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Volumn 25, Issue 3, 2008, Pages 213-224

Glycosylation of the two O-glycosylated domains of human MUC2 mucin in patients transposed with artificial urinary bladders constructed from proximal colonic tissue

Author keywords

Artificial urinary bladder; Glycosylation; Mass spectrometry; MUC2

Indexed keywords

BLOOD GROUP A ANTIGEN; BLOOD GROUP B ANTIGEN; GALACTOSAMINE; MUCIN 2; N ACETYLGALACTOSAMINITOL; OLIGOSACCHARIDE; SODIUM BOROHYDRIDE; TUMOR ANTIGEN; UNCLASSIFIED DRUG;

EID: 40949114730     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-007-9079-3     Document Type: Article
Times cited : (17)

References (57)
  • 2
    • 0035146448 scopus 로고    scopus 로고
    • Database analysis of O-glycosylation sites in proteins
    • Christlet, T.H.T., Veluraja, K.: Database analysis of O-glycosylation sites in proteins. Biophys. J. 80, 952-960 (2001)
    • (2001) Biophys. J. , vol.80 , pp. 952-960
    • Christlet, T.H.T.1    Veluraja, K.2
  • 3
    • 40949132398 scopus 로고
    • The specificity of UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides
    • Elhammer, A.P., Poorman, R.A., Brown, E., Maggiora, L.L., Hoogerheide, J.G., Kezdy, F.J.: The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides. J. Biol. Chem. 275, 1057-1064 (1993)
    • (1993) J. Biol. Chem. , vol.275 , pp. 1057-1064
    • Elhammer, A.P.1    Poorman, R.A.2    Brown, E.3    Maggiora, L.L.4    Hoogerheide, J.G.5    Kezdy, F.J.6
  • 4
    • 0031809552 scopus 로고    scopus 로고
    • NetOglyc: Prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility
    • Hansen, J.E., Lund, O., Gooley, A.A., Williams, K.L., Brunak, S.: NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconj. J. 15, 115-130 (1998)
    • (1998) Glycoconj. J. , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Gooley, A.A.3    Williams, K.L.4    Brunak, S.5
  • 5
    • 0025865091 scopus 로고
    • Amino acid distributions around O-linked glycosylation sites
    • Wilson, I.B., Gavel, Y., von Heijne, G.: Amino acid distributions around O-linked glycosylation sites. Biochem. J. 275, 529-534 (1991)
    • (1991) Biochem. J. , vol.275 , pp. 529-534
    • Wilson, I.B.1    Gavel, Y.2    Von Heijne, G.3
  • 6
    • 0028289734 scopus 로고
    • Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine:polypeptide N- acetylgalactosaminyltransferase. Studies with the MUC1 tandem repeat
    • Nishimori, I., Johnson, N.R., Sanderson, S.D., Perini, F., Mountjoy, K., Cerny, R.L., Gross, M.L., Hollingsworth, M.A.: Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase. Studies with the MUC1 tandem repeat. J. Biol. Chem. 269, 16123-16130 (1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 16123-16130
    • Nishimori, I.1    Johnson, N.R.2    Sanderson, S.D.3    Perini, F.4    Mountjoy, K.5    Cerny, R.L.6    Gross, M.L.7    Hollingsworth, M.A.8
  • 7
    • 0026470310 scopus 로고
    • Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine:polypeptide N- acetylgalactosaminyltransferase. Studies with the MUC1 tandem repeat
    • O'Connel, B.C., Hagen, F.K., Tabak, L.A.: Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase. Studies with the MUC1 tandem repeat. J. Biol. Chem. 267, 25010-25018 (1992)
    • (1992) J. Biol. Chem. , vol.267 , pp. 25010-25018
    • O'Connel, B.C.1    Hagen, F.K.2    Tabak, L.A.3
  • 8
    • 0030764614 scopus 로고    scopus 로고
    • Discovery of the shortest sequence motif for high level mucin-type O-glycosylation
    • Yoshida, A., Suzuki, M., Ikenaga, H., Takeuchi, M.: Discovery of the shortest sequence motif for high level mucin-type O-glycosylation. J. Biol. Chem. 272, 16884-16888 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 16884-16888
    • Yoshida, A.1    Suzuki, M.2    Ikenaga, H.3    Takeuchi, M.4
  • 9
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • Ten Hagen, K.G., Fritz, T.A., Tabak, L.A.: All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13, 1R-16R (2003)
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 10
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-alpha- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt, M.R., Hang, H.C., Ten Hagen, K.G., Rarick, J., Gerken, T.A., Tabak, L.A., Bertozzi, C.R.: Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem. Biol. 11, 1009-1016 (2004)
    • (2004) Chem. Biol. , vol.11 , pp. 1009-1016
    • Pratt, M.R.1    Hang, H.C.2    Ten Hagen, K.G.3    Rarick, J.4    Gerken, T.A.5    Tabak, L.A.6    Bertozzi, C.R.7
  • 11
    • 0025064482 scopus 로고
    • Control of mucin synthesis: The peptide portion of synthetic O-glycopeptide substrates influences the activity of O-glycan core 1 UDPgalactose:N-acetyl-alpha-galactosaminyl-R beta 3-galactosyltransferase
    • Brockhausen, I., Moller, G., Merz, G., Adermann, K., Paulsen, H.: Control of mucin synthesis: the peptide portion of synthetic O-glycopeptide substrates influences the activity of O-glycan core 1 UDPgalactose:N-acetyl-alpha- galactosaminyl-R beta 3-galactosyltransferase. Biochemistry 29, 10206-10212 (1990)
    • (1990) Biochemistry , vol.29 , pp. 10206-10212
    • Brockhausen, I.1    Moller, G.2    Merz, G.3    Adermann, K.4    Paulsen, H.5
  • 12
    • 0039374466 scopus 로고    scopus 로고
    • Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyl-transferases. Site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions
    • Hanisch, F.G., Muller, S., Hassan, H., Clausen, H., Zachara, N., Gooley, A.A., Paulsen, H., Alving, K., Peter-Katalinic, J.: Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyl-transferases. Site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions. J. Biol. Chem. 274, 9946-9954 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 9946-9954
    • Hanisch, F.G.1    Muller, S.2    Hassan, H.3    Clausen, H.4    Zachara, N.5    Gooley, A.A.6    Paulsen, H.7    Alving, K.8    Peter-Katalinic, J.9
  • 13
    • 0028179379 scopus 로고
    • UDPgalactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D- galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates
    • Granovsky, M., Bielfeldt, T., Peters, S., Paulsen, H., Meldal, M., Brockhausen, J., Brockhausen, I.: UDPgalactose:glycoprotein-N-acetyl-D- galactosamine 3-beta-D-galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates. Eur. J. Biochem. 221, 1039-1046 (1994)
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1039-1046
    • Granovsky, M.1    Bielfeldt, T.2    Peters, S.3    Paulsen, H.4    Meldal, M.5    Brockhausen, J.6    Brockhausen, I.7
  • 14
    • 0032500663 scopus 로고    scopus 로고
    • Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence
    • Gerken, T.A., Owens, C.L., Pasumarthy, M.: Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence. J. Biol. Chem. 273, 26580-26588 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 26580-26588
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 15
    • 0033603316 scopus 로고    scopus 로고
    • High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells
    • Muller, S., Alving, K., Peter-Katalinic, J., Zachara, N., Gooley, A.A., Hanisch, F.G.: High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells. J. Biol. Chem. 274, 18165-18172 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 18165-18172
    • Muller, S.1    Alving, K.2    Peter-Katalinic, J.3    Zachara, N.4    Gooley, A.A.5    Hanisch, F.G.6
  • 16
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins, P.P., McEver, R.P., Cummings, R.D.: Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J. Biol. Chem. 271, 18732-18742 (1996)
    • (1996) J. Biol. Chem. , vol.271 , pp. 18732-18742
    • Wilkins, P.P.1    McEver, R.P.2    Cummings, R.D.3
  • 17
    • 0030894597 scopus 로고    scopus 로고
    • Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:galnac transferase peptide binding site
    • Gerken, T.A., Owens, C.L., Pasumarthy, M.: Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:galnac transferase peptide binding site. J. Biol. Chem. 272, 9709-9719 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 9709-9719
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 18
    • 1842531413 scopus 로고    scopus 로고
    • Kinetic modeling confirms the biosynthesis of mucin core 1 (beta-Gal(1-3) alpha-GalNAc-O-Ser/Thr) O-glycan structures are modulated by neighboring glycosylation effects
    • Gerken, T.A.: Kinetic modeling confirms the biosynthesis of mucin core 1 (beta-Gal(1-3) alpha-GalNAc-O-Ser/Thr) O-glycan structures are modulated by neighboring glycosylation effects. Biochemistry 43, 4137-4142 (2004)
    • (2004) Biochemistry , vol.43 , pp. 4137-4142
    • Gerken, T.A.1
  • 19
    • 3342960623 scopus 로고    scopus 로고
    • Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyl transferases T1 and T2: Kinetic modeling of the porcine and canine submaxillary gland mucin tandem repeats
    • Gerken, T.A., Tep, C., Rarick, J.: Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and canine submaxillary gland mucin tandem repeats. Biochemistry 43, 9888-9900 (2004)
    • (2004) Biochemistry , vol.43 , pp. 9888-9900
    • Gerken, T.A.1    Tep, C.2    Rarick, J.3
  • 21
    • 0028106680 scopus 로고
    • Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of the amino terminus and overall sequence similarity to prepro-von Willebrand factor
    • Gum, J.R., Hicks, J.W., Toribara, N.W., Siddiki, B., Kim, Y.S.: Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of the amino terminus and overall sequence similarity to prepro-von Willebrand factor. J. Biol. Chem. 269, 2440-2446 (1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 2440-2446
    • Gum, J.R.1    Hicks, J.W.2    Toribara, N.W.3    Siddiki, B.4    Kim, Y.S.5
  • 22
    • 0033023242 scopus 로고    scopus 로고
    • Studies on the "insoluble" glycoprotein complex from human colon. Identification of reduction-insensitive MUC2 oligomers and C-terminal cleavage
    • Herrmann, A., Davies, J.R., Lindell, G., Martensson, S., Packer, N.H., Swallow, D.M., Carlstedt, I.: Studies on the "insoluble" glycoprotein complex from human colon. Identification of reduction-insensitive MUC2 oligomers and C-terminal cleavage. J. Biol. Chem. 274, 15828-15836 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 15828-15836
    • Herrmann, A.1    Davies, J.R.2    Lindell, G.3    Martensson, S.4    Packer, N.H.5    Swallow, D.M.6    Carlstedt, I.7
  • 23
    • 0026802436 scopus 로고
    • The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region
    • Gum Jr, J.R., Hicks, J.W., Toribara, N.W., Rothe, E.M., Lagace, R.E., Kim, Y.S.: The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region. J. Biol. Chem. 267, 21375-21383 (1992)
    • (1992) J. Biol. Chem. , vol.267 , pp. 21375-21383
    • Gum Jr., J.R.1    Hicks, J.W.2    Toribara, N.W.3    Rothe, E.M.4    Lagace, R.E.5    Kim, Y.S.6
  • 26
    • 16644377467 scopus 로고    scopus 로고
    • Mucus production after transposition of intestinal segments into the urinary tract
    • N'Dow, J., Pearson, J., Neal, D.: Mucus production after transposition of intestinal segments into the urinary tract. World J. Urol. 22, 178-185 (2004)
    • (2004) World J. Urol. , vol.22 , pp. 178-185
    • N'Dow, J.1    Pearson, J.2    Neal, D.3
  • 27
    • 0037236839 scopus 로고    scopus 로고
    • Metabolic and functional consequences of urinary reconstruction with bowel
    • Gerharz, E.W., Turner, W.H., Kalbe, T., Woodhouse, C.R.: Metabolic and functional consequences of urinary reconstruction with bowel. Br. J. Urol. Int. 91, 143-149 (2003)
    • (2003) Br. J. Urol. Int. , vol.91 , pp. 143-149
    • Erharz, E.W.1    Turner, W.H.2    Kalbe, T.3    Woodhouse, C.R.4
  • 28
    • 0036282018 scopus 로고    scopus 로고
    • Health related quality of life assessment after radical cystectomy: Comparison of ileal conduit with continent orthotopic neobladder
    • Dutta, S.C., Chang, S.C., Coffey, C.S., Smith Jr., J.A., Jack, G., Cookson, M.S.: Health related quality of life assessment after radical cystectomy: comparison of ileal conduit with continent orthotopic neobladder. J. Urol. 168, 164-167 (2002)
    • (2002) J. Urol. , vol.168 , pp. 164-167
    • Dutta, S.C.1    Chang, S.C.2    Coffey, C.S.3    Smith Jr., J.A.4    Jack, G.5    Cookson, M.S.6
  • 30
    • 0024361842 scopus 로고
    • Voiding pattern, urinary volume, composition and bacterial contamination in patients with urinary-diversion via a continent ileal reservoir
    • Akerlund, S., Berglund, B., Kock, N.G., Philipson, B.M.: Voiding pattern, urinary volume, composition and bacterial contamination in patients with urinary-diversion via a continent ileal reservoir. Br J. Urol. 63, 619-623 (1989)
    • (1989) Br J. Urol. , vol.63 , pp. 619-623
    • Akerlund, S.1    Berglund, B.2    Kock, N.G.3    Philipson, B.M.4
  • 31
    • 0024992323 scopus 로고
    • Rupture of ileal neobladder due to urethral obstruction by mucous plug
    • Haupt, G., Pannek, J., Knopf, H.J., Schulze, H., Senge, T.: Rupture of ileal neobladder due to urethral obstruction by mucous plug. J. Urol. 144, 740-741 (1990)
    • (1990) J. Urol. , vol.144 , pp. 740-741
    • Haupt, G.1    Pannek, J.2    Knopf, H.J.3    Schulze, H.4    Senge, T.5
  • 32
    • 0023521437 scopus 로고
    • Secretomotor function of intestinal segments used in lower urinary tract reconstruction
    • Murray, K., Nurse, D.E., Mundy, A.R.: Secretomotor function of intestinal segments used in lower urinary tract reconstruction. Br. J. Urol. 60, 532-535 (1987)
    • (1987) Br. J. Urol. , vol.60 , pp. 532-535
    • Murray, K.1    Nurse, D.E.2    Mundy, A.R.3
  • 33
    • 0033817289 scopus 로고    scopus 로고
    • Mucin gene expression in human urothelium and in intestinal segments transposed into the urinary tract
    • N'Dow, J., Pearson, J.P., Bennett, M.K., Neal, D.E., Robson, C.N.: Mucin gene expression in human urothelium and in intestinal segments transposed into the urinary tract. J. Urol. 164, 1398-1404 (2000)
    • (2000) J. Urol. , vol.164 , pp. 1398-1404
    • N'Dow, J.1    Pearson, J.P.2    Bennett, M.K.3    Neal, D.E.4    Robson, C.N.5
  • 34
    • 0035043573 scopus 로고    scopus 로고
    • Reducing mucus production after urinary reconstruction: A prospective randomized trial
    • N'Dow, J., Robson, C.N., Matthews, J.N., Neal, D.E., Pearson, J.P.: Reducing mucus production after urinary reconstruction: a prospective randomized trial. J. Urol. 165, 1433-1440 (2001)
    • (2001) J. Urol. , vol.165 , pp. 1433-1440
    • N'Dow, J.1    Robson, C.N.2    Matthews, J.N.3    Neal, D.E.4    Pearson, J.P.5
  • 35
    • 0022260871 scopus 로고
    • Oligosaccharide structures of human colonic mucin
    • Podolsky, D.K.: Oligosaccharide structures of human colonic mucin. J. Biol. Chem. 260, 8262-8271 (1985)
    • (1985) J. Biol. Chem. , vol.260 , pp. 8262-8271
    • Podolsky, D.K.1
  • 36
    • 0022373135 scopus 로고
    • Oligosaccharide structures of isolated human colonic mucin species
    • Podolsky, D.K.: Oligosaccharide structures of isolated human colonic mucin species. J. Biol. Chem. 260, 15510-15515 (1985)
    • (1985) J. Biol. Chem. , vol.260 , pp. 15510-15515
    • Podolsky, D.K.1
  • 37
    • 0035884645 scopus 로고    scopus 로고
    • a-antigen-like structures carried on core 3 are prominent features of glycans from the mucin of normal human descending colon
    • a-antigen-like structures carried on core 3 are prominent features of glycans from the mucin of normal human descending colon. Biochem. J. 358, 657-664 (2001)
    • (2001) Biochem. J. , vol.358 , pp. 657-664
    • Capon, C.1    Maes, E.2    Michalski, J.C.3    Leffler, H.4    Kim, Y.S.5
  • 39
    • 10644254423 scopus 로고    scopus 로고
    • Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract
    • Robbe, C., Capon, C., Coddeville, B., Michalski, J.C.: Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract. Biochem. J. 384, 307-16 (2004)
    • (2004) Biochem. J. , vol.384 , pp. 307-16
    • Robbe, C.1    Capon, C.2    Coddeville, B.3    Michalski, J.C.4
  • 40
    • 0025666748 scopus 로고
    • The detubularized right colonic segment as urinary reservoir: Evolution of technique for continent diversion
    • Mansson, W., Davidsson, T., Colleen, S.: The detubularized right colonic segment as urinary reservoir: evolution of technique for continent diversion. J. Urol. 144, 1359-1361 (1990)
    • (1990) J. Urol. , vol.144 , pp. 1359-1361
    • Mansson, W.1    Davidsson, T.2    Colleen, S.3
  • 41
    • 0014408452 scopus 로고
    • Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins
    • Carlson, D.M.: Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins. J. Biol. Chem. 243, 616-626 (1968)
    • (1968) J. Biol. Chem. , vol.243 , pp. 616-626
    • Carlson, D.M.1
  • 42
    • 0016758296 scopus 로고
    • Characterization by gas-liquid chromatography, mass spectrometry and proton-magnetic resonance spectroscopy of pertrimethylsilyl methyl glycosides obtained in the methanolysis of glycoproteins and glycopeptides
    • Kamerling, J.P., Gerwig, G.J., Vliegenthart, J.F., Clamp, J.R.: Characterization by gas-liquid chromatography, mass spectrometry and proton-magnetic resonance spectroscopy of pertrimethylsilyl methyl glycosides obtained in the methanolysis of glycoproteins and glycopeptides. Biochem. J. 151, 491-495 (1975)
    • (1975) Biochem. J. , vol.151 , pp. 491-495
    • Kamerling, J.P.1    Gerwig, G.J.2    Vliegenthart, J.F.3    Clamp, J.R.4
  • 44
    • 1242339631 scopus 로고    scopus 로고
    • Diagnostic ions for the rapid analysis by nano-electrospray ionization quadrupole time-of-flight mass spectrometry of O-glycans from human mucins
    • Robbe, C., Capon, C., Coddeville, B., Michalski, J.C.: Diagnostic ions for the rapid analysis by nano-electrospray ionization quadrupole time-of-flight mass spectrometry of O-glycans from human mucins. Rapid Commun. Mass Spectrom. 18, 412-420 (2004)
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 412-420
    • Robbe, C.1    Capon, C.2    Coddeville, B.3    Michalski, J.C.4
  • 45
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon, B., Costello, C.E.: A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 5, 397-409 (1988)
    • (1988) Glycoconj. J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 46
    • 0029917911 scopus 로고    scopus 로고
    • Sulphated mucin oligosaccharides from porcine small intestine analysed by four-sector tandem mass spectrometry
    • Karlsson, N.G., Karlsson, H., Hansson, G.C.: Sulphated mucin oligosaccharides from porcine small intestine analysed by four-sector tandem mass spectrometry. J. Mass Spectrom. 31, 560-572 (1996)
    • (1996) J. Mass Spectrom. , vol.31 , pp. 560-572
    • Karlsson, N.G.1    Karlsson, H.2    Hansson, G.C.3
  • 48
    • 1242337458 scopus 로고    scopus 로고
    • Mucins and mucin binding proteins in colorectal cancer
    • Byrd, J.C., Bresalier, R.S.: Mucins and mucin binding proteins in colorectal cancer. Cancer Metastasis Rev. 23, 77-99 (2004)
    • (2004) Cancer Metastasis Rev. , vol.23 , pp. 77-99
    • Byrd, J.C.1    Bresalier, R.S.2
  • 49
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • Kim, Y.J., Varki, A.: Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj. J. 14, 569-576 (1997)
    • (1997) Glycoconj. J. , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 50
    • 0029813776 scopus 로고    scopus 로고
    • Cell surface carbohydrates as prognostic markers in human carcinomas
    • Dabelsteen, E.: Cell surface carbohydrates as prognostic markers in human carcinomas. J. Pathol. 179, 358-69 (1996)
    • (1996) J. Pathol. , vol.179 , pp. 358-69
    • Dabelsteen, E.1
  • 51
    • 0022608782 scopus 로고
    • The microbial flora of the continent cecal urinary reservoir, its stoma and the peristomal skin
    • Mansson, W., Colleen, S., Mardh, P.A.: the microbial flora of the continent cecal urinary reservoir, its stoma and the peristomal skin. J. Urol. 135, 247-250 (1986)
    • (1986) J. Urol. , vol.135 , pp. 247-250
    • Mansson, W.1    Colleen, S.2    Mardh, P.A.3
  • 52
    • 16644395789 scopus 로고    scopus 로고
    • Bladder, bowel and bugs-bacteriuria in patients with intestinal urinary diversion
    • Wullt, B., Agace, W., Mansson, W.: Bladder, bowel and bugs-bacteriuria in patients with intestinal urinary diversion. World J. Urol. 22, 186-195 (2004)
    • (2004) World J. Urol. , vol.22 , pp. 186-195
    • Wullt, B.1    Agace, W.2    Mansson, W.3
  • 53
    • 0034922516 scopus 로고    scopus 로고
    • Increasing the intra-Golgi pH of cultured LS174T goblet-differentiated cells mimics the decreased mucin sulfation and increased Thomsen-Friedenreich antigen (Gal beta1-3GalNac alpha-) expression seen in colon cancer
    • Campbell, B.J., Rowe, B.E., Leiper, K., Rhodes, J.M.: Increasing the intra-Golgi pH of cultured LS174T goblet-differentiated cells mimics the decreased mucin sulfation and increased Thomsen-Friedenreich antigen (Gal beta1-3GalNac alpha-) expression seen in colon cancer. Glycobiology 11, 385-393 (2001)
    • (2001) Glycobiology , vol.11 , pp. 385-393
    • Campbell, B.J.1    Rowe, B.E.2    Leiper, K.3    Rhodes, J.M.4
  • 55
    • 0025788220 scopus 로고
    • UDP-GalNAc:NeuAc alpha 2,3Gal beta-R (GalNAc to Gal) beta 1,4-N-acetylgalactosaminyltransferase responsible for the Sda specificity in human colon carcinoma CaCo-2 cell line
    • Malagolini, N., Dall'Olio, F., Serafini-Cessi, F.: UDP-GalNAc:NeuAc alpha 2,3Gal beta-R (GalNAc to Gal) beta 1,4-N-acetylgalactosaminyltransferase responsible for the Sda specificity in human colon carcinoma CaCo-2 cell line. Biochem. Biophys. Res. Commun. 180, 681-686 (1991)
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 681-686
    • Malagolini, N.1    Dall'Olio, F.2    Serafini-Cessi, F.3
  • 57
    • 16644399674 scopus 로고    scopus 로고
    • Tumour formation within intestinal segments transposed to the urinary tract
    • Pickard, R.: Tumour formation within intestinal segments transposed to the urinary tract. World J. Urol. 22, 227-234 (2004)
    • (2004) World J. Urol. , vol.22 , pp. 227-234
    • Pickard, R.1


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