메뉴 건너뛰기




Volumn 113, Issue 26, 2016, Pages 7207-7212

B-cell-independent sialylation of IgG

Author keywords

B cell; IgG; IVIg; Sialylation; Sialyltransferase

Indexed keywords

IMMUNOGLOBULIN G; SIALYLTRANSFERASE; SIALYLTRANSFERASE ST6GAL1; UNCLASSIFIED DRUG; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE; OVALBUMIN; POLYSACCHARIDE; SIALIC ACID DERIVATIVE;

EID: 84976578131     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1523968113     Document Type: Article
Times cited : (106)

References (37)
  • 1
    • 0027115518 scopus 로고
    • Manipulating the immune system with immune globulin
    • Dwyer JM (1992) Manipulating the immune system with immune globulin. N Engl J Med 326(2):107-116.
    • (1992) N Engl J Med , vol.326 , Issue.2 , pp. 107-116
    • Dwyer, J.M.1
  • 2
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV (2006) Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313(5787):670-673.
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 3
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony RM, Wermeling F, Karlsson MC, Ravetch JV (2008) Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc Natl Acad Sci USA 105(50):19571-19578.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.50 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 4
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • Anthony RM, Kobayashi T, Wermeling F, Ravetch JV (2011) Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 475(7354): 110-113.
    • (2011) Nature , vol.475 , Issue.7354 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 5
    • 84934290153 scopus 로고    scopus 로고
    • Anti-HA glycoforms drive B cell affinity selection and determine influenza vaccine efficacy
    • Wang TT, et al. (2015) Anti-HA glycoforms drive B cell affinity selection and determine influenza vaccine efficacy. Cell 162(1):160-169.
    • (2015) Cell , vol.162 , Issue.1 , pp. 160-169
    • Wang, T.T.1
  • 6
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • Anthony RM, et al. (2008) Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320(5874):373-376.
    • (2008) Science , vol.320 , Issue.5874 , pp. 373-376
    • Anthony, R.M.1
  • 7
    • 79959817309 scopus 로고    scopus 로고
    • Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's)
    • Espy C, et al. (2011) Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's). Arthritis Rheum 63(7):2105-2115.
    • (2011) Arthritis Rheum , vol.63 , Issue.7 , pp. 2105-2115
    • Espy, C.1
  • 8
    • 77952487132 scopus 로고    scopus 로고
    • Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: Results from a large prospective cohort study
    • van de Geijn FE, et al. (2009) Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: Results from a large prospective cohort study. Arthritis Res Ther 11(6):R193.
    • (2009) Arthritis Res Ther , vol.11 , Issue.6 , pp. R193
    • Van De, G.F.E.1
  • 9
    • 0037031849 scopus 로고    scopus 로고
    • Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation
    • Martin LT, Marth JD, Varki A, Varki NM (2002) Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation. J Biol Chem 277(36):32930-32938.
    • (2002) J Biol Chem , vol.277 , Issue.36 , pp. 32930-32938
    • Martin, L.T.1    Marth, J.D.2    Varki, A.3    Varki, N.M.4
  • 10
    • 70350055478 scopus 로고    scopus 로고
    • Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I
    • Barb AW, Brady EK, Prestegard JH (2009) Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I. Biochemistry 48(41):9705-9707.
    • (2009) Biochemistry , vol.48 , Issue.41 , pp. 9705-9707
    • Barb, A.W.1    Brady, E.K.2    Prestegard, J.H.3
  • 12
    • 77949274595 scopus 로고    scopus 로고
    • Transcriptional regulation of the human ST6GAL2 gene in cerebral cortex and neuronal cells
    • Lehoux S, et al. (2010) Transcriptional regulation of the human ST6GAL2 gene in cerebral cortex and neuronal cells. Glycoconj J 27(1):99-114.
    • (2010) Glycoconj J , vol.27 , Issue.1 , pp. 99-114
    • Lehoux, S.1
  • 13
    • 77955301097 scopus 로고    scopus 로고
    • Role for hepatic and circulatory ST6Gal-1 sialyltransferase in regulating myelopoiesis
    • Jones MB, et al. (2010) Role for hepatic and circulatory ST6Gal-1 sialyltransferase in regulating myelopoiesis. J Biol Chem 285(32):25009-25017.
    • (2010) J Biol Chem , vol.285 , Issue.32 , pp. 25009-25017
    • Jones, M.B.1
  • 14
    • 84860848749 scopus 로고    scopus 로고
    • Anti-inflammatory IgG production requires functional P1 promoter in β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1) gene
    • Jones MB, Nasirikenari M, Lugade AA, Thanavala Y, Lau JT (2012) Anti-inflammatory IgG production requires functional P1 promoter in β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1) gene. J Biol Chem 287(19):15365-15370.
    • (2012) J Biol Chem , vol.287 , Issue.19 , pp. 15365-15370
    • Jones, M.B.1    Nasirikenari, M.2    Lugade, A.A.3    Thanavala, Y.4    Lau, J.T.5
  • 15
    • 0030818183 scopus 로고    scopus 로고
    • B lymphocyte-specific, Cre-mediated mutagenesis in mice
    • Rickert RC, Roes J, Rajewsky K (1997) B lymphocyte-specific, Cre-mediated mutagenesis in mice. Nucleic Acids Res 25(6):1317-1318.
    • (1997) Nucleic Acids Res , vol.25 , Issue.6 , pp. 1317-1318
    • Rickert, R.C.1    Roes, J.2    Rajewsky, K.3
  • 16
    • 31344445556 scopus 로고    scopus 로고
    • Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling
    • Collins BE, Smith BA, Bengtson P, Paulson JC (2006) Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling. Nat Immunol 7(2):199-206.
    • (2006) Nat Immunol , vol.7 , Issue.2 , pp. 199-206
    • Collins, B.E.1    Smith, B.A.2    Bengtson, P.3    Paulson, J.C.4
  • 17
    • 0020601369 scopus 로고
    • Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of gal beta 1 leads to 4GlcNAc alpha 2 leads to 6 sialyltransferase from liver
    • Kaplan HA, Woloski BM, Hellman M, Jamieson JC (1983) Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of Gal beta 1 leads to 4GlcNAc alpha 2 leads to 6 sialyltransferase from liver. J Biol Chem 258(19):11505-11509.
    • (1983) J Biol Chem , vol.258 , Issue.19 , pp. 11505-11509
    • Kaplan, H.A.1    Woloski, B.M.2    Hellman, M.3    Jamieson, J.C.4
  • 18
    • 0024446826 scopus 로고
    • Conversion of a Golgi apparatus sialyltransferase to a secretory protein by replacement of the NH2-terminal signal anchor with a signal peptide
    • Colley KJ, Lee EU, Adler B, Browne JK, Paulson JC (1989) Conversion of a Golgi apparatus sialyltransferase to a secretory protein by replacement of the NH2-terminal signal anchor with a signal peptide. J Biol Chem 264(30):17619-17622.
    • (1989) J Biol Chem , vol.264 , Issue.30 , pp. 17619-17622
    • Colley, K.J.1    Lee, E.U.2    Adler, B.3    Browne, J.K.4    Paulson, J.C.5
  • 19
    • 0023623637 scopus 로고
    • Primary structure of betagalactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor
    • Weinstein J, Lee EU, McEntee K, Lai PH, Paulson JC (1987) Primary structure of betagalactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. JBiolChem262(36): 17735-17743.
    • (1987) J Biol Chem 262 , vol.36 , pp. 17735-17743
    • Weinstein, J.1    Lee, E.U.2    McEntee, K.3    Lai, P.H.4    Paulson, J.C.5
  • 20
    • 0017833167 scopus 로고
    • Characterization of sialic acids
    • Schauer R (1978) Characterization of sialic acids. Methods Enzymol 50:64-89.
    • (1978) Methods Enzymol , vol.50 , pp. 64-89
    • Schauer, R.1
  • 21
    • 0021364466 scopus 로고
    • The release and purification of sialic acids from glycoconjugates: Methods to minimize the loss and migration of O-acetyl groups
    • Varki A, Diaz S (1984) The release and purification of sialic acids from glycoconjugates: Methods to minimize the loss and migration of O-acetyl groups. Anal Biochem 137(1):236-247.
    • (1984) Anal Biochem , vol.137 , Issue.1 , pp. 236-247
    • Varki, A.1    Diaz, S.2
  • 22
    • 84864127482 scopus 로고    scopus 로고
    • The origin and function of platelet glycosyltransferases
    • Wandall HH, et al. (2012) The origin and function of platelet glycosyltransferases. Blood 120(3):626-635.
    • (2012) Blood , vol.120 , Issue.3 , pp. 626-635
    • Wandall, H.H.1
  • 23
    • 0027420552 scopus 로고
    • Trans-sialidase: A unique enzyme activity discovered in the protozoan Trypanosoma cruzi
    • Colli W (1993) Trans-sialidase: A unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J 7(13):1257-1264.
    • (1993) FASEB J , vol.7 , Issue.13 , pp. 1257-1264
    • Colli, W.1
  • 24
  • 25
    • 84897370502 scopus 로고    scopus 로고
    • Platelets support extracellular sialylation by supplying the sugar donor substrate
    • Lee MM, et al. (2014) Platelets support extracellular sialylation by supplying the sugar donor substrate. J Biol Chem 289(13):8742-8748.
    • (2014) J Biol Chem , vol.289 , Issue.13 , pp. 8742-8748
    • Lee, M.M.1
  • 26
    • 84907486928 scopus 로고    scopus 로고
    • Platelet secretion and hemostasis require syntaxin-binding protein STXBP5
    • Ye S, et al. (2014) Platelet secretion and hemostasis require syntaxin-binding protein STXBP5. J Clin Invest 124(10):4517-4528.
    • (2014) J Clin Invest , vol.124 , Issue.10 , pp. 4517-4528
    • Ye, S.1
  • 27
    • 84868642198 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcgammaRIIB and dectin-1
    • Karsten CM, et al. (2012) Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcgammaRIIB and dectin-1. Nat Med 18(19): 1401-1406.
    • (2012) Nat Med , vol.18 , Issue.19 , pp. 1401-1406
    • Karsten, C.M.1
  • 28
    • 84877316930 scopus 로고    scopus 로고
    • Enhanced phagocytic activity of HIV-specific antibodies correlates with natural production of immunoglobulins with skewed affinity for FcγR2a and FcγR2b
    • Ackerman ME, et al. (2013) Enhanced phagocytic activity of HIV-specific antibodies correlates with natural production of immunoglobulins with skewed affinity for FcγR2a and FcγR2b. J Virol 87(10):5468-5476.
    • (2013) J Virol , vol.87 , Issue.10 , pp. 5468-5476
    • Ackerman, M.E.1
  • 29
    • 84877152391 scopus 로고    scopus 로고
    • Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity
    • Ackerman ME, et al. (2013) Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest 123(5):2183-2192.
    • (2013) J Clin Invest , vol.123 , Issue.5 , pp. 2183-2192
    • Ackerman, M.E.1
  • 30
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields RL, et al. (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 277(30):26733-26740.
    • (2002) J Biol Chem , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1
  • 31
    • 80054944116 scopus 로고    scopus 로고
    • Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans
    • Mizushima T, et al. (2011) Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells 16(11):1071-1080.
    • (2011) Genes Cells , vol.16 , Issue.11 , pp. 1071-1080
    • Mizushima, T.1
  • 32
    • 0019793439 scopus 로고
    • Turnover of free sialic acid, CMP-sialic acid, and bound sialic acid in rat brain
    • Ferwerda W, Blok CM, Heijlman J (1981) Turnover of free sialic acid, CMP-sialic acid, and bound sialic acid in rat brain. J Neurochem 36(4):1492-1499.
    • (1981) J Neurochem , vol.36 , Issue.4 , pp. 1492-1499
    • Ferwerda, W.1    Blok, C.M.2    Heijlman, J.3
  • 33
    • 84889053976 scopus 로고    scopus 로고
    • Enzymatic basis for N-glycan sialylation: Structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation
    • Meng L, et al. (2013) Enzymatic basis for N-glycan sialylation: Structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation. JBiolChem288(48):34680-34698.
    • (2013) J Biol Chem 288 , vol.48 , pp. 34680-34698
    • Meng, L.1
  • 34
    • 84859416185 scopus 로고    scopus 로고
    • Multifarious roles of sialic acids in immunity
    • Varki A, Gagneux P (2012) Multifarious roles of sialic acids in immunity. Ann N Y Acad Sci 1253:16-36.
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 16-36
    • Varki, A.1    Gagneux, P.2
  • 35
    • 84879642611 scopus 로고    scopus 로고
    • Antigenic liposomes displaying CD22 ligands induce antigen-specific B cell apoptosis
    • Macauley MS, et al. (2013) Antigenic liposomes displaying CD22 ligands induce antigen-specific B cell apoptosis. J Clin Invest 123(7):3074-3083.
    • (2013) J Clin Invest , vol.123 , Issue.7 , pp. 3074-3083
    • Macauley, M.S.1
  • 36
    • 34547099820 scopus 로고    scopus 로고
    • Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death
    • Toscano MA, et al. (2007) Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death. Nat Immunol 8(8):825-834.
    • (2007) Nat Immunol , vol.8 , Issue.8 , pp. 825-834
    • Toscano, M.A.1
  • 37
    • 84908584273 scopus 로고    scopus 로고
    • Liquid chromatography-selected reaction monitoring (LC-SRM) approach for the separation and quantitation of sialylated N-glycans linkage isomers
    • Tao S, Huang Y, Boyes BE, Orlando R (2014) Liquid chromatography-selected reaction monitoring (LC-SRM) approach for the separation and quantitation of sialylated N-glycans linkage isomers. Anal Chem 86(21):10584-10590.
    • (2014) Anal Chem , vol.86 , Issue.21 , pp. 10584-10590
    • Tao, S.1    Huang, Y.2    Boyes, B.E.3    Orlando, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.