메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

MALDI-TOF-MS reveals differential N-linked plasma-and IgG-glycosylation profiles between mothers and their newborns

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84988891186     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep34001     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 33645098806 scopus 로고    scopus 로고
    • Mother's little helpers: Mechanisms of maternal-fetal tolerance
    • Trowsdale, J. & Betz, A. G. Mother's little helpers: mechanisms of maternal-fetal tolerance. Nature Immunol. 7, 241-246 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 241-246
    • Trowsdale, J.1    Betz, A.G.2
  • 2
    • 79954453952 scopus 로고    scopus 로고
    • Gimme shelter: The immune system during pregnancy
    • Munoz-Suano, A., Hamilton, A. B. & Betz, A. G. Gimme shelter: the immune system during pregnancy. Immunol Rev 241, 20-38 (2011).
    • (2011) Immunol Rev , vol.241 , pp. 20-38
    • Munoz-Suano, A.1    Hamilton, A.B.2    Betz, A.G.3
  • 3
    • 53849107145 scopus 로고    scopus 로고
    • Reference values for 1-acid glycoprotein, 1-antitrypsin, albumin, haptoglobin, C-reactive protein, IgA, IgG and IgM during pregnancy
    • Larsson, A., Palm, M., Hansson, L.-O., Basu, S. & Axelsson, O. V. E. Reference values for 1-acid glycoprotein, 1-antitrypsin, albumin, haptoglobin, C-reactive protein, IgA, IgG and IgM during pregnancy. Acta Obstet. Gynecol. Scand. 87, 1084-1088 (2008).
    • (2008) Acta Obstet. Gynecol. Scand. , vol.87 , pp. 1084-1088
    • Larsson, A.1    Palm, M.2    Hansson, L.-O.3    Basu, S.4    Axelsson, O.V.E.5
  • 4
    • 0038384134 scopus 로고    scopus 로고
    • Placental transport of immunoglobulin G
    • Simister, N. E. Placental transport of immunoglobulin G. Vaccine 21, 3365-3369 (2003).
    • (2003) Vaccine , vol.21 , pp. 3365-3369
    • Simister, N.E.1
  • 5
    • 0013837680 scopus 로고
    • The immunological Development of the Human Fetus
    • van Furth, R., Schuit, H. R. E. & Hijmans, W. The immunological Development of The Human Fetus. J. Exp. Med. 122, 1173-1188 (1965).
    • (1965) J. Exp. Med. , vol.122 , pp. 1173-1188
    • Van Furth, R.1    Schuit, H.R.E.2    Hijmans, W.3
  • 6
    • 0022411043 scopus 로고
    • Blood volume changes in normal pregnancy
    • Hytten, F. Blood volume changes in normal pregnancy. Clin Haematol 14, 601-612 (1985).
    • (1985) Clin Haematol , vol.14 , pp. 601-612
    • Hytten, F.1
  • 7
    • 84875410765 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy: How does IgG modulate the immune system
    • Schwab, I. & Nimmerjahn, F. Intravenous immunoglobulin therapy: how does IgG modulate the immune system Nat. Rev. Immunol. 13, 176-189 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 176-189
    • Schwab, I.1    Nimmerjahn, F.2
  • 8
    • 0037178791 scopus 로고    scopus 로고
    • Lack of Fucose on Human IgG1 N-Linked oligosaccharide improves binding to human Fc RIII and antibodydependent cellular toxicity
    • Shields, R. L. et al. Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human Fc RIII and Antibodydependent Cellular Toxicity. J. Biol. Chem. 277, 26733-26740 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 9
    • 84942919876 scopus 로고    scopus 로고
    • In Vitro Glycoengineering of IgG1 and Its Effect on Fc Receptor Binding and ADCC Activity
    • Thomann, M. et al. In Vitro Glycoengineering of IgG1 and Its Effect on Fc Receptor Binding and ADCC Activity. Plos One 10, e0134949 (2015).
    • (2015) Plos One , vol.10 , pp. e0134949
    • Thomann, M.1
  • 10
    • 0028061347 scopus 로고
    • A major histocompatibility complex class I-like Fc receptor cloned from human placenta: Possible role in transfer of immunoglobulin G from mother to fetus
    • Story, C. M., Mikulska, J. E. & Simister, N. E. A major histocompatibility complex class I-like Fc receptor cloned from human placenta: possible role in transfer of immunoglobulin G from mother to fetus. J. Exp. Med. 180, 2377-2381 (1994).
    • (1994) J. Exp. Med. , vol.180 , pp. 2377-2381
    • Story, C.M.1    Mikulska, J.E.2    Simister, N.E.3
  • 11
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • Roopenian, D. C. & Akilesh, S. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7, 715-725 (2007).
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 12
    • 0029185950 scopus 로고
    • Selective placental transport of maternal IgG to the fetus
    • Williams, P. J. et al. Selective placental transport of maternal IgG to the fetus. Placenta 16, 749-756 (1995).
    • (1995) Placenta , vol.16 , pp. 749-756
    • Williams, P.J.1
  • 13
    • 0030434866 scopus 로고    scopus 로고
    • Glycosylation and placental transport of immunoglobulin G
    • Kibe, T. et al. Glycosylation and Placental Transport of Immunoglobulin G. J. Clin. Biochem. Nutr. 21, 57-63 (1996).
    • (1996) J. Clin. Biochem. Nutr. , vol.21 , pp. 57-63
    • Kibe, T.1
  • 14
    • 84878855286 scopus 로고    scopus 로고
    • Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G
    • Einarsdottir, H. K. et al. Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G. Glycoconj J 30, 147-157 (2013).
    • (2013) Glycoconj J , vol.30 , pp. 147-157
    • Einarsdottir, H.K.1
  • 15
    • 84952366430 scopus 로고    scopus 로고
    • Multi-Angle effector function analysis of human monoclonal IgG glycovariants
    • Dashivets, T. et al. Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants. Plos One 10, e0143520 (2015).
    • (2015) Plos One , vol.10 , pp. e0143520
    • Dashivets, T.1
  • 16
    • 84865677743 scopus 로고    scopus 로고
    • Isotype and glycoform selection for antibody therapeutics
    • Jefferis, R. Isotype and glycoform selection for antibody therapeutics. Arch. Biochem. Biophys. 526, 159-166 (2012).
    • (2012) Arch. Biochem. Biophys. , vol.526 , pp. 159-166
    • Jefferis, R.1
  • 17
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields, R. L. et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J Biol Chem 276, 6591-6604 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1
  • 19
    • 84879304669 scopus 로고    scopus 로고
    • Inhibition of HPA-1a alloantibody-mediated platelet destruction by a deglycosylated anti-HPA-1a monoclonal antibody in mice: Toward targeted treatment of fetal-alloimmune thrombocytopenia
    • Bakchoul, T. et al. Inhibition of HPA-1a alloantibody-mediated platelet destruction by a deglycosylated anti-HPA-1a monoclonal antibody in mice: toward targeted treatment of fetal-alloimmune thrombocytopenia. Blood 122, 321-327 (2013).
    • (2013) Blood , vol.122 , pp. 321-327
    • Bakchoul, T.1
  • 20
    • 81855226434 scopus 로고    scopus 로고
    • Polymorphisms in B3GAT1 SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults
    • Huffman, J. E. et al. Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults. Hum. Mol. Genet. 20, 5000-5011 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 5000-5011
    • Huffman, J.E.1
  • 21
    • 84964292866 scopus 로고    scopus 로고
    • Pregnancy-associated serum N-glycome changes studied by high-throughput MALDI-TOF-MS
    • Jansen, B. C. et al. Pregnancy-associated serum N-glycome changes studied by high-throughput MALDI-TOF-MS. Nature Scientific Reports 6, 23296 (2016).
    • (2016) Nature Scientific Reports , vol.6 , pp. 23296
    • Jansen, B.C.1
  • 22
    • 84902814201 scopus 로고    scopus 로고
    • High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification
    • Reiding, K. R., Blank, D., Kuijper, D. M., Deelder, A. M. & Wuhrer, M. High-throughput profiling of protein N-glycosylation by MALDI-TOF-MS employing linkage-specific sialic acid esterification. Anal. Chem. 86, 5784-5793 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 5784-5793
    • Reiding, K.R.1    Blank, D.2    Kuijper, D.M.3    Deelder, A.M.4    Wuhrer, M.5
  • 23
    • 84949036097 scopus 로고    scopus 로고
    • MassyTools: A high throughput targeted data processing tool for relative quantitation and quality control developed for glycomic and glycoproteomic MALDI-MS
    • Jansen, B. C. et al. MassyTools: A high throughput targeted data processing tool for relative quantitation and quality control developed for glycomic and glycoproteomic MALDI-MS. J. Proteome Res. 14, 5088-5098 (2015).
    • (2015) J. Proteome Res. , vol.14 , pp. 5088-5098
    • Jansen, B.C.1
  • 26
    • 84893121418 scopus 로고    scopus 로고
    • A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy
    • Kapur, R. et al. A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy. Blood 123, 471-480 (2014).
    • (2014) Blood , vol.123 , pp. 471-480
    • Kapur, R.1
  • 28
  • 29
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG IgG-Fc and IgG-Fab isolated from the sera of patients with ANCAassociated systemic vasculitis
    • Holland, M. et al. Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCAassociated systemic vasculitis. Biochim. Biophys. Acta 1760, 669-677 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 669-677
    • Holland, M.1
  • 30
    • 84946233610 scopus 로고    scopus 로고
    • An intrinsic mechanism of secreted protein aging and turnover
    • Yang, W. H. et al. An intrinsic mechanism of secreted protein aging and turnover. Proc. Natl. Acad. Sci. USA 112, 13657-13662 (2015).
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 13657-13662
    • Yang, W.H.1
  • 31
    • 0016766056 scopus 로고
    • The Concentrations of Retinol-Binding protein, prealbumin, and transferrin in the sera of newly delivered mothers and children of various ages
    • Vahlquist, A., Rask, L., Peterson, P. A. & Berg, T. The Concentrations of Retinol-Binding Protein, Prealbumin, and Transferrin in the Sera of Newly Delivered Mothers and Children of Various Ages. Scand. J. Clin. Lab. Inv. 35, 569-575 (1975).
    • (1975) Scand. J. Clin. Lab. Inv. , vol.35 , pp. 569-575
    • Vahlquist, A.1    Rask, L.2    Peterson, P.A.3    Berg, T.4
  • 32
    • 0027240214 scopus 로고
    • Plasma protein levels in normal human fetuses: 13 to 41 weeks' gestation
    • Fryer, A. A., Jones, P., Strange, R., Hume, R. & Bell, J. E. Plasma protein levels in normal human fetuses: 13 to 41 weeks' gestation. Br. J. Obstet. Gynaecol. 100, 850-855 (1993).
    • (1993) Br. J. Obstet. Gynaecol. , vol.100 , pp. 850-855
    • Fryer, A.A.1    Jones, P.2    Strange, R.3    Hume, R.4    Bell, J.E.5
  • 34
    • 0030822690 scopus 로고    scopus 로고
    • Protein transport across the in vitro perfused human placenta
    • Malek, A., Sager, R., Lang, A. B. & Schneider, H. Protein transport across the in vitro perfused human placenta. Am. J. Reprod. Immunol. 38, 263-271 (1997).
    • (1997) Am. J. Reprod. Immunol. , vol.38 , pp. 263-271
    • Malek, A.1    Sager, R.2    Lang, A.B.3    Schneider, H.4
  • 35
    • 0016292591 scopus 로고
    • Protein binding by specific receptors on human placenta, murine placenta, and suckling murine intestine in relation to protein transport across these tissues
    • Gitlin, J. D. & Gitlin, D. Protein binding by specific receptors on human placenta, murine placenta, and suckling murine intestine in relation to protein transport across these tissues. J Clin Invest 54, 1155-1166 (1974).
    • (1974) J Clin Invest , vol.54 , pp. 1155-1166
    • Gitlin, J.D.1    Gitlin, D.2
  • 36
    • 25644434348 scopus 로고    scopus 로고
    • Transport of maternal immunoglobulins through the human placental barrier in normal pregnancy and during inflammation
    • Ben-Hur, H. et al. Transport of maternal immunoglobulins through the human placental barrier in normal pregnancy and during inflammation. Int. J. Mol. Med 16, 401-407 (2005).
    • (2005) Int. J. Mol. Med , vol.16 , pp. 401-407
    • Ben-Hur, H.1
  • 37
    • 0020021127 scopus 로고
    • Carbohydrate-Specific Receptors of the Liver
    • Ashwell, a. G. & Harford, J. Carbohydrate-Specific Receptors of the Liver. Ann. Rev. Biochem. 51, 531-554 (1982).
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, A.G.1    Harford, J.2
  • 38
    • 63649163810 scopus 로고    scopus 로고
    • The asialoglycoprotein receptor regulates levels of plasma glycoproteins terminating with sialic Acid 2,6-Galactose
    • Steirer, L. M., Park, E. I., Townsend, R. R. & Baenziger, J. U. The Asialoglycoprotein Receptor Regulates Levels of Plasma Glycoproteins Terminating with Sialic Acid 2,6-Galactose. The Journal of Biological Chemistry 284, 3777-3783 (2009).
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 3777-3783
    • Steirer, L.M.1    Park, E.I.2    Townsend, R.R.3    Baenziger, J.U.4
  • 39
    • 28044469503 scopus 로고    scopus 로고
    • The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid 2,6GalNAc
    • Park, E. I., Mi, Y., Unverzagt, C., Gabius, H.-J. & Baenziger, J. U. The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid 2,6GalNAc. Proc. Natl. Acad. Sci. USA 102, 17125-17129 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17125-17129
    • Park, E.I.1    Mi, Y.2    Unverzagt, C.3    Gabius, H.-J.4    Baenziger, J.U.5
  • 40
    • 84949267265 scopus 로고    scopus 로고
    • Immunoglobulin concentrations in plasma and saliva during the neonatal period
    • Pineda-Martinez, S. et al. Immunoglobulin Concentrations in Plasma and Saliva During the Neonatal Period. Pediatrics & Neonatology 57, 213-218 (2016).
    • (2016) Pediatrics & Neonatology , vol.57 , pp. 213-218
    • Pineda-Martinez, S.1
  • 41
    • 0015181978 scopus 로고
    • Human IgG subclasses in maternal and fetal serum
    • Morell, A., Skvaril, F., van Loghem, E. & Kleemola, M. Human IgG subclasses in maternal and fetal serum. Vox Sang 21, 481-492 (1971).
    • (1971) Vox Sang , vol.21 , pp. 481-492
    • Morell, A.1    Skvaril, F.2    Van Loghem, E.3    Kleemola, M.4
  • 42
    • 84941060330 scopus 로고    scopus 로고
    • Automation of High-Throughput mass Spectrometry-Based Plasma N-Glycome analysis with Linkage-Specific sialic acid esterification
    • Bladergroen, M. R. et al. Automation of High-Throughput Mass Spectrometry-Based Plasma N-Glycome Analysis with Linkage-Specific Sialic Acid Esterification. J. Proteome Res. 14, 4080-4086 (2015).
    • (2015) J. Proteome Res. , vol.14 , pp. 4080-4086
    • Bladergroen, M.R.1
  • 43
    • 84910647104 scopus 로고    scopus 로고
    • IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancyassociated changes
    • Bondt, A. et al. IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancyassociated changes. Mol. Cell. Proteomics 13, 3029-3039 (2014).
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1
  • 44
    • 0001884644 scopus 로고
    • Individual comparisons by ranking methods
    • Wilcoxon, F. Individual Comparisons by Ranking Methods. Biometics Bull. 1, 80-83 (1945).
    • (1945) Biometics Bull. , vol.1 , pp. 80-83
    • Wilcoxon, F.1
  • 45
    • 84943987463 scopus 로고
    • Multiple comparisons among means
    • Dunn, O. J. Multiple Comparisons among Means. J. Am. Stat. Assoc. 56, 52-64 (1961).
    • (1961) J. Am. Stat. Assoc. , vol.56 , pp. 52-64
    • Dunn, O.J.1
  • 46
    • 45549094069 scopus 로고    scopus 로고
    • Glyco Workbench: A tool for the Computer-Assisted annotation of mass spectra of glycans
    • Ceroni, A. et al. GlycoWorkbench: A Tool for the Computer-Assisted Annotation of Mass Spectra of Glycans. J. Proteome Res. 7, 1650-1659 (2008).
    • (2008) J. Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1
  • 47
    • 80054016444 scopus 로고    scopus 로고
    • High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations
    • Pucic, M. et al. High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations. Mol. Cell. Proteomics 10, M111.010090 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. M111010090
    • Pucic, M.1
  • 48
    • 84899846338 scopus 로고    scopus 로고
    • Association of N-Glycosylation with breast carcinoma and systemic features using High-Resolution quantitative UPLC
    • Saldova, R. et al. Association of N-Glycosylation with Breast Carcinoma and Systemic Features Using High-Resolution Quantitative UPLC. J. Proteome Res. 13, 2314-2327 (2014).
    • (2014) J. Proteome Res. , vol.13 , pp. 2314-2327
    • Saldova, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.