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Volumn 9, Issue 3, 2010, Pages 1367-1373

Quantitation of saccharide compositions of O-glycans by mass spectrometry of glycopeptides and its application to rheumatoid arthritis

Author keywords

Galactose; Glycopeptide; Mass spectrometry; Mucin type O glycan; Quantitation; Rheumatoid arthritis

Indexed keywords

GLYCAN DERIVATIVE; GLYCOPEPTIDE; HEMOPEXIN; IMMUNOGLOBULIN A1; N ACETYLGALACTOSAMINE;

EID: 77949862643     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr900913k     Document Type: Article
Times cited : (57)

References (50)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo, K.; Marth, J. D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126, 855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 70349886556 scopus 로고    scopus 로고
    • Folding of glycoproteins: Toward understanding the biophysics of the glycosylation code
    • Shental-Bechor, D.; Levy, Y. Folding of glycoproteins: toward understanding the biophysics of the glycosylation code. Curr. Opin. Struct. Biol 2009, 19, 524-533.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 3
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammationpotential for therapeutics and diagnostics
    • Dube D. H.; Bertozzi, C. R. Glycans in cancer and inflammationpotential for therapeutics and diagnostics. Nat. Rev. Drug Discovery 2005, 4, 477-488.
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 4
    • 50449083310 scopus 로고    scopus 로고
    • Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation
    • Arnold, J. N.; Saldova, R.; Hamid, U. M.; Rudd, P. M. Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics 2008, 8, 3284-3293.
    • (2008) Proteomics , vol.8 , pp. 3284-3293
    • Arnold, J.N.1    Saldova, R.2    Hamid, U.M.3    Rudd, P.M.4
  • 5
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: Their functions and target proteins
    • Takahashi, M.; Kuroki, Y.; Ohtsubo, K.; Taniguchi, N. Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr., Res. 2009, 344, 1387-1390.
    • (2009) Carbohydr., Res. , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 6
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A rapidly expanding disease family
    • Jaeken, J.; Matthijs, G. Congenital disorders of glycosylation: a rapidly expanding disease family. Annu. Rev. Genomics Hum. Genet. 2007, 8, 261-278.
    • (2007) Annu. Rev. Genomics Hum. Genet. , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 7
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian, E.; Ten Hagen, K. G. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconjueate J. 2009, 26, 325-334.
    • (2009) Glycoconjueate J. , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 9
    • 33745828096 scopus 로고    scopus 로고
    • Polypeptide GalNAc-transferase T3 and familial tumoral cal- Cinosis. Secretion of fibroblast growth factor 23 requires O- glycosylation
    • Kato, K.; Jeanneau, C.; Tarp, M. A.; Benet-Pages, A; LorenzDepiereux, B.; Bennett, E. P.; Mandel, U.; Strom, T. M.; Clausen, H. Polypeptide GalNAc-transferase T3 and familial tumoral cal- cinosis. Secretion of fibroblast growth factor 23 requires O- glycosylation. J. Biol. Chem. 2006, 281, 18370-18377.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18370-18377
    • Kato, K.1    Jeanneau, C.2    Tarp, M.A.3    Benet-Pages, A.4    Lorenzdepiereux, B.5    Bennett, E.P.6    Mandel, U.7    Strom, T.M.8    Clausen, H.9
  • 11
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptie N- aceylagactpsaminyltransferases
    • Ten Hagen, K. G.; Fritz, T. A.; Tabak, L. A. All in the family: the UDP-GalNAc:polypeptie N-aceylagactpsaminyltransferases. Gly- coboiology 2003, 13, 1R-16R.
    • (2003) Glycoboiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 12
    • 0026816653 scopus 로고
    • Some proline substituent effects in the tandem mass spectrum of protonated pentaalanlne
    • Schwartz, B. L.; Bursey, M. M. Some proline substituent effects In the tandem mass spectrum of protonated pentaalanlne. Biol. Mass Spectrom. 1992, 21, 92-96.
    • (1992) Biol. Mass Spectrom. , vol.21 , pp. 92-96
    • Schwartz, B.L.1    Bursey, M.M.2
  • 13
    • 0029823591 scopus 로고    scopus 로고
    • Probing the proline effect in CID of protonated peptides
    • Valsar, T.; Urban, J. Probing the proline effect in CID of protonated peptides. J, Mass Spectro. 1996, 31, 1185-1187.
    • (1996) J, Mass Spectro. , vol.31 , pp. 1185-1187
    • Valsar, T.1    Urban, J.2
  • 14
    • 21444448470 scopus 로고    scopus 로고
    • Determination of aberrant O-glycosylatl in the IgAl. hinge region, by electron, capture dissociation fourier transform-ion cyclotron resonance mass spectrometry
    • Renfrew, M. B.; Cooper, H. J.; Tomana, M.; Kulhavy, R.; Hoikid, Y.; Toma, K.; Emmett, M. R.; Mestechy, J.; Marshall, A. G.; Novak, J. Determination of aberrant O-glycosylatl In the IgAl. hinge region, by electron, capture dissociation fourier transform-ion cyclotron resonance mass spectrometry. T. Biol. Chem. 2005, 280, 19136-19145.
    • (2005) T. Biol. Chem. , vol.280 , pp. 19136-19145
    • Renfrew, M.B.1    Cooper, H.J.2    Tomana, M.3    Kulhavy, R.4    Hoikid, Y.5    Toma, K.6    Emmett, M.R.7    Mestechy, J.8    Marshall, A.G.9    Novak, J.10
  • 15
    • 24044523213 scopus 로고    scopus 로고
    • Sitespecific glycosylation analysis of human apolipoprofein B100 using LC/ESI MS/MS
    • Harazono, A; Kawasaki, N.; Kawanishi, T.; Hayakawa, T. Sitespecific glycosylation analysis of human apolipoprofein B100 using LC/ESI MS/MS. Glycobiology 2005, 15, 447-462.
    • (2005) Glycobiology , vol.15 , pp. 447-462
    • Harazono, A.1    Kawasaki, N.2    Kawanishi, T.3    Hayakawa, T.4
  • 16
    • 28444460388 scopus 로고    scopus 로고
    • Differential analysis of site-specific glycans on plasma and cellular fibronectins: Application of a hydrophllic affinity method for glycopeptide enrichment
    • Tajiri, M.; Yoshida, S.; Wada, Y. Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophllic affinity method for glycopeptide enrichment. Glycobiology 2005, 15, 1332-1340.
    • (2005) Glycobiology , vol.15 , pp. 1332-1340
    • Tajiri, M.1    Yoshida, S.2    Wada, Y.3
  • 21
    • 0030830164 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUCl. All putative sites within the tandem repeat are glycosylation targets in vivo
    • Muller, S.; Goletz, S.; Packer, N.; Gooley, A.; Lawson, A. M.; Hanisch, F. G. Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUCl. All putative sites within the tandem repeat are glycosylation targets in vivo. J. Biol. Chem. 1997, 272, 24780-24793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24780-24793
    • Muller, S.1    Goletz, S.2    Packer, N.3    Gooley, A.4    Lawson, A.M.5    Hanisch, F.G.6
  • 22
    • 0031899415 scopus 로고    scopus 로고
    • Localization of O-glycosylatlon sites of MUCl tandem repeats by QTOF ESI mass spectrometry
    • Hanisch, F. G.; Green, B. N.; Bateman, R.; Peter-Katalinlc, J. Localization of O-glycosylatlon sites of MUCl tandem repeats by QTOF ESI mass spectrometry. J.. Mass Spectrom. 1998, 33, 358-362.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 358-362
    • Hanisch, F.G.1    Green, B.N.2    Bateman, R.3    Peter-Katalinlc, J.4
  • 23
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinic, J. Methods in enzymology: O-glycosylation of proteins. Method Enzymol. 2005, 405, 139-171.
    • (2005) Method Enzymol. , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 24
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E.; Coon, J. J.; Schroeder, M. J.; Shabanowitz, J.; Hunt, D. F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A 2004, 101, 9528-9533.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 25
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron, transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner, J.; Premsler, T.; Sickmann, A. Application of electron, transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 2008, 8, 4466-4483.
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 26
    • 0012252007 scopus 로고    scopus 로고
    • Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage
    • Kjeldsen, F.; Haselmann, K. F.; Budnik, B. A; Sorensen, E. S.; Zubarev, R. A. Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal. Chem: 2003, 75, 2355-2361.
    • (2003) Anal. Chem , vol.75 , pp. 2355-2361
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3    Sorensen, E.S.4    Zubarev, R.A.5
  • 27
    • 33847347565 scopus 로고    scopus 로고
    • Structural analysis of O-glycopeptId.es employing negative- And positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry
    • Deguchi, K.; Ito, H.; Baba, T.; Hirabayashi, A; Nakagawa, H.; Fumoto, M.; Hinou, H.; Nishimura, S. Structural analysis of O-glycopeptId.es employing negative- and positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry. Rapid Commun, Mass Spectrom. 2007, 21, 691-698.
    • (2007) Rapid Commun, Mass Spectrom. , vol.21 , pp. 691-698
    • Deguchi, K.1    Ito, H.2    Baba, T.3    Hirabayashi, A.4    Nakagawa, H.5    Fumoto, M.6    Hinou, H.7    Nishimura, S.8
  • 28
    • 67649563273 scopus 로고    scopus 로고
    • Quantification of post-translationally modified peptides of bovine alpha-Crystallin using tandem mass tags and electron transfer dissociation
    • Viner, R. I.; Zhang, T.; Second, T.; Zabrouskov, V. Quantification of post-translationally modified peptides of bovine alpha-Crystallin using tandem mass tags and electron transfer dissociation. J. Proteomics 2009, 72, 874-885.
    • (2009) J. Proteomics , vol.72 , pp. 874-885
    • Viner, R.I.1    Zhang, T.2    Second, T.3    Zabrouskov, V.4
  • 29
    • 67049158217 scopus 로고    scopus 로고
    • Identification of protein O-GlcNAcylation sites using electron. transfer dissociation mass spectrometry on native peptides
    • Chalkley, R. J.; Thalhammer, A.; Schoepfer, R.; Burlingame, A. L. Identification of protein O-GlcNAcylation sites using electron. transfer dissociation mass spectrometry on native peptides. Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 8894-8899.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8894-8899
    • Chalkley, R.J.1    Thalhammer, A.2    Schoepfer, R.3    Burlingame, A.L.4
  • 30
    • 76649126396 scopus 로고    scopus 로고
    • Enrichment and site-mapping of O-Linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation (ETD) mass spectrometry
    • Wang, Z.; Udeshi, N. D.; O'Malley, M.; Shabanowitz, J.; Hunt, D. F.; Hart, G. W. Enrichment and site-mapping of O-Linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation (ETD) mass spectrometry. Mol Cell Proteomics 2010, 9, 153-160.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 153-160
    • Wang, Z.1    Udeshi, N.D.2    O'Malley, M.3    Shabanowitz, J.4    Hunt, D.F.5    Hart, G.W.6
  • 31
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada, Y.; Tajiri, M.; Yoshida, S. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal. Chem. 2004, 76, 6560-6565.
    • (2004) Anal. Chem. , vol.76 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 33
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgAl, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions
    • Mattu, T. S.; Pleass, R. J.; Willis, A. C.; Kilian, M.; Wormald, M. R.; Lellouch, A. C.; Rudd, P. M.; Woof, J. M.; Dwek, R. A. The glycosylation and structure of human serum IgAl, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. J. Biol. Chem. 1998, 273, 2260-2272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5    Lellouch, A.C.6    Rudd, P.M.7    Woof, J.M.8    Dwek, R.A.9
  • 34
    • 0027355459 scopus 로고
    • Defective galactosylation and clearance of IgAl molecules as a possible etiopathogenic factor in IgA nephropathy
    • Mestecky, J.; Tomana, M.; Crowley-Nowick, P. A.; Moldoveanu, Z.; Julian, B. A.; Jackson, S. Defective galactosylation and clearance of IgAl molecules as a possible etiopathogenic factor in IgA nephropathy. Contrib. Nephrol. 1993, 104, 172-182.
    • (1993) Contrib. Nephrol. , vol.104 , pp. 172-182
    • Mestecky, J.1    Tomana, M.2    Crowley-Nowick, P.A.3    Moldoveanu, Z.4    Julian, B.A.5    Jackson, S.6
  • 37
    • 0024642881 scopus 로고
    • A comparative analysis of disease-associated changes in the galactosylation of serum IgG
    • Parekh, R.; Isenberg, D.; Rook, G.; Roltt, I.; Dwek, R.; Rademacher, T. A comparative analysis of disease-associated changes in the galactosylation of serum IgG. J. Autommun.1989, 2, 101-114.
    • (1989) J. Autommun. , vol.2 , pp. 101-114
    • Parekh, R.1    Isenberg, D.2    Rook, G.3    Roltt, I.4    Dwek, R.5    Rademacher, T.6
  • 40
    • 0032759101 scopus 로고    scopus 로고
    • And characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions
    • Amado, M.; Almeida, R.; Schwientek, T.; Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1999, 1473, 35-53.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 35-53
    • Amado, M.1    Almeida, R.2    Schwientek, T.3    Identification, C.H.4
  • 42
    • 0028280439 scopus 로고
    • Structural analysis of the N-glycans from human immunoglobulin Al: Comparison of normal human serum immunoglobulin Al with that isolated from patients with rheumatoid arthritis
    • Field, M. C.; Amatayakul-Chantier, S.; Rademacher, T. W.; Rudd, P. M.; Dwek, R. A. Structural analysis of the N-glycans from human immunoglobulin Al: comparison of normal human serum immunoglobulin Al with that isolated from patients with rheumatoid arthritis. Biochem. 1994, 299 (Pt 1), 261-275.
    • (1994) Biochem. , vol.299 , Issue.PART 1 , pp. 261-275
    • Field, M.C.1    Amatayakul-Chantier, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 43
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 betal, 3-galactosyltransferase
    • Ju, T.; Brewer, K.; D'Souza, A.; Cummings, R. D.; Canfield, W. M. Cloning and expression of human core 1 betal, 3-galactosyltransferase. J. Biol. Chem. 2002, 277, 178-186.
    • (2002) J. Biol. Chem. , vol.277 , pp. 178-186
    • Ju, T.1    Brewer, K.2    D'Souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 47
    • 11144335891 scopus 로고    scopus 로고
    • Mucin biosynthesis: Upregulation of core 2 beta 1,6 N- acetylglucosaminyitransferase by retinoic acid and Th2 cytokines in a human airway epithelial cell line
    • Beum, P. V.; Basma, H.; Bastola, D. R.; Cheng, P. W. Mucin biosynthesis: upregulation of core 2 beta 1,6 N-acetylglucosaminyitransferase by retinoic acid and Th2 cytokines in a human airway epithelial cell line. Am. J. Physiol.; Lune Cell Mol. Physiol. 2005, 288, L116-124.
    • (2005) Am. J. Physiol.; Lune Cell Mol. Physiol. , vol.288
    • Beum, P.V.1    Basma, H.2    Bastola, D.R.3    Cheng, P.W.4
  • 48
    • 0037458698 scopus 로고    scopus 로고
    • Initiation of O-glycan synthesis in IgAl hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2
    • Iwasaki, H.; Zhang, Y.; Tachibana, K.; Gotoh, M.; Kikuchi, N.; Kwon, Y. D.; Togayachi, A.; Kudo, T.; Kubota, T.; Narimatsu, H. Initiation of O-glycan synthesis in IgAl hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. J. Biol. Chem. 2003, 278, 5613-5621.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5613-5621
    • Iwasaki, H.1    Zhang, Y.2    Tachibana, K.3    Gotoh, M.4    Kikuchi, N.5    Kwon, Y.D.6    Togayachi, A.7    Kudo, T.8    Kubota, T.9    Narimatsu, H.10
  • 49
    • 28444496685 scopus 로고    scopus 로고
    • Patients with unsolved congenital disorders of glycosylation type II can be subdivided in six. distinct biochemical groups
    • Wbpereis, S.; Morava, E.; Grunewald, S.; Adamowicz, M.; Huijben, K. M.; Lefeber, D. J.; Wevers, R. A. Patients with unsolved congenital disorders of glycosylation type II can be subdivided in six. distinct biochemical groups. Glycobiology 2005, 15,1312-1319.
    • (2005) Glycobiology , vol.15 , pp. 1312-1319
    • Wbpereis, S.1    Morava, E.2    Grunewald, S.3    Adamowicz, M.4    Huijben, K.M.5    Lefeber, D.J.6    Wevers, R.A.7


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