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Volumn 14, Issue 10, 2015, Pages 4402-4412

N-Glycosylation of Serum IgG and Total Glycoproteins in MAN1B1 Deficiency

Author keywords

biomarkers; CDG; glycomics; human serum; IgG; MAN1B1; N glycans; sialyl Lewis x; ultra performance liquid chromatography

Indexed keywords

GLYCAN; GLYCOPROTEIN; IMMUNOGLOBULIN G; MANNOSE; PLASMA PROTEIN; SIALYL LEWIS X ANTIGEN; ALPHA MANNOSIDASE; BIOLOGICAL MARKER; CD15 ANTIGEN;

EID: 84942906413     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00709     Document Type: Article
Times cited : (26)

References (33)
  • 1
    • 84887610544 scopus 로고    scopus 로고
    • Changes in serum N-glycosylation profiles: Functional significance and potential for diagnostics
    • In; Rauter, A. P. RSC Publishing, Vol.
    • Marino, K.; Saldova, R.; Adamczyk, B.; Rudd, P. M. Changes in serum N-glycosylation profiles: functional significance and potential for diagnostics. In Carbohydrate Chemistry: Chemical and Biological Approaches; Rauter, A. P., Ed.; RSC Publishing, 2012; Vol. 37, pp 57-93.
    • (2012) Carbohydrate Chemistry: Chemical and Biological Approaches , vol.37 , pp. 57-93
    • Marino, K.1    Saldova, R.2    Adamczyk, B.3    Rudd, P.M.4
  • 3
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J. N.; Wormald, M. R.; Sim, R. B.; Rudd, P. M.; Dwek, R. A. The impact of glycosylation on the biological function and structure of human immunoglobulins Annu. Rev. Immunol. 2007, 25, 21-50 10.1146/annurev.immunol.25.022106.141702
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 4
    • 84926616856 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation with emphasis on cerebellar involvement
    • Barone, R.; Fiumara, A.; Jaeken, J. Congenital disorders of glycosylation with emphasis on cerebellar involvement Semin Neurol 2014, 34, 357-66 10.1055/s-0034-1387197
    • (2014) Semin Neurol , vol.34 , pp. 357-366
    • Barone, R.1    Fiumara, A.2    Jaeken, J.3
  • 6
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze, H. H. Genetic defects in the human glycome Nat. Rev. Genet. 2006, 7, 537-51 10.1038/nrg1894
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 537-551
    • Freeze, H.H.1
  • 7
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob, C. A.; Burda, P.; Roth, J.; Aebi, M. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure J. Cell Biol. 1998, 142, 1223-33 10.1083/jcb.142.5.1223
    • (1998) J. Cell Biol. , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 11
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Marino, K.; Bones, J.; Kattla, J. J.; Rudd, P. M. A systematic approach to protein glycosylation analysis: a path through the maze Nat. Chem. Biol. 2010, 6, 713-23 10.1038/nchembio.437
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 713-723
    • Marino, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 12
    • 84884264843 scopus 로고    scopus 로고
    • Automated, high-throughput IgG-antibody glycoprofiling platform
    • Stöckmann, H.; Adamczyk, B.; Hayes, J.; Rudd, P. M. Automated, high-throughput IgG-antibody glycoprofiling platform Anal. Chem. 2013, 85, 8841-9 10.1021/ac402068r
    • (2013) Anal. Chem. , vol.85 , pp. 8841-8849
    • Stöckmann, H.1    Adamczyk, B.2    Hayes, J.3    Rudd, P.M.4
  • 14
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J. C.; Patel, T. P.; Bruce, J. A.; Goulding, P. N.; Charles, S. M.; Parekh, R. B. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid Anal. Biochem. 1995, 230, 229-38 10.1006/abio.1995.1468
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 15
    • 34447310112 scopus 로고    scopus 로고
    • Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions
    • Royle, L.; Radcliffe, C. M.; Dwek, R. A.; Rudd, P. M. Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions Methods Mol. Biol. 2006, 347, 125-43 10.1385/1-59745-167-3:125
    • (2006) Methods Mol. Biol. , vol.347 , pp. 125-143
    • Royle, L.1    Radcliffe, C.M.2    Dwek, R.A.3    Rudd, P.M.4
  • 18
    • 58149381931 scopus 로고    scopus 로고
    • Glycosylation changes on serum glycoproteins in ovarian cancer may contribute to disease pathogenesis
    • Saldova, R.; Wormald, M. R.; Dwek, R. A.; Rudd, P. M. Glycosylation changes on serum glycoproteins in ovarian cancer may contribute to disease pathogenesis Dis. Markers 2008, 25, 219-32 10.1155/2008/601583
    • (2008) Dis. Markers , vol.25 , pp. 219-232
    • Saldova, R.1    Wormald, M.R.2    Dwek, R.A.3    Rudd, P.M.4
  • 19
    • 84860222212 scopus 로고    scopus 로고
    • Golgi pH, its regulation and roles in human disease
    • Rivinoja, A.; Pujol, F. M.; Hassinen, A.; Kellokumpu, S. Golgi pH, its regulation and roles in human disease Ann. Med. 2012, 44, 542-54 10.3109/07853890.2011.579150
    • (2012) Ann. Med. , vol.44 , pp. 542-554
    • Rivinoja, A.1    Pujol, F.M.2    Hassinen, A.3    Kellokumpu, S.4
  • 21
    • 1242317024 scopus 로고    scopus 로고
    • Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa
    • Okazaki, A.; Shoji-Hosaka, E.; Nakamura, K.; Wakitani, M.; Uchida, K.; Kakita, S.; Tsumoto, K.; Kumagai, I.; Shitara, K. Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa J. Mol. Biol. 2004, 336, 1239-49 10.1016/j.jmb.2004.01.007
    • (2004) J. Mol. Biol. , vol.336 , pp. 1239-1249
    • Okazaki, A.1    Shoji-Hosaka, E.2    Nakamura, K.3    Wakitani, M.4    Uchida, K.5    Kakita, S.6    Tsumoto, K.7    Kumagai, I.8    Shitara, K.9
  • 22
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umana, P.; Jean-Mairet, J.; Moudry, R.; Amstutz, H.; Bailey, J. E. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity Nat. Biotechnol. 1999, 17, 176-80 10.1038/6179
    • (1999) Nat. Biotechnol. , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 23
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko, Y.; Nimmerjahn, F.; Ravetch, J. V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 2006, 313, 670-3 10.1126/science.1129594
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 25
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra, R.; Wormald, M. R.; Rudd, P. M.; Fischer, P. B.; Dwek, R. A.; Sim, R. B. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein Nat. Med. 1995, 1, 237-43 10.1038/nm0395-237
    • (1995) Nat. Med. , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3    Fischer, P.B.4    Dwek, R.A.5    Sim, R.B.6
  • 27
    • 77956041687 scopus 로고    scopus 로고
    • The sialome - Far more than the sum of its parts
    • Cohen, M.; Varki, A. The sialome - far more than the sum of its parts OMICS 2010, 14, 455-64 10.1089/omi.2009.0148
    • (2010) OMICS , vol.14 , pp. 455-464
    • Cohen, M.1    Varki, A.2
  • 28
    • 21644463169 scopus 로고    scopus 로고
    • Siglecs in innate immunity
    • Crocker, P. R. Siglecs in innate immunity Curr. Opin. Pharmacol. 2005, 5, 431-7 10.1016/j.coph.2005.03.003
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 431-437
    • Crocker, P.R.1
  • 29
    • 0036815746 scopus 로고    scopus 로고
    • Siglecs: Sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling
    • Crocker, P. R. Siglecs: sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling Curr. Opin. Struct. Biol. 2002, 12, 609-15 10.1016/S0959-440X(02)00375-5
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 609-615
    • Crocker, P.R.1
  • 30
    • 84891708255 scopus 로고    scopus 로고
    • Sialic acids siglec interaction: A unique strategy to circumvent innate immune response by pathogens
    • Khatua, B.; Roy, S.; Mandal, C. Sialic acids siglec interaction: a unique strategy to circumvent innate immune response by pathogens Indian J. Med. Res. 2013, 138, 648-662
    • (2013) Indian J. Med. Res. , vol.138 , pp. 648-662
    • Khatua, B.1    Roy, S.2    Mandal, C.3
  • 31
    • 84891708446 scopus 로고    scopus 로고
    • A perspective on the emergence of sialic acids as potent determinants affecting leishmania biology
    • Ghoshal, A.; Mandal, C. A perspective on the emergence of sialic acids as potent determinants affecting leishmania biology Mol. Biol. Int. 2011, 2011, 532106 10.4061/2011/532106
    • (2011) Mol. Biol. Int. , vol.2011 , pp. 532106
    • Ghoshal, A.1    Mandal, C.2
  • 32
    • 39049137589 scopus 로고    scopus 로고
    • Alpha 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo
    • Hedlund, M.; Ng, E.; Varki, A.; Varki, N. M. alpha 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo Cancer Res. 2008, 68, 388-94 10.1158/0008-5472.CAN-07-1340
    • (2008) Cancer Res. , vol.68 , pp. 388-394
    • Hedlund, M.1    Ng, E.2    Varki, A.3    Varki, N.M.4
  • 33
    • 84859416185 scopus 로고    scopus 로고
    • Multifarious roles of sialic acids in immunity
    • Varki, A.; Gagneux, P. Multifarious roles of sialic acids in immunity Ann. N. Y. Acad. Sci. 2012, 1253, 16-36 10.1111/j.1749-6632.2012.06517.x
    • (2012) Ann. N. Y. Acad. Sci. , vol.1253 , pp. 16-36
    • Varki, A.1    Gagneux, P.2


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