scopus 로고    scopus 로고
    • Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
    • Eisenbarth, S. C., O. R. Colegio, W. O'Connor, F. S. Sutterwala, and R. A. Flavell. 2008. Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants. Nature 453: 1122-1126.
    • (2008) Nature , vol.453 , pp. 1122-1126
    • Eisenbarth, S.C.1    Colegio, O.R.2    O'Connor, W.3    Sutterwala, F.S.4    Flavell, R.A.5
  • 4
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α
    • Sallusto, F., and A. Lanzavecchia. 1994. Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α. J. Exp. Med. 179: 1109-1118.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 5
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta, E. S., M. Ebersold, W. Garrett, M. Pypaert, and I. Mellman. 2003. Activation of lysosomal function during dendritic cell maturation. Science 299: 1400-1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 6
    • 0030745046 scopus 로고    scopus 로고
    • Interleukin 1β and the stimulation of Langerhans cell migration: Comparisons with tumour necrosis factor α
    • Cumberbatch, M., R. J. Dearman, and I. Kimber. 1997. Interleukin 1β and the stimulation of Langerhans cell migration: comparisons with tumour necrosis factor α. Arch. Dermatol. Res. 289: 277-284.
    • (1997) Arch. Dermatol. Res. , vol.289 , pp. 277-284
    • Cumberbatch, M.1    Dearman, R.J.2    Kimber, I.3
  • 7
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta, E. S., and I. Mellman. 2005. Cell biology of antigen processing in vitro and in vivo. Annu. Rev. Immunol. 23: 975-1028.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 8
    • 33645734929 scopus 로고    scopus 로고
    • Toll-dependent selection of microbial antigens for presentation by dendritic cells
    • Blander, J. M., and R. Medzhitov. 2006. Toll-dependent selection of microbial antigens for presentation by dendritic cells. Nature 440: 808-812.
    • (2006) Nature , vol.440 , pp. 808-812
    • Blander, J.M.1    Medzhitov, R.2
  • 10
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S. J. 2005. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77: 598-625.
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 11
    • 33646826643 scopus 로고    scopus 로고
    • Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid
    • Malle, E., G. Marsche, J. Arnhold, and M. J. Davies. 2006. Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid. Biochim. Biophys. Acta 1761: 392-415.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 392-415
    • Malle, E.1    Marsche, G.2    Arnhold, J.3    Davies, M.J.4
  • 12
    • 27144440590 scopus 로고    scopus 로고
    • Inactivation of protease inhibitors and lysozyme by hypochlorous acid: Role of side-chain oxidation and protein unfolding in loss of biological function
    • Hawkins, C. L., and M. J. Davies. 2005. Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function. Chem. Res. Toxicol. 18: 1600-1610.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1600-1610
    • Hawkins, C.L.1    Davies, M.J.2
  • 13
    • 0344393610 scopus 로고    scopus 로고
    • Fragmentation of extracellular matrix by hypochlorous acid
    • Woods, A. A., and M. J. Davies. 2003. Fragmentation of extracellular matrix by hypochlorous acid. Biochem. J. 376: 219-227.
    • (2003) Biochem. J. , vol.376 , pp. 219-227
    • Woods, A.A.1    Davies, M.J.2
  • 14
    • 0036049974 scopus 로고    scopus 로고
    • Effects of oxidised low density lipoprotein on dendritic cells: A possible immunoregulatory component of the atherogenic micro-environment?
    • Alderman, C. J., P. R. Bunyard, B. M. Chain, J. C. Foreman, D. S. Leake, and D. R. Katz. 2002. Effects of oxidised low density lipoprotein on dendritic cells: a possible immunoregulatory component of the atherogenic micro-environment? Cardiovasc. Res. 55: 806-819.
    • (2002) Cardiovasc. Res. , vol.55 , pp. 806-819
    • Alderman, C.J.1    Bunyard, P.R.2    Chain, B.M.3    Foreman, J.C.4    Leake, D.S.5    Katz, D.R.6
  • 16
    • 0031897801 scopus 로고    scopus 로고
    • Defective TCR expression in transgenic mice constructed using cDNA-based α- and β-chain genes under the control of heterologous regulatory elements
    • Barnden, M. J., J. Allison, W. R. Heath, and F. R. Carbone. 1998. Defective TCR expression in transgenic mice constructed using cDNA-based α- and β-chain genes under the control of heterologous regulatory elements. Immunol. Cell Biol. 76: 34-40.
    • (1998) Immunol. Cell Biol. , vol.76 , pp. 34-40
    • Barnden, M.J.1    Allison, J.2    Heath, W.R.3    Carbone, F.R.4
  • 17
    • 33744801689 scopus 로고    scopus 로고
    • Mannose-pepstatin conjugates as targeted inhibitors of antigen processing
    • Free, P., C. A. Hurley, T. Kageyama, B. M. Chain, and A. B. Tabor. 2006. Mannose-pepstatin conjugates as targeted inhibitors of antigen processing. Org. Biomol. Chem. 4: 1817-1830.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 1817-1830
    • Free, P.1    Hurley, C.A.2    Kageyama, T.3    Chain, B.M.4    Tabor, A.B.5
  • 19
    • 0028219162 scopus 로고
    • A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels
    • Nesterenko, M. V., M. Tilley, and S. J. Upton. 1994. A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 28: 239-242.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, M.2    Upton, S.J.3
  • 20
    • 34548206228 scopus 로고    scopus 로고
    • Hypochlorous acid-mediated protein oxidation: How important are chloramine transfer reactions and protein tertiary structure?
    • Pattison, D. I., C. L. Hawkins, and M. J. Davies. 2007. Hypochlorous acid-mediated protein oxidation: how important are chloramine transfer reactions and protein tertiary structure? Biochemistry 46: 9853-9864.
    • (2007) Biochemistry , vol.46 , pp. 9853-9864
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 21
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman, E. R., and R. L. Levine. 2003. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25: 207-218.
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 23
    • 0033793249 scopus 로고    scopus 로고
    • Enhanced immunogenicity of aldehyde-bearing antigens: A possible link between innate and adaptive immunity
    • Allison, M. E., and D. T. Fearon. 2000. Enhanced immunogenicity of aldehyde-bearing antigens: a possible link between innate and adaptive immunity. Eur. J. Immunol. 30: 2881-2887.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2881-2887
    • Allison, M.E.1    Fearon, D.T.2
  • 25
    • 0034477636 scopus 로고    scopus 로고
    • Composition of N-linked carbohydrates from ovalbumin and co-purified glycoproteins
    • Harvey, D. J., D. R. Wing, B. Küster, and I. B. Wilson. 2000. Composition of N-linked carbohydrates from ovalbumin and co-purified glycoproteins. J. Am. Soc. Mass Spectrom. 11: 564-571.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 564-571
    • Harvey, D.J.1    Wing, D.R.2    Küster, B.3    Wilson, I.B.4
  • 26
    • 2342585497 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization tandem mass spectrometry and post-source decay fragmentation study of phenylhydrazones of N-linked oligosaccharides from ovalbumin
    • Lattova, E., H. Perreault, and O. Krokhin. 2004. Matrix-assisted laser desorption/ionization tandem mass spectrometry and post-source decay fragmentation study of phenylhydrazones of N-linked oligosaccharides from ovalbumin. J. Am. Soc. Mass Spectrom. 15: 725-735.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 725-735
    • Lattova, E.1    Perreault, H.2    Krokhin, O.3
  • 27
    • 0032714086 scopus 로고    scopus 로고
    • The reaction of hyaluronic acid and its monomers, glucuronic acid and N-acetylglucosamine, with reactive oxygen species
    • Jahn, M., J. W. Baynes, and G. Spiteller. 1999. The reaction of hyaluronic acid and its monomers, glucuronic acid and N-acetylglucosamine, with reactive oxygen species. Carbohydr. Res. 321: 228-234.
    • (1999) Carbohydr. Res. , vol.321 , pp. 228-234
    • Jahn, M.1    Baynes, J.W.2    Spiteller, G.3
  • 28
    • 0019474658 scopus 로고
    • Studies on the capacity of B cells to serve as antigen-presenting cells
    • Chesnut, R. W., and H. M. Grey. 1981. Studies on the capacity of B cells to serve as antigen-presenting cells. J. Immunol. 126: 1075-1079.
    • (1981) J. Immunol. , vol.126 , pp. 1075-1079
    • Chesnut, R.W.1    Grey, H.M.2
  • 30
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P., and Y. F. Dufrêne. 2006. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3: 347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrêne, Y.F.2
  • 32
    • 38749118269 scopus 로고    scopus 로고
    • The lectin-like oxidized low-density-lipoprotein receptor: A pro-inflammatory factor in vascular disease
    • Dunn, S., R. S. Vohra, J. E. Murphy, S. Homer-Vanniasinkam, J. H. Walker, and S. Ponnambalam. 2008. The lectin-like oxidized low-density-lipoprotein receptor: a pro-inflammatory factor in vascular disease. Biochem. J. 409: 349-355.
    • (2008) Biochem. J. , vol.409 , pp. 349-355
    • Dunn, S.1    Vohra, R.S.2    Murphy, J.E.3    Homer-Vanniasinkam, S.4    Walker, J.H.5    Ponnambalam, S.6
  • 33
    • 36148941000 scopus 로고    scopus 로고
    • Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: An oxidative mechanism for regulating proteolysis during inflammation
    • Wang, Y., H. Rosen, D. K. Madtes, B. Shao, T. R. Martin, J. W. Heinecke, and X. Fu. 2007. Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: an oxidative mechanism for regulating proteolysis during inflammation. J. Biol. Chem. 282: 31826-31834.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31826-31834
    • Wang, Y.1    Rosen, H.2    Madtes, D.K.3    Shao, B.4    Martin, T.R.5    Heinecke, J.W.6    Fu, X.7
  • 35
    • 0026777691 scopus 로고
    • Enhancement of trinitrophenyl-specific humoral response to TNP proteins as the result of carrier chlorination
    • Marcinkiewicz, J., E. Olszowska, S. Olszowski, and J. M. Zgliczynski. 1992. Enhancement of trinitrophenyl-specific humoral response to TNP proteins as the result of carrier chlorination. Immunology 76: 385-388.
    • (1992) Immunology , vol.76 , pp. 385-388
    • Marcinkiewicz, J.1    Olszowska, E.2    Olszowski, S.3    Zgliczynski, J.M.4
  • 37
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • Chapman, A. L., M. B. Hampton, R. Senthilmohan, C. C. Winterbourn, and A. J. Kettle. 2002. Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. J. Biol. Chem. 277: 9757-9762.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9757-9762
    • Chapman, A.L.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 38
    • 70149091118 scopus 로고    scopus 로고
    • Neutrophil bleaching of GFP-expressing staphylococci: Probing the intraphagosomal fate of individual bacteria
    • Schwartz, J., K. G. Leidal, J. K. Femling, J. P. Weiss, and W. M. Nauseef. 2009. Neutrophil bleaching of GFP-expressing staphylococci: probing the intraphagosomal fate of individual bacteria. J. Immunol. 183: 2632-2641.
    • (2009) J. Immunol. , vol.183 , pp. 2632-2641
    • Schwartz, J.1    Leidal, K.G.2    Femling, J.K.3    Weiss, J.P.4    Nauseef, W.M.5
  • 39
    • 4344577056 scopus 로고    scopus 로고
    • Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
    • Zheng, L., B. Nukuna, M. L. Brennan, M. Sun, M. Goormastic, M. Settle, D. Schmitt, X. Fu, L. Thomson, P. L. Fox, et al. 2004. Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J. Clin. Invest. 114: 529-541.
    • (2004) J. Clin. Invest. , vol.114 , pp. 529-541
    • Zheng, L.1    Nukuna, B.2    Brennan, M.L.3    Sun, M.4    Goormastic, M.5    Settle, M.6    Schmitt, D.7    Fu, X.8    Thomson, L.9    Fox, P.L.10
  • 42
    • 23844495082 scopus 로고    scopus 로고
    • Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: An oxidative mechanism for regulation of serine proteinases by myeloperoxidase
    • Shao, B., A. Belaaouaj, C. L. Verlinde, X. Fu, and J. W. Heinecke. 2005. Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase. J. Biol. Chem. 280: 29311-29321.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29311-29321
    • Shao, B.1    Belaaouaj, A.2    Verlinde, C.L.3    Fu, X.4    Heinecke, J.W.5
  • 43
    • 58949087905 scopus 로고    scopus 로고
    • Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation
    • Hawkins, C. L., D. I. Pattison, N. R. Stanley, and M. J. Davies. 2008. Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation. Biochem. J. 416: 441-452.
    • (2008) Biochem. J. , vol.416 , pp. 441-452
    • Hawkins, C.L.1    Pattison, D.I.2    Stanley, N.R.3    Davies, M.J.4
  • 44
    • 0033151902 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of proteins in plasma: Formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
    • Hawkins, C. L., and M. J. Davies. 1999. Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation. Biochem. J. 340: 539-548.
    • (1999) Biochem. J. , vol.340 , pp. 539-548
    • Hawkins, C.L.1    Davies, M.J.2
  • 45
    • 0242407243 scopus 로고    scopus 로고
    • Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: Evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation
    • Rees, M. D., C. L. Hawkins, and M. J. Davies. 2003. Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation. J. Am. Chem. Soc. 125: 13719-13733.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13719-13733
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 46
    • 33746894710 scopus 로고    scopus 로고
    • Hypochlorous acid enhances immunogenicity and uptake of allogeneic ovarian tumor cells by dendritic cells to cross-prime tumor-specific T cells
    • Chiang, C. L., J. A. Ledermann, A. N. Rad, D. R. Katz, and B. M. Chain. 2006. Hypochlorous acid enhances immunogenicity and uptake of allogeneic ovarian tumor cells by dendritic cells to cross-prime tumor-specific T cells. Cancer Immunol. Immunother. 55: 1384-1395.
    • (2006) Cancer Immunol. Immunother. , vol.55 , pp. 1384-1395
    • Chiang, C.L.1    Ledermann, J.A.2    Rad, A.N.3    Katz, D.R.4    Chain, B.M.5
  • 47
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • Delamarre, L., R. Couture, I. Mellman, and E. S. Trombetta. 2006. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J. Exp. Med. 203: 2049-2055.
    • (2006) J. Exp. Med. , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 48
    • 51049094007 scopus 로고    scopus 로고
    • Oxidation of ovarian epithelial cancer cells by hypochlorous acid enhances immunogenicity and stimulates T cells that recognize autologous primary tumor
    • Chiang, C. L., J. A. Ledermann, E. Aitkens, E. Benjamin, D. R. Katz, and B. M. Chain. 2008. Oxidation of ovarian epithelial cancer cells by hypochlorous acid enhances immunogenicity and stimulates T cells that recognize autologous primary tumor. Clin. Cancer Res. 14: 4898-4907.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 4898-4907
    • Chiang, C.L.1    Ledermann, J.A.2    Aitkens, E.3    Benjamin, E.4    Katz, D.R.5    Chain, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.