메뉴 건너뛰기




Volumn 436, Issue 2, 2013, Pages 252-258

Sialic acid-dependent attachment of mucins from three mouse strains to Entamoeba histolytica

Author keywords

Entamoeba histolytica; Lectin; Mucin; O glycan; Sialic acid

Indexed keywords

GLYCAN; GLYCOPROTEIN; MUCIN; SIALIC ACID; SIALIDASE;

EID: 84879604947     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.05.085     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 0023555730 scopus 로고
    • Isolation of the galactose-binding lectin that mediates the in vitro adherence of Entamoeba histolytica
    • Petri W.A., Smith R.D., Schlesinger P.H., et al. Isolation of the galactose-binding lectin that mediates the in vitro adherence of Entamoeba histolytica. J. Clin. Invest. 1987, 80:1238-1244.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1238-1244
    • Petri, W.A.1    Smith, R.D.2    Schlesinger, P.H.3
  • 2
    • 0036405392 scopus 로고    scopus 로고
    • The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica
    • Petri W.A., Haque R., Mann B.J. The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica. Annu. Rev. Microbiol. 2002, 56:39-64.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 39-64
    • Petri, W.A.1    Haque, R.2    Mann, B.J.3
  • 3
    • 23344432226 scopus 로고    scopus 로고
    • Resistance to intestinal Entamoeba histolytica infection is conferred by innate immunity and Gr-1+ cells
    • Asgharpour A., Gilchrist C., Baba D., et al. Resistance to intestinal Entamoeba histolytica infection is conferred by innate immunity and Gr-1+ cells. Infect. Immun. 2005, 73:4522-4529.
    • (2005) Infect. Immun. , vol.73 , pp. 4522-4529
    • Asgharpour, A.1    Gilchrist, C.2    Baba, D.3
  • 7
    • 82155175676 scopus 로고    scopus 로고
    • Composition and functional role of the mucus layers in the intestine
    • Johansson M.E., Ambort D., Pelaseyed T., et al. Composition and functional role of the mucus layers in the intestine. Cell. Mol. Life Sci. 2011, 68:3635-3641.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 3635-3641
    • Johansson, M.E.1    Ambort, D.2    Pelaseyed, T.3
  • 8
    • 7044270542 scopus 로고    scopus 로고
    • From mucins to mucus: toward a more coherent understanding of this essential barrier
    • Thornton D.J., Sheehan J.K. From mucins to mucus: toward a more coherent understanding of this essential barrier. Proc. Am. Thorac. Soc. 2004, 1:54-61.
    • (2004) Proc. Am. Thorac. Soc. , vol.1 , pp. 54-61
    • Thornton, D.J.1    Sheehan, J.K.2
  • 9
    • 77952788856 scopus 로고    scopus 로고
    • Membrane-tethered mucins have multiple functions on the ocular surface
    • Govindarajan B., Gipson I.K. Membrane-tethered mucins have multiple functions on the ocular surface. Exp. Eye Res. 2010, 90:655-663.
    • (2010) Exp. Eye Res. , vol.90 , pp. 655-663
    • Govindarajan, B.1    Gipson, I.K.2
  • 10
    • 84863220988 scopus 로고    scopus 로고
    • Infection, inflammation and host carbohydrates: a Glyco-evasion hypothesis
    • Kreisman L.S.C., Cobb B.A. Infection, inflammation and host carbohydrates: a Glyco-evasion hypothesis. Glycobiology 2012, 22:1019-1030.
    • (2012) Glycobiology , vol.22 , pp. 1019-1030
    • Kreisman, L.S.C.1    Cobb, B.A.2
  • 11
    • 34247576327 scopus 로고    scopus 로고
    • Refined methodology to purify mucins from pig colonic mucosa
    • Libao-Mercado A.J., de Lange C.F.M. Refined methodology to purify mucins from pig colonic mucosa. Livest. Sci. 2007, 109:141-144.
    • (2007) Livest. Sci. , vol.109 , pp. 141-144
    • Libao-Mercado, A.J.1    de Lange, C.F.M.2
  • 12
    • 2642648665 scopus 로고    scopus 로고
    • Functional heterogeneity of colonic adenocarcinoma mucins for inhibition of Entamoeba histolytica adherence to target cells
    • Göttke M.U., Keller K., Belley A., et al. Functional heterogeneity of colonic adenocarcinoma mucins for inhibition of Entamoeba histolytica adherence to target cells. J. Eukaryot. Microbiol. 1998, 45:17S-23S.
    • (1998) J. Eukaryot. Microbiol. , vol.45
    • Göttke, M.U.1    Keller, K.2    Belley, A.3
  • 13
    • 78650370233 scopus 로고    scopus 로고
    • Glycoblotting-assisted O-glycomics: ammonium carbamate allows for highly efficient O-glycan release from glycoproteins
    • Miura Y., Kato K., Takegawa Y., et al. Glycoblotting-assisted O-glycomics: ammonium carbamate allows for highly efficient O-glycan release from glycoproteins. Anal. Chem. 2010, 82:10021-10029.
    • (2010) Anal. Chem. , vol.82 , pp. 10021-10029
    • Miura, Y.1    Kato, K.2    Takegawa, Y.3
  • 14
    • 82355184490 scopus 로고    scopus 로고
    • Qualitative and quantitative cellular glycomics of glycosphingolipids based on rhodococcal endoglycosylceramidase-assisted glycan cleavage, glycoblotting-assisted sample preparation, and matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometry analysis
    • Fujitani N., Takegawa Y., Ishibashi Y., et al. Qualitative and quantitative cellular glycomics of glycosphingolipids based on rhodococcal endoglycosylceramidase-assisted glycan cleavage, glycoblotting-assisted sample preparation, and matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometry analysis. J. Biol. Chem. 2011, 286:41669-41679.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41669-41679
    • Fujitani, N.1    Takegawa, Y.2    Ishibashi, Y.3
  • 15
    • 83655164793 scopus 로고    scopus 로고
    • Simultaneous analysis of heparan sulfate, chondroitin/dermatan sulfates, and hyaluronan disaccharides by glycoblotting-assisted sample preparation followed by single-step zwitter-ionic-hydrophilic interaction chromatography
    • Takegawa Y., Araki K., Fujitani N., et al. Simultaneous analysis of heparan sulfate, chondroitin/dermatan sulfates, and hyaluronan disaccharides by glycoblotting-assisted sample preparation followed by single-step zwitter-ionic-hydrophilic interaction chromatography. Anal. Chem. 2011, 83:9443-9449.
    • (2011) Anal. Chem. , vol.83 , pp. 9443-9449
    • Takegawa, Y.1    Araki, K.2    Fujitani, N.3
  • 16
    • 0028953265 scopus 로고
    • High affinity binding of the Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides
    • Adler P., Wood S.J., Lee Y.C., et al. High affinity binding of the Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides. J. Biol. Chem. 1995, 270:5164-5171.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5164-5171
    • Adler, P.1    Wood, S.J.2    Lee, Y.C.3
  • 18
    • 82555187448 scopus 로고    scopus 로고
    • A versatile method for analysis of serine/threonine posttranslational modifications by β-elimination in the presence of pyrazolone analogues
    • Furukawa J., Fujitani N., Araki K., et al. A versatile method for analysis of serine/threonine posttranslational modifications by β-elimination in the presence of pyrazolone analogues. Anal. Chem. 2011, 83:9060-9067.
    • (2011) Anal. Chem. , vol.83 , pp. 9060-9067
    • Furukawa, J.1    Fujitani, N.2    Araki, K.3
  • 19
    • 66149127716 scopus 로고    scopus 로고
    • Supported molecular matrix electrophoresis: a new tool for characterization of glycoproteins
    • Matsuno Y.K., Saito T., Gotoh M., et al. Supported molecular matrix electrophoresis: a new tool for characterization of glycoproteins. Anal. Chem. 2009, 81:3816-3823.
    • (2009) Anal. Chem. , vol.81 , pp. 3816-3823
    • Matsuno, Y.K.1    Saito, T.2    Gotoh, M.3
  • 20
    • 0038157153 scopus 로고    scopus 로고
    • Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family
    • Young W.W., Holcomb D.R., Ten Hagen K.G., et al. Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family. Glycobiology 2003, 13:549-557.
    • (2003) Glycobiology , vol.13 , pp. 549-557
    • Young, W.W.1    Holcomb, D.R.2    Ten Hagen, K.G.3
  • 21
    • 45749155148 scopus 로고    scopus 로고
    • Characterization of mouse sialyltransferase genes: their evolution and diversity
    • Takashima S. Characterization of mouse sialyltransferase genes: their evolution and diversity. Biosci. Biotechnol. Biochem. 2008, 72:1155-1167.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1155-1167
    • Takashima, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.