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Volumn 4, Issue , 2014, Pages

Changes in IgG and total plasma protein glycomes in acute systemic inflammation

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLATED IGG; IMMUNOGLOBULIN G; POLYSACCHARIDE;

EID: 84896320475     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep04347     Document Type: Article
Times cited : (121)

References (52)
  • 1
    • 0027360634 scopus 로고
    • Concepts and principles of glycobiology
    • Opdenakker, G., Rudd, P. M., Ponting, C. P. & Dwek, R. A. Concepts and principles of glycobiology. FASEB J 7, 1330-1337 (1993). (Pubitemid 23336160)
    • (1993) FASEB Journal , vol.7 , Issue.14 , pp. 1330-1337
    • Opdenakker, G.1    Rudd, P.M.2    Ponting, C.P.3    Dwek, R.A.4
  • 2
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • Moremen, K. W., Tiemeyer, M. & Nairn, A. V. Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol 13, 448-462 (2012).
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 3
    • 63149160691 scopus 로고    scopus 로고
    • The effect of individual N-glycans on enzyme activity
    • Skropeta, D. The effect of individual N-glycans on enzyme activity. Bioorg Med Chem 17, 2645-2653 (2009).
    • (2009) Bioorg Med Chem , vol.17 , pp. 2645-2653
    • Skropeta, D.1
  • 4
    • 44849133511 scopus 로고    scopus 로고
    • Sweet and sour: The impact of sugars on disease
    • DOI 10.1093/rheumatology/ken081
    • Alavi, A. & Axford, J. S. Sweet and sour: the impact of sugars on disease. Rheumatology (Oxford) 47, 760-770 (2008). (Pubitemid 351796358)
    • (2008) Rheumatology , vol.47 , Issue.6 , pp. 760-770
    • Alavi, A.1    Axford, J.S.2
  • 5
    • 84862843922 scopus 로고    scopus 로고
    • Alternative glycosylation modulates function of IgG and other proteins - Implications on evolution and disease
    • Gornik, O., Pavic, T. & Lauc, G. Alternative glycosylation modulates function of IgG and other proteins - Implications on evolution and disease. Biochim Biophys Acta 1820, 1318-1326 (2012).
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1318-1326
    • Gornik, O.1    Pavic, T.2    Lauc, G.3
  • 6
    • 0035937526 scopus 로고    scopus 로고
    • Glycosylation and the immune system
    • DOI 10.1126/science.291.5512.2370
    • Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A. & Dwek, R. A. Glycosylation and the immune system. Science 291, 2370-2376. (2001). (Pubitemid 32231792)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2370-2376
    • Rudd, P.M.1    Elliott, T.2    Cresswell, P.3    Wilson, I.A.4    Dwek, R.A.5
  • 8
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • DOI 10.1021/bp040016j
    • Jefferis, R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 21, 11-16 (2005). (Pubitemid 40218466)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 11-16
    • Jefferis, R.1
  • 9
    • 84868642198 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcgammaRIIB and dectin-1
    • Karsten, C. M. et al. Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcgammaRIIB and dectin-1. Nat Med (2012).
    • (2012) Nat Med
    • Karsten, C.M.1
  • 11
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcγRIIIa Asn-162: An element required for high affinity binding to non-fucosylated IgG glycoforms
    • DOI 10.1074/jbc.M510171200
    • Ferrara, C., Stuart, F., Sondermann, P., Brunker, P. & Umana, P. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to nonfucosylated IgG glycoforms. J Biol Chem 281, 5032-5036 (2006). (Pubitemid 43847767)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brunker, P.4    Umana, P.5
  • 13
    • 33646740982 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa
    • Iida, S. et al. Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa. Clin Cancer Res 12, 2879-2887 (2006).
    • (2006) Clin Cancer Res , vol.12 , pp. 2879-2887
    • Iida, S.1
  • 14
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Kaneko, Y., Nimmerjahn, F. & Ravetch, J. V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313, 670-673 (2006). (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 15
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: The antiinflammatory activity of sialylated IgG Fcs
    • Anthony, R. M. & Ravetch, J. V. A novel role for the IgG Fc glycan: the antiinflammatory activity of sialylated IgG Fcs. J Clin Immunol 30 Suppl 1, , S9-14 (2010).
    • (2010) J Clin Immunol , vol.30 , Issue.SUPPL. 1
    • Anthony, R.M.1    Ravetch, J.V.2
  • 16
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony, R.M., Wermeling, F., Karlsson, M. C. & Ravetch, J. V. Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc Natl Acad Sci USA 105, 19571-19578 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 17
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H) 2 pathway
    • Anthony, R. M., Kobayashi, T., Wermeling, F. & Ravetch, J. V. Intravenous gammaglobulin suppresses inflammation through a novel T(H) 2 pathway. Nature 475, 110-113 (2011).
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 18
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • DOI 10.1126/science.1154315
    • Anthony, R. M., Nimmerjahn, F., Ashline, D. J., Reinhold, V. N., Paulson, J. C. & Ravetch, J. V. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320, 373-376 (2008). (Pubitemid 351555659)
    • (2008) Science , vol.320 , Issue.5874 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3    Reinhold, V.N.4    Paulson, J.C.5    Ravetch, J.V.6
  • 19
    • 61849180382 scopus 로고    scopus 로고
    • Variability, heritability and environmental determinants of human plasma n-glycome
    • Knez?ević, A. et al. Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome. J Proteome Res 8, 694-701 (2009).
    • (2009) J Proteome Res , vol.8 , pp. 694-701
    • Knezević, A.1
  • 20
    • 80054016444 scopus 로고    scopus 로고
    • High throughput isolation and glycosylation analysis of IgGvariability and heritability of the IgG glycome in three isolated human populations
    • Pucic, M. et al. High throughput isolation and glycosylation analysis of IgGvariability and heritability of the IgG glycome in three isolated human populations. Mol Cell Proteomics 10, M111 010090 (2011).
    • (2011) Mol Cell Proteomics , vol.10
    • Pucic, M.1
  • 21
    • 29244470323 scopus 로고    scopus 로고
    • Modulation of systemic inflammatory response after cardiac surgery
    • Raja, S. G. & Dreyfus, G. D. Modulation of systemic inflammatory response after cardiac surgery. Asian cardiovascular & thoracic annals 13, 382-395 (2005). (Pubitemid 41824742)
    • (2005) Asian Cardiovascular and Thoracic Annals , vol.13 , Issue.4 , pp. 382-395
    • Raja, S.G.1    Dreyfus, G.D.2
  • 22
    • 0141676741 scopus 로고    scopus 로고
    • The systemic inflammatory response to cardiopulmonary bypass
    • DOI 10.1016/S0889-8537(03)00039-7
    • Pintar, T. & Collard, C. D. The systemic inflammatory response to cardiopulmonary bypass. Anesthesiology clinics of North America 21, 453-464 (2003). (Pubitemid 37169539)
    • (2003) Anesthesiology Clinics of North America , vol.21 , Issue.3 , pp. 453-464
    • Pintar, T.1    Collard, C.D.2
  • 24
    • 34249901589 scopus 로고    scopus 로고
    • Circulating inflammatory mediators and organ dysfunction after cardiovascular surgery with cardiopulmonary bypass: A prospective observational study
    • de Mendonca-Filho, H. T. et al. Circulating inflammatory mediators and organ dysfunction after cardiovascular surgery with cardiopulmonary bypass: a prospective observational study. Crit Care 10, R46 (2006).
    • (2006) Crit Care , vol.10
    • De Mendonca-Filho, H.T.1
  • 26
    • 84864309495 scopus 로고    scopus 로고
    • Management of complex cardiovascular problems: The evidence-based medicine approach
    • Hu, D. Management of complex cardiovascular problems: the evidence-based medicine approach. Wiley-Blackwel (2007).
    • (2007) Wiley-Blackwel
    • Hu, D.1
  • 28
    • 84862813662 scopus 로고    scopus 로고
    • N-glycans in liver-secreted and immunoglogulin-derived protein fractions
    • Bekesova, S. et al. N-glycans in liver-secreted and immunoglogulin- derived protein fractions. Journal of proteomics 75, 2216-2224 (2012).
    • (2012) Journal of Proteomics , vol.75 , pp. 2216-2224
    • Bekesova, S.1
  • 30
    • 84875453727 scopus 로고    scopus 로고
    • Performance analysis of EuroSCORE II compared to the original logistic EuroSCORE and STS scores for predicting 30-day mortality after transcatheter aortic valve replacement
    • Durand, E. et al. Performance analysis of EuroSCORE II compared to the original logistic EuroSCORE and STS scores for predicting 30-day mortality after transcatheter aortic valve replacement. The American journal of cardiology 111, 891-897 (2013).
    • (2013) The American Journal of Cardiology , vol.111 , pp. 891-897
    • Durand, E.1
  • 32
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • Hart, G. W. & Copeland, R. J. Glycomics hits the big time. Cell 143, 672-676 (2010).
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 33
    • 84884992503 scopus 로고    scopus 로고
    • Epigenetic regulation of glycosylation is the quantum mechanics of biology
    • Lauc, G., Vojta, A. & Zoldos, V. Epigenetic regulation of glycosylation is the quantum mechanics of biology. Biochim Biophys Acta 1840, 65-70 (2013).
    • (2013) Biochim Biophys Acta , vol.1840 , pp. 65-70
    • Lauc, G.1    Vojta, A.2    Zoldos, V.3
  • 34
    • 78149457418 scopus 로고    scopus 로고
    • Protein glycosylation - An evolutionary crossroad between genes and environment
    • Lauc, G. & Zoldos?, V. Protein glycosylation - an evolutionary crossroad between genes and environment. Mol Biosyst 6, 2373-2379 (2010).
    • (2010) Mol Biosyst , vol.6 , pp. 2373-2379
    • Lauc, G.1    Zoldos, V.2
  • 35
    • 84875264285 scopus 로고    scopus 로고
    • Glycomics meets genomics, epigenomics and other high throughput omics for system biology studies
    • Zoldos, V., Horvat, T. & Lauc, G. Glycomics meets genomics, epigenomics and other high throughput omics for system biology studies. Curr Opin Chem Biol 17, 34-40 (2013).
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 34-40
    • Zoldos, V.1    Horvat, T.2    Lauc, G.3
  • 36
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflammatory diseases
    • Gornik, O. & Lauc, G. Glycosylation of serum proteins in inflammatory diseases. Dis Markers 25, 267-278 (2008).
    • (2008) Dis Markers , vol.25 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 38
    • 41849147087 scopus 로고    scopus 로고
    • Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis
    • Gornik, O., Gornik, I., Gasparovic, V. & Lauc, G. Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis. Clin Biochem 41, 504-510 (2008).
    • (2008) Clin Biochem , vol.41 , pp. 504-510
    • Gornik, O.1    Gornik, I.2    Gasparovic, V.3    Lauc, G.4
  • 39
    • 79955563481 scopus 로고    scopus 로고
    • Change of transferrin sialylation differs between mild sepsis and severe sepsis and septic shock
    • Gornik, O., Gornik, I., Kolednjak, I. Z. & Lauc, G. Change of transferrin sialylation differs between mild sepsis and severe sepsis and septic shock. Intern Med 50, 861-869 (2011).
    • (2011) Intern Med , vol.50 , pp. 861-869
    • Gornik, O.1    Gornik, I.2    Kolednjak, I.Z.3    Lauc, G.4
  • 41
    • 0031809628 scopus 로고    scopus 로고
    • 1- antichymotrypsin and haptoglobin
    • DOI 10.1023/A:1006972307166
    • Brinkman-van der Linden, E. C., de Haan, P. F., Havenaar, E. C. & van Dijk, W. Inflammation-induced expression of sialyl LewisX is not restricted to alpha1-acid glycoprotein but also occurs to a lesser extent on alpha1-antichymotrypsin and haptoglobin. Glycoconj J 15, 177-182 (1998). (Pubitemid 28260922)
    • (1998) Glycoconjugate Journal , vol.15 , Issue.2 , pp. 177-182
    • Brinkman-Van Der Linden, E.C.M.1    De Haan, P.F.2    Havenaar, E.C.3    Van Dijk, W.4
  • 43
    • 33748750415 scopus 로고    scopus 로고
    • Selectins and glycosyltransferases in leukocyte rolling in vivo
    • DOI 10.1111/j.1742-4658.2006.05437.x
    • Sperandio, M. Selectins and glycosyltransferases in leukocyte rolling in vivo. FEBS J 273, 4377-4389 (2006). (Pubitemid 44401589)
    • (2006) FEBS Journal , vol.273 , Issue.19 , pp. 4377-4389
    • Sperandio, M.1
  • 44
    • 0036696903 scopus 로고    scopus 로고
    • Glycosylation in the control of selectin counter-receptor structure and function
    • Lowe, J. B. Glycosylation in the control of selectin counter-receptor structure and function. Immunol Rev 186, 19-36 (2002).
    • (2002) Immunol Rev , vol.186 , pp. 19-36
    • Lowe, J.B.1
  • 46
    • 46349088505 scopus 로고    scopus 로고
    • Biological function of fucosylation in cancer biology
    • DOI 10.1093/jb/mvn011
    • Miyoshi, E., Moriwaki, K. & Nakagawa, T. Biological function of fucosylation in cancer biology. J Biochem 143, 725-729 (2008). (Pubitemid 351918934)
    • (2008) Journal of Biochemistry , vol.143 , Issue.6 , pp. 725-729
    • Miyoshi, E.1    Moriwaki, K.2    Nakagawa, T.3
  • 48
    • 84891958414 scopus 로고    scopus 로고
    • Glycosylation of Immunoglobulin G: Role of genetic and epigenetic influences
    • Menni, C. et al. Glycosylation of Immunoglobulin G: Role of genetic and epigenetic influences. PLoS One 8, e82558 (2013).
    • (2013) PLoS One , vol.8
    • Menni, C.1
  • 49
    • 84864127482 scopus 로고    scopus 로고
    • The origin and function of platelet glycosyltransferases
    • Wandall, H. H. et al. The origin and function of platelet glycosyltransferases. Blood (2012).
    • (2012) Blood
    • Wandall, H.H.1
  • 50
    • 84860848749 scopus 로고    scopus 로고
    • Antiinflammatory IgG production requires functional P1 promoter in betagalactoside alpha2, 6-sialyltransferase 1 (ST6Gal-1) gene
    • Jones, M. B., Nasirikenari, M., Lugade, A. A., Thanavala, Y. & Lau, J. T. Antiinflammatory IgG production requires functional P1 promoter in betagalactoside alpha2, 6-sialyltransferase 1 (ST6Gal-1) gene. J Biol Chem 287, 15365-15370 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 15365-15370
    • Jones, M.B.1    Nasirikenari, M.2    Lugade, A.A.3    Thanavala, Y.4    Lau, J.T.5
  • 51
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • DOI 10.1146/annurev.immunol.26.021607.090232
    • Nimmerjahn, F. & Ravetch, J. V. Anti-inflammatory actions of intravenous immunoglobulin. Annu Rev Immunol 26, 513-533 (2008). (Pubitemid 351600384)
    • (2008) Annual Review of Immunology , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 52
    • 80054976616 scopus 로고    scopus 로고
    • High throughput plasma N-glycome profiling using multiplexed labelling and UPLC with fluorescence detection
    • Knezevic, A., Bones, J., Kracun, S. K., Gornik, O., Rudd, P. M. & Lauc, G. High throughput plasma N-glycome profiling using multiplexed labelling and UPLC with fluorescence detection. The Analyst 136, 4670-4673 (2011).
    • (2011) The Analyst , vol.136 , pp. 4670-4673
    • Knezevic, A.1    Bones, J.2    Kracun, S.K.3    Gornik, O.4    Rudd, P.M.5    Lauc, G.6


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