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Volumn 20, Issue 6, 2013, Pages 407-417

Detection of Hanganutziu-Deicher antigens in O-glycans from pig heart tissues by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Author keywords

Hanganutziu Deicher antigen; heart; matrix assisted laser desorption ionization time of flight mass spectrometry; O glycans; xenotransplantation

Indexed keywords

ANTIGEN; GLYCAN DERIVATIVE; HANGANUTZIU DEICHER ANTIGEN; UNCLASSIFIED DRUG;

EID: 84889588014     PISSN: 0908665X     EISSN: 13993089     Source Type: Journal    
DOI: 10.1111/xen.12045     Document Type: Article
Times cited : (18)

References (24)
  • 2
    • 2442538314 scopus 로고    scopus 로고
    • Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation?
    • DOI 10.1111/j.1399-3089.2004.00126.x
    • Miwa Y, Kobayashi T, Nagasaka T, et al. Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation? Xenotransplantation 2004; 11: 247-253. (Pubitemid 38623061)
    • (2004) Xenotransplantation , vol.11 , Issue.3 , pp. 247-253
    • Miwa, Y.1    Kobayashi, T.2    Nagasaka, T.3    Liu, D.4    Yu, M.5    Yokoyama, I.6    Suzukiz, A.7    Nakao, A.8
  • 4
    • 0029033071 scopus 로고
    • Human complement regulatory proteins protect swine-to-primate cardiac xenografts from humoral injury
    • et al.
    • McCurry KR, Kooyman DL, Alvarado CG, et al. Human complement regulatory proteins protect swine-to-primate cardiac xenografts from humoral injury. Nat Med 1995; 1: 423-427.
    • (1995) Nat Med , vol.1 , pp. 423-427
    • McCurry, K.R.1    Kooyman, D.L.2    Alvarado, C.G.3
  • 5
    • 84855175325 scopus 로고    scopus 로고
    • Alpha 1,3-galactosyltransferase deficiency in pigs increases sialyltransferase activities that potentially raise non-gal xenoantigenicity
    • et al.
    • Park JY, Park MR, Kwon DN, et al. Alpha 1,3-galactosyltransferase deficiency in pigs increases sialyltransferase activities that potentially raise non-gal xenoantigenicity. J Biomed Biotechnol 2011; 2011: 560850.
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 560850
    • Park, J.Y.1    Park, M.R.2    Kwon, D.N.3
  • 6
    • 84866037252 scopus 로고    scopus 로고
    • Elimination of alpha-gal xenoreactive epitope: Alpha-galactosidase treatment of porcine heart valves
    • et al.
    • Choi SY, Jeong HJ, Lim HG, et al. Elimination of alpha-gal xenoreactive epitope: alpha-galactosidase treatment of porcine heart valves. J Heart Valve Dis 2012; 21: 387-397.
    • (2012) J Heart Valve Dis , vol.21 , pp. 387-397
    • Choi, S.Y.1    Jeong, H.J.2    Lim, H.G.3
  • 7
    • 78650370233 scopus 로고    scopus 로고
    • Glycoblotting-assisted O-glycomics: Ammonium carbamate allows for highly efficient O-glycan release from glycoproteins
    • et al.
    • 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
  • 8
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • DOI 10.1016/j.bbapap.2006.10.007, PII S1570963906003487, Posttranslational Modifications in Proteomics
    • Geyer H, Geyer R,. Strategies for analysis of glycoprotein glycosylation. Biochim Biophys Acta 2006; 1764: 1853-1869. (Pubitemid 44895032)
    • (2006) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1764 , Issue.12 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 9
    • 84862870851 scopus 로고    scopus 로고
    • Mass spectrometric O-glycan analysis after combined O-glycan release by beta-elimination and 1-phenyl-3-methyl-5-pyrazolone labeling
    • Zauner G, Koeleman CA, Deelder AM, Wuhrer M,. Mass spectrometric O-glycan analysis after combined O-glycan release by beta-elimination and 1-phenyl-3-methyl-5-pyrazolone labeling. Biochim Biophys Acta 2012; 1820: 1420-1428.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1420-1428
    • Zauner, G.1    Koeleman, C.A.2    Deelder, A.M.3    Wuhrer, M.4
  • 10
    • 79952111630 scopus 로고    scopus 로고
    • Hyphenated technique for releasing and MALDI MS analysis of O-glycans in mucin-type glycoprotein samples
    • et al.
    • Yamada K, Hyodo S, Kinoshita M, et al. Hyphenated technique for releasing and MALDI MS analysis of O-glycans in mucin-type glycoprotein samples. Anal Chem 2010; 82: 7436-7443.
    • (2010) Anal Chem , vol.82 , pp. 7436-7443
    • Yamada, K.1    Hyodo, S.2    Kinoshita, M.3
  • 11
    • 84862833409 scopus 로고    scopus 로고
    • One-pot nonreductive O-glycan release and labeling with 1-phenyl-3-methyl-5-pyrazolone followed by ESI-MS analysis
    • et al.
    • Wang C, Fan W, Zhang P, et al. One-pot nonreductive O-glycan release and labeling with 1-phenyl-3-methyl-5-pyrazolone followed by ESI-MS analysis. Proteomics 2011; 11: 4229-4242.
    • (2011) Proteomics , vol.11 , pp. 4229-4242
    • Wang, C.1    Fan, W.2    Zhang, P.3
  • 13
    • 10644254423 scopus 로고    scopus 로고
    • Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract
    • DOI 10.1042/BJ20040605
    • Robbe C, Capon C, Coddeville B, Michalski JC,. Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract. Biochem J 2004; 384: 307-316. (Pubitemid 39656243)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 307-316
    • Robbe, C.1    Capon, C.2    Coddeville, B.3    Michalski, J.-C.4
  • 14
    • 69249155637 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification
    • Dias WB, Cheung WD, Wang Z, Hart GW,. Regulation of calcium/calmodulin- dependent kinase IV by O-GlcNAc modification. J Biol Chem 2009; 284: 21327-21337.
    • (2009) J Biol Chem , vol.284 , pp. 21327-21337
    • Dias, W.B.1    Cheung, W.D.2    Wang, Z.3    Hart, G.W.4
  • 15
    • 84860893138 scopus 로고    scopus 로고
    • Msb2 shedding protects Candida albicans against antimicrobial peptides
    • et al.
    • Szafranski-Schneider E, Swidergall M, Cottier F, et al. Msb2 shedding protects Candida albicans against antimicrobial peptides. PLoS Pathog 2012; 8: e1002501.
    • (2012) PLoS Pathog , vol.8
    • Szafranski-Schneider, E.1    Swidergall, M.2    Cottier, F.3
  • 16
    • 0347064294 scopus 로고    scopus 로고
    • Elimination of Oxidative Degradation during the per-O-Methylation of Carbohydrates
    • DOI 10.1021/ja035660t
    • Ciucanu I, Costello CE,. Elimination of oxidative degradation during the per-O-methylation of carbohydrates. J Am Chem Soc 2003; 125: 16213-16219. (Pubitemid 38020645)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.52 , pp. 16213-16219
    • Ciucanu, I.1    Costello, C.E.2
  • 17
    • 84857297460 scopus 로고    scopus 로고
    • Suppression of peeling during the release of O-glycans by hydrazinolysis
    • et al.
    • Kozak RP, Royle L, Gardner RA, et al. Suppression of peeling during the release of O-glycans by hydrazinolysis. Anal Biochem 2012; 423: 119-128.
    • (2012) Anal Biochem , vol.423 , pp. 119-128
    • Kozak, R.P.1    Royle, L.2    Gardner, R.A.3
  • 18
    • 73249128479 scopus 로고    scopus 로고
    • Enzymatic/chemical release of O-glycans allowing MS analysis at high sensitivity
    • Goetz JA, Novotny MV, Mechref Y,. Enzymatic/chemical release of O-glycans allowing MS analysis at high sensitivity. Anal Chem 2009; 81: 9546-9552.
    • (2009) Anal Chem , vol.81 , pp. 9546-9552
    • Goetz, J.A.1    Novotny, M.V.2    Mechref, Y.3
  • 19
    • 0037297818 scopus 로고    scopus 로고
    • Microscale analysis of mucin-type O-glycans by a coordinated fluorophore-assisted carbohydrate electrophoresis and mass spectrometry approach
    • DOI 10.1002/elps.200390071
    • Robbe C, Capon C, Flahaut C, Michalski JC,. Microscale analysis of mucin-type O-glycans by a coordinated fluorophore-assisted carbohydrate electrophoresis and mass spectrometry approach. Electrophoresis 2003; 24: 611-621. (Pubitemid 36336382)
    • (2003) Electrophoresis , vol.24 , Issue.4 , pp. 611-621
    • Robbe, C.1    Capon, C.2    Flahaut, C.3    Michalski, J.-C.4
  • 20
    • 78449307982 scopus 로고    scopus 로고
    • Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis
    • et al.
    • Yu G, Zhang Y, Zhang Z, et al. Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis. Anal Chem 2010; 82: 9534-9542.
    • (2010) Anal Chem , vol.82 , pp. 9534-9542
    • Yu, G.1    Zhang, Y.2    Zhang, Z.3
  • 21
    • 33744467070 scopus 로고    scopus 로고
    • Mass spectrometric profiling of O-linked glycans released directly from glycoproteins in gels using in-gel reductive β-elimination
    • DOI 10.1002/pmic.200500331
    • Taylor AM, Holst O, Thomas-Oates J,. Mass spectrometric profiling of O-linked glycans released directly from glycoproteins in gels using in-gel reductive beta-elimination. Proteomics 2006; 6: 2936-2946. (Pubitemid 43806392)
    • (2006) Proteomics , vol.6 , Issue.10 , pp. 2936-2946
    • Taylor, A.M.1    Holst, O.2    Thomas-Oates, J.3
  • 22
    • 0035894307 scopus 로고    scopus 로고
    • Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis
    • DOI 10.1021/ac015534c
    • Huang Y, Mechref Y, Novotny MV,. Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis. Anal Chem 2001; 73: 6063-6069. (Pubitemid 34042226)
    • (2001) Analytical Chemistry , vol.73 , Issue.24 , pp. 6063-6069
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 23
    • 0036894272 scopus 로고    scopus 로고
    • Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis
    • DOI 10.1021/ac025890a
    • Schulz BL, Packer NH, Karlsson NG,. Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis. Anal Chem 2002; 74: 6088-6097. (Pubitemid 35428807)
    • (2002) Analytical Chemistry , vol.74 , Issue.23 , pp. 6088-6097
    • Schulz, B.L.1    Packer, N.H.2    Karlsson, N.G.3
  • 24
    • 0037096068 scopus 로고    scopus 로고
    • Analysis of O-linked reducing oligosaccharides released by an in-line flow system
    • DOI 10.1006/abio.2002.5657
    • Karlsson NG, Packer NH,. Analysis of O-linked reducing oligosaccharides released by an in-line flow system. Anal Biochem 2002; 305: 173-185. (Pubitemid 34666790)
    • (2002) Analytical Biochemistry , vol.305 , Issue.2 , pp. 173-185
    • Karlsson, N.G.1    Packer, N.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.