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Volumn 6, Issue 11, 2007, Pages 4304-4312

A new approach for mapping sialylated N-glycosites in serum proteomes

Author keywords

COFRADIC; Diagonal chromatography; Serum; Sialic acid

Indexed keywords

FETUIN; GLYCOPEPTIDE; OROSOMUCOID; OXYGEN 18; PROTEOME; SIALIC ACID; SIALIDASE;

EID: 36348974133     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0703728     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0034444960 scopus 로고    scopus 로고
    • Achievements and challenges of sialic acid research
    • Schauer, R. Achievements and challenges of sialic acid research. Glycoconj. J. 2000, 17 (7-9), 485-499.
    • (2000) Glycoconj. J , vol.17 , Issue.7-9 , pp. 485-499
    • Schauer, R.1
  • 2
    • 0026069647 scopus 로고
    • Biosynthesis and function of N- and O-substituted sialic acids
    • Schauer, R. Biosynthesis and function of N- and O-substituted sialic acids. Glycobiology 1991, 1 (5), 449-452.
    • (1991) Glycobiology , vol.1 , Issue.5 , pp. 449-452
    • Schauer, R.1
  • 3
    • 31144475414 scopus 로고    scopus 로고
    • Phenotypic changes induced by expression of beta-galactoside alpha2,6 sialyltransferase I in the human colon cancer cell line SW948
    • Chiricolo, M.; Malagolini, N.; Bonfiglioli, S.; Dall'Olio, F. Phenotypic changes induced by expression of beta-galactoside alpha2,6 sialyltransferase I in the human colon cancer cell line SW948. Glycobiology 2006, 16 (2), 146-154.
    • (2006) Glycobiology , vol.16 , Issue.2 , pp. 146-154
    • Chiricolo, M.1    Malagolini, N.2    Bonfiglioli, S.3    Dall'Olio, F.4
  • 4
    • 0034124195 scopus 로고    scopus 로고
    • Transcriptional regulation of human beta-galactoside alpha2,6-sialyltransferase (hST6Gal I) gene during differentiation of the HL-60 cell line
    • Taniguchi, A.; Hasegawa, Y.; Higai, K.; Matsumoto, K. Transcriptional regulation of human beta-galactoside alpha2,6-sialyltransferase (hST6Gal I) gene during differentiation of the HL-60 cell line. Glycobiology 2000, 10 (6), 623-628.
    • (2000) Glycobiology , vol.10 , Issue.6 , pp. 623-628
    • Taniguchi, A.1    Hasegawa, Y.2    Higai, K.3    Matsumoto, K.4
  • 5
    • 0028926833 scopus 로고
    • Characterization of a promoter region supporting transcription of a novel human beta-galactoside alpha-2,6-sialyltransferase transcript in HepG2 cells
    • Aas-Eng, D. A.; Asheim, H. C.; Deggerdal, A.; Smeland, E.; Funderud, S. Characterization of a promoter region supporting transcription of a novel human beta-galactoside alpha-2,6-sialyltransferase transcript in HepG2 cells. Biochim. Biophys. Acta 1995, 1261 (1), 166-169.
    • (1995) Biochim. Biophys. Acta , vol.1261 , Issue.1 , pp. 166-169
    • Aas-Eng, D.A.1    Asheim, H.C.2    Deggerdal, A.3    Smeland, E.4    Funderud, S.5
  • 6
    • 0028328899 scopus 로고
    • Desialylation of metastatic human colorectal carcinoma cells facilitates binding to Kupffer cells
    • Petrick, A. T.; Meterissian, S.; Steele, G., Jr.; Thomas, P. Desialylation of metastatic human colorectal carcinoma cells facilitates binding to Kupffer cells. Clin. Exp. Metastasis 1994, 12 (2), 108-116.
    • (1994) Clin. Exp. Metastasis , vol.12 , Issue.2 , pp. 108-116
    • Petrick, A.T.1    Meterissian, S.2    Steele Jr., G.3    Thomas, P.4
  • 7
    • 17144454454 scopus 로고    scopus 로고
    • Tissue sialic acid and fibronectin levels in human prostatic cancer
    • Suer, S.; Sonmez, H.; Karaaslan, I.; Baloglu, H.; Kokoglu, E. Tissue sialic acid and fibronectin levels in human prostatic cancer. Cancer Lett. 1996, 99 (2), 135-137.
    • (1996) Cancer Lett , vol.99 , Issue.2 , pp. 135-137
    • Suer, S.1    Sonmez, H.2    Karaaslan, I.3    Baloglu, H.4    Kokoglu, E.5
  • 8
    • 0030837804 scopus 로고    scopus 로고
    • Increased sialyl Lewis A expression and fucosyltransferase activity with acquisition of a high metastatic capacity in a colon cancer cell line
    • Yamada, N.; Chung, Y. S.; Takatsuka, S.; Arimoto, Y.; Sawada, T.; Dohi, T.; Sowa, M. Increased sialyl Lewis A expression and fucosyltransferase activity with acquisition of a high metastatic capacity in a colon cancer cell line. Br. J. Cancer 1997, 76 (5), 582-587.
    • (1997) Br. J. Cancer , vol.76 , Issue.5 , pp. 582-587
    • Yamada, N.1    Chung, Y.S.2    Takatsuka, S.3    Arimoto, Y.4    Sawada, T.5    Dohi, T.6    Sowa, M.7
  • 9
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lechn affinity column
    • Yang, Z.; Hancock, W. S. Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lechn affinity column. J. Chromatogr. A 2004, 1053 (1-2), 79-88.
    • (2004) J. Chromatogr. A , vol.1053 , Issue.1-2 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 10
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique
    • Cummings, R. D.; Kornfeld, S. Fractionation of asparagine-linked oligosaccharides by serial lectin-Agarose affinity chromatography. A rapid, sensitive, and specific technique. J. Biol. Chem. 1982, 257 (19), 11235-11240.
    • (1982) J. Biol. Chem , vol.257 , Issue.19 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 11
    • 0013958696 scopus 로고
    • Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A
    • Brown, J. R.; Hartley, B. S. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. Biochem. J. 1966, 101 (1), 214-228.
    • (1966) Biochem. J , vol.101 , Issue.1 , pp. 214-228
    • Brown, J.R.1    Hartley, B.S.2
  • 13
    • 1842423659 scopus 로고    scopus 로고
    • Reversible labeling of cysteine-containing peptides allows their specific chromatographic isolation for non-gel proteome studies
    • Gevaert, K.; Ghesquiere, B.; Staes, A.; Martens, L.; Van Damme, J.; Thomas, G. R.; Vandekerckhove, J. Reversible labeling of cysteine-containing peptides allows their specific chromatographic isolation for non-gel proteome studies. Proteomics 2004, 4 (4), 897-908.
    • (2004) Proteomics , vol.4 , Issue.4 , pp. 897-908
    • Gevaert, K.1    Ghesquiere, B.2    Staes, A.3    Martens, L.4    Van Damme, J.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 14
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K.; Goethals, M.; Martens, L.; Van Damme, J.; Staes, A.; Thomas, G. R.; Vandekerckhove, J. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 2003, 21 (5), 566-569.
    • (2003) Nat. Biotechnol , vol.21 , Issue.5 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 16
    • 33748295546 scopus 로고    scopus 로고
    • Proteome-wide characterization of N-glycosylation events by diagonal chromatography
    • Ghesquiere, B.; Van Damme, J.; Martens, L.; Vandekerckhove, J.; Gevaert, K. Proteome-wide characterization of N-glycosylation events by diagonal chromatography. J. Proteome Res. 2006, 5 (9), 2438-2447.
    • (2006) J. Proteome Res , vol.5 , Issue.9 , pp. 2438-2447
    • Ghesquiere, B.1    Van Damme, J.2    Martens, L.3    Vandekerckhove, J.4    Gevaert, K.5
  • 17
    • 33845425069 scopus 로고    scopus 로고
    • A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes
    • Hanoulle, X.; Damme, J. V.; Staes, A.; Martens, L.; Goethals, M.; Vandekerckhove, J.; Gevaert, K. A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes. J. Proteome Res. 2006, 5 (12), 3438-3445.
    • (2006) J. Proteome Res , vol.5 , Issue.12 , pp. 3438-3445
    • Hanoulle, X.1    Damme, J.V.2    Staes, A.3    Martens, L.4    Goethals, M.5    Vandekerckhove, J.6    Gevaert, K.7
  • 20
    • 33744986528 scopus 로고    scopus 로고
    • Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: The proteome of human multipotent adult progenitor cells
    • Gevaert, K.; Pinxteren, J.; Demol, H.; Hugelier, K.; Staes, A.; Van Damme, J.; Martens, L.; Vandekerckhove, J. Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: the proteome of human multipotent adult progenitor cells. J. Proteome Res. 2006, 5 (6), 1415-1428.
    • (2006) J. Proteome Res , vol.5 , Issue.6 , pp. 1415-1428
    • Gevaert, K.1    Pinxteren, J.2    Demol, H.3    Hugelier, K.4    Staes, A.5    Van Damme, J.6    Martens, L.7    Vandekerckhove, J.8
  • 21
    • 4444271864 scopus 로고    scopus 로고
    • Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18
    • Staes, A.; Demol, H.; Van Damme, J.; Martens, L.; Vandekerckhove, J.; Gevaert, K. Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18. J. Proteome Res. 2004, 3 (4), 786-791.
    • (2004) J. Proteome Res , vol.3 , Issue.4 , pp. 786-791
    • Staes, A.1    Demol, H.2    Van Damme, J.3    Martens, L.4    Vandekerckhove, J.5    Gevaert, K.6
  • 22
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20 (18), 3551-3567.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 23
    • 0005917528 scopus 로고
    • Studies on fetuin, a glycoprotein of fetal serum. II. Nature of the carbohydrate units
    • Spiro, R. G. Studies on fetuin, a glycoprotein of fetal serum. II. Nature of the carbohydrate units. J. Biol. Chem. 1962, 237 382-388.
    • (1962) J. Biol. Chem , vol.237 , pp. 382-388
    • Spiro, R.G.1
  • 24
    • 0024316209 scopus 로고
    • Separation of the complex asparagine-linked oligosaccharides of the glycoprotein fetuin and elucidation of three triantennary structures having sialic acids linked only to galactose residues
    • Bendiak, B.; Harris-Brandts, M.; Michnick, S. W.; Carver, J. P.; Cumming, D. A. Separation of the complex asparagine-linked oligosaccharides of the glycoprotein fetuin and elucidation of three triantennary structures having sialic acids linked only to galactose residues. Biochemistry 1989, 28 (15), 6491-6499.
    • (1989) Biochemistry , vol.28 , Issue.15 , pp. 6491-6499
    • Bendiak, B.1    Harris-Brandts, M.2    Michnick, S.W.3    Carver, J.P.4    Cumming, D.A.5
  • 25
    • 0024356890 scopus 로고
    • Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine
    • Cumming, D. A.; Hellerqvist, C. G.; Harris-Brandts, M.; Michnick, S. W.; Carver, J. P.; Bendiak, B. Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine. Biochemistry 1989, 28 (15), 6500-6512.
    • (1989) Biochemistry , vol.28 , Issue.15 , pp. 6500-6512
    • Cumming, D.A.1    Hellerqvist, C.G.2    Harris-Brandts, M.3    Michnick, S.W.4    Carver, J.P.5    Bendiak, B.6
  • 26
    • 0026574265 scopus 로고
    • Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein
    • Treuheit, M. J.; Costello, C. E.; Halsall, H. B. Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein. Biochem. J. 1992, 283 (Pt 1), 105-112.
    • (1992) Biochem. J , vol.283 , Issue.PART 1 , pp. 105-112
    • Treuheit, M.J.1    Costello, C.E.2    Halsall, H.B.3
  • 28
    • 27944475591 scopus 로고    scopus 로고
    • Comparative glycoproteomics of N-linked complex-type glycoforms containing sialic acid in human serum
    • Qiu, R.; Regnier, F. E. Comparative glycoproteomics of N-linked complex-type glycoforms containing sialic acid in human serum. Anal. Chem. 2005, 77 (22), 7225-7231.
    • (2005) Anal. Chem , vol.77 , Issue.22 , pp. 7225-7231
    • Qiu, R.1    Regnier, F.E.2
  • 29
    • 33644690335 scopus 로고    scopus 로고
    • Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach
    • Lewandrowski, U.; Moebius, J.; Walter, U.; Sickmann, A. Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol. Cell. Proteomics 2006, 5 (2), 226-233.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.2 , pp. 226-233
    • Lewandrowski, U.1    Moebius, J.2    Walter, U.3    Sickmann, A.4
  • 30
    • 0037176224 scopus 로고    scopus 로고
    • Use of a lectin affinity selector in the search for unusual glycosylation in proteomics
    • Xiong, L.; Regnier, F. E. Use of a lectin affinity selector in the search for unusual glycosylation in proteomics. J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. 2002, 782 (1-2), 405-418.
    • (2002) J. Chromatogr., B: Anal. Technol. Biomed. Life Sci , vol.782 , Issue.1-2 , pp. 405-418
    • Xiong, L.1    Regnier, F.E.2
  • 31
    • 0022003140 scopus 로고    scopus 로고
    • Tarentino, A. L.; Gomez, C. M.; Plummer, T. H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 1985, 24 (17), 4665-4671.
    • Tarentino, A. L.; Gomez, C. M.; Plummer, T. H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 1985, 24 (17), 4665-4671.
  • 33
    • 33748788003 scopus 로고    scopus 로고
    • Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis
    • Krokhin, O. V.; Antonovici, M.; Ens, W.; Wilkins, J. A.; Standing, K. G. Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis. Anal. Chem. 2006, 78 (18), 6645-6650.
    • (2006) Anal. Chem , vol.78 , Issue.18 , pp. 6645-6650
    • Krokhin, O.V.1    Antonovici, M.2    Ens, W.3    Wilkins, J.A.4    Standing, K.G.5
  • 34
    • 18144419694 scopus 로고    scopus 로고
    • Use of multidimensional lectin affinity chromatography in differential glycoproteomics
    • Qiu, R.; Regnier, F. E. Use of multidimensional lectin affinity chromatography in differential glycoproteomics. Anal. Chem. 2005, 77 (9), 2802-2809.
    • (2005) Anal. Chem , vol.77 , Issue.9 , pp. 2802-2809
    • Qiu, R.1    Regnier, F.E.2
  • 35
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: Application to pancreatic cancer serum
    • Zhao, J.; Simeone, D. M.; Heidt, D.; Anderson, M. A.; Lubman, D. M. Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J. Proteome Res. 2006, 5 (7), 1792-1802.
    • (2006) J. Proteome Res , vol.5 , Issue.7 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 36
    • 0001481450 scopus 로고
    • The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens
    • Cassidy, J. T.; Jourdian, G. W.; Roseman, S. The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens. J. Biol. Chem. 1965, 240 (9), 3501-3506.
    • (1965) J. Biol. Chem , vol.240 , Issue.9 , pp. 3501-3506
    • Cassidy, J.T.1    Jourdian, G.W.2    Roseman, S.3
  • 38
    • 36349019291 scopus 로고    scopus 로고
    • Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes
    • Lewandrowski, U.; Zahedi, R. P.; Moebius, J.; Walter, U.; Sickmann, A. Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes. Mol. Cell. Proteomics 2007.
    • (2007) Mol. Cell. Proteomics
    • Lewandrowski, U.1    Zahedi, R.P.2    Moebius, J.3    Walter, U.4    Sickmann, A.5
  • 39
    • 0028827236 scopus 로고    scopus 로고
    • Turner, G. A. Haptoglobin. A potential reporter molecule for glycosylation changes in disease. Adv. Exp. Med. Biol. 1995, 376, 231-238.
    • Turner, G. A. Haptoglobin. A potential reporter molecule for glycosylation changes in disease. Adv. Exp. Med. Biol. 1995, 376, 231-238.
  • 40
    • 33750105559 scopus 로고    scopus 로고
    • Study of serum haptoglobin and its glycoforms in the diagnosis of hepatocellular carcinoma: A glycoproteomic approach
    • Ang, I. L.; Poon, T. C.; Lai, P. B.; Chan, A. T.; Ngai, S. M.; Hui, A. Y.; Iohnson, P. J.; Sung, J. J. Study of serum haptoglobin and its glycoforms in the diagnosis of hepatocellular carcinoma: a glycoproteomic approach. J. Proteome Res. 2006, 5 (10), 2691-2700.
    • (2006) J. Proteome Res , vol.5 , Issue.10 , pp. 2691-2700
    • Ang, I.L.1    Poon, T.C.2    Lai, P.B.3    Chan, A.T.4    Ngai, S.M.5    Hui, A.Y.6    Iohnson, P.J.7    Sung, J.J.8
  • 42
    • 0018691942 scopus 로고
    • Inhibition of platelet aggregation by native and desialised alpha-1 acid glycoprotein
    • Costello, M.; Fiedel, B. A.; Gewurz, H. Inhibition of platelet aggregation by native and desialised alpha-1 acid glycoprotein. Nature 1979, 281 (5733), 677-678.
    • (1979) Nature , vol.281 , Issue.5733 , pp. 677-678
    • Costello, M.1    Fiedel, B.A.2    Gewurz, H.3
  • 43
    • 24044534176 scopus 로고    scopus 로고
    • Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response
    • Chavan, M. M.; Kawle, P. D.; Mehta, N. G. Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response. Glycobiology 2005, 15 (9), 838-848.
    • (2005) Glycobiology , vol.15 , Issue.9 , pp. 838-848
    • Chavan, M.M.1    Kawle, P.D.2    Mehta, N.G.3
  • 44
    • 0027410273 scopus 로고
    • Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera
    • De Graaf, T. W.; Van der Stelt, M. E.; Anbergen, M. G.; van Dijk, W. Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera. J. Exp. Med. 1993, 177 (3), 657-666.
    • (1993) J. Exp. Med , vol.177 , Issue.3 , pp. 657-666
    • De Graaf, T.W.1    Van der Stelt, M.E.2    Anbergen, M.G.3    van Dijk, W.4
  • 45
    • 0030668904 scopus 로고    scopus 로고
    • Williams, J. P.; Weiser, M. R.; Pechet, T. T.; Kobzik, L.; Moore, F. D., Jr.; Hechtman, H. B. alpha 1-Acid glycoprotein reduces local and remote injuries after intestinal ischemia in the rat. Am. J. Physiol. 1997, 273 (5 Pt 1), G1031-G1035.
    • Williams, J. P.; Weiser, M. R.; Pechet, T. T.; Kobzik, L.; Moore, F. D., Jr.; Hechtman, H. B. alpha 1-Acid glycoprotein reduces local and remote injuries after intestinal ischemia in the rat. Am. J. Physiol. 1997, 273 (5 Pt 1), G1031-G1035.
  • 46
    • 0022121876 scopus 로고
    • Isolation and characterization of influenza C virus inhibitor in rat serum
    • Kitame, F.; Nakamura, K.; Saito, A.; Sinohara, H.; Homma, M. Isolation and characterization of influenza C virus inhibitor in rat serum. Virus Res. 1985, 3 (3), 231-244.
    • (1985) Virus Res , vol.3 , Issue.3 , pp. 231-244
    • Kitame, F.1    Nakamura, K.2    Saito, A.3    Sinohara, H.4    Homma, M.5
  • 48
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese, S.; Reidegeld, K. A.; Meyer, H. E.; Warscheid, B. Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research. Proteomics 2007, 7 (3), 340-350.
    • (2007) Proteomics , vol.7 , Issue.3 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3    Warscheid, B.4


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