메뉴 건너뛰기




Volumn 20, Issue 4, 2013, Pages 199-208

The sweets standing at the borderline between allo- and xenotransplantation

Author keywords

glycan database; mass spectrometry; non Gal antigen; pig glycome; xenotransplantation

Indexed keywords

CARBOHYDRATE ANTIGEN; GALACTOSYLTRANSFERASE; GLYCAN; GLYCOSPHINGOLIPID;

EID: 84881169732     PISSN: 0908665X     EISSN: 13993089     Source Type: Journal    
DOI: 10.1111/xen.12030     Document Type: Review
Times cited : (10)

References (81)
  • 1
    • 0019304768 scopus 로고
    • The first human blood transfusion
    • Farr AD,. The first human blood transfusion. Med Hist 1980; 24: 143-162.
    • (1980) Med Hist , vol.24 , pp. 143-162
    • Farr, A.D.1
  • 2
    • 33749091429 scopus 로고
    • Some aspects of the biochemistry of the human blood-group substances
    • Morgan WT, Watkins WM,. Some aspects of the biochemistry of the human blood-group substances. Br Med Bull 1959; 15: 109-113.
    • (1959) Br Med Bull , vol.15 , pp. 109-113
    • Morgan, W.T.1    Watkins, W.M.2
  • 3
    • 0031025604 scopus 로고    scopus 로고
    • Clinical xenotransplantation: Past, present and future
    • Taniguchi S, Cooper DK,. Clinical xenotransplantation: past, present and future. Ann R Coll Surg Engl 1997; 79: 13-19.
    • (1997) Ann R Coll Surg Engl , vol.79 , pp. 13-19
    • Taniguchi, S.1    Cooper, D.K.2
  • 4
    • 0033931039 scopus 로고    scopus 로고
    • Cardiac xenotransplantation: Clinical experience and future direction
    • Adams DH, Chen RH, Kadner A,. Cardiac xenotransplantation: clinical experience and future direction. Ann Thorac Surg 2000; 70: 320-326.
    • (2000) Ann Thorac Surg , vol.70 , pp. 320-326
    • Adams, D.H.1    Chen, R.H.2    Kadner, A.3
  • 5
    • 0033055352 scopus 로고    scopus 로고
    • Xenotransplantation: A potential solution to the critical organ donor shortage
    • Sim KH, Marinov A, Levy GA,. Xenotransplantation: a potential solution to the critical organ donor shortage. Can J Gastroenterol 1999; 13: 311-318.
    • (1999) Can J Gastroenterol , vol.13 , pp. 311-318
    • Sim, K.H.1    Marinov, A.2    Levy, G.A.3
  • 6
    • 0028618657 scopus 로고
    • Xenotransplantation and its future
    • Hammer C,. Xenotransplantation and its future. Forensic Sci Int 1994; 69: 259-268.
    • (1994) Forensic Sci Int , vol.69 , pp. 259-268
    • Hammer, C.1
  • 7
    • 0025076225 scopus 로고
    • Another look at cardiac xenotransplantation
    • Bailey LL,. Another look at cardiac xenotransplantation. J Card Surg 1990; 5: 210-218.
    • (1990) J Card Surg , vol.5 , pp. 210-218
    • Bailey, L.L.1
  • 8
    • 28644446730 scopus 로고    scopus 로고
    • Acute rejection is associated with antibodies to non-Gal antigens in baboons using Gal-knockout pig kidneys
    • Chen G, Qian H, Starzl T, et al. Acute rejection is associated with antibodies to non-Gal antigens in baboons using Gal-knockout pig kidneys. Nat Med 2005; 11: 1295-1298.
    • (2005) Nat Med , vol.11 , pp. 1295-1298
    • Chen, G.1    Qian, H.2    Starzl, T.3
  • 9
    • 13444282227 scopus 로고    scopus 로고
    • Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: Initial experience
    • Kuwaki K, Tseng YL, Dor FJ, et al. Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: initial experience. Nat Med 2005; 11: 29-31.
    • (2005) Nat Med , vol.11 , pp. 29-31
    • Kuwaki, K.1    Tseng, Y.L.2    Dor, F.J.3
  • 10
    • 2442567900 scopus 로고    scopus 로고
    • Production of alpha-1,3-galactosyltransferase null pigs by means of nuclear transfer with fibroblasts bearing loss of heterozygosity mutations
    • Kolber-Simonds D, Lai L, Watt SR, et al. Production of alpha-1,3-galactosyltransferase null pigs by means of nuclear transfer with fibroblasts bearing loss of heterozygosity mutations. Proc Natl Acad Sci U S A 2004; 101: 7335-7340.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7335-7340
    • Kolber-Simonds, D.1    Lai, L.2    Watt, S.R.3
  • 11
    • 0347367029 scopus 로고    scopus 로고
    • Production of alpha 1,3-galactosyltransferase-deficient pigs
    • Phelps CJ, Koike C, Vaught TD, et al. Production of alpha 1,3-galactosyltransferase-deficient pigs. Science 2003; 299: 411-414.
    • (2003) Science , vol.299 , pp. 411-414
    • Phelps, C.J.1    Koike, C.2    Vaught, T.D.3
  • 12
    • 0027716847 scopus 로고
    • Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation
    • Oriol R, Ye Y, Koren E, Cooper DK,. Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation. Transplantation 1993; 56: 1433-1442.
    • (1993) Transplantation , vol.56 , pp. 1433-1442
    • Oriol, R.1    Ye, Y.2    Koren, E.3    Cooper, D.K.4
  • 13
    • 0026623093 scopus 로고
    • Identification of carbohydrate structures that bind human antiporcine antibodies: Implications for discordant xenografting in humans
    • Good AH, Cooper DK, Malcolm AJ, et al. Identification of carbohydrate structures that bind human antiporcine antibodies: implications for discordant xenografting in humans. Transplant Proc 1992; 24: 559-562.
    • (1992) Transplant Proc , vol.24 , pp. 559-562
    • Good, A.H.1    Cooper, D.K.2    Malcolm, A.J.3
  • 14
    • 0028171342 scopus 로고
    • Oligosaccharides and discordant xenotransplantation
    • Cooper DK, Koren E, Oriol R,. Oligosaccharides and discordant xenotransplantation. Immunol Rev 1994; 141: 31-58.
    • (1994) Immunol Rev , vol.141 , pp. 31-58
    • Cooper, D.K.1    Koren, E.2    Oriol, R.3
  • 15
    • 0004106191 scopus 로고    scopus 로고
    • 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, xxix.
    • Varki A,. Essentials of Glycobiology, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 2009, xxix, 784.
    • (2009) Essentials of Glycobiology , pp. 784
    • Varki, A.1
  • 17
    • 0035937526 scopus 로고    scopus 로고
    • Glycosylation and the immune system
    • Rudd PM, Elliott T, Cresswell P, et al. Glycosylation and the immune system. Science 2001; 291: 2370-2376.
    • (2001) Science , vol.291 , pp. 2370-2376
    • Rudd, P.M.1    Elliott, T.2    Cresswell, P.3
  • 19
    • 33845528765 scopus 로고    scopus 로고
    • ABO blood group and related antigens, natural antibodies and transplantation
    • Milland J, Sandrin MS,. ABO blood group and related antigens, natural antibodies and transplantation. Tissue Antigens 2006; 68: 459-466.
    • (2006) Tissue Antigens , vol.68 , pp. 459-466
    • Milland, J.1    Sandrin, M.S.2
  • 20
    • 0035090644 scopus 로고    scopus 로고
    • Histo-blood group A antigen expression in pig kidneys-implication for ABO incompatible pig-to-human xenotransplantation
    • Rydberg L, Molne J, Strokan V, et al. Histo-blood group A antigen expression in pig kidneys-implication for ABO incompatible pig-to-human xenotransplantation. Scand J Urol Nephrol 2001; 35: 54-62.
    • (2001) Scand J Urol Nephrol , vol.35 , pp. 54-62
    • Rydberg, L.1    Molne, J.2    Strokan, V.3
  • 21
    • 0028567482 scopus 로고
    • Cardiac allotransplantation across the ABO-blood group barrier by the neutralization of preformed antibodies: The baboon as a model for the human
    • Ye Y, Niekrasz M, Kehoe M, et al. Cardiac allotransplantation across the ABO-blood group barrier by the neutralization of preformed antibodies: the baboon as a model for the human. Lab Anim Sci 1994; 44: 121-124.
    • (1994) Lab Anim Sci , vol.44 , pp. 121-124
    • Ye, Y.1    Niekrasz, M.2    Kehoe, M.3
  • 22
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze HH,. Genetic defects in the human glycome. Nat Rev Genet 2006; 7: 537-551.
    • (2006) Nat Rev Genet , vol.7 , pp. 537-551
    • Freeze, H.H.1
  • 23
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • Fuster MM, Esko JD,. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat Rev Cancer 2005; 5: 526-542.
    • (2005) Nat Rev Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 24
    • 34548487272 scopus 로고    scopus 로고
    • Screening and diagnosis of congenital disorders of glycosylation
    • Marklova E, Albahri Z,. Screening and diagnosis of congenital disorders of glycosylation. Clin Chim Acta 2007; 385: 6-20.
    • (2007) Clin Chim Acta , vol.385 , pp. 6-20
    • Marklova, E.1    Albahri, Z.2
  • 25
    • 39549103661 scopus 로고    scopus 로고
    • Altered glycosylation of proteins in cancer: What is the potential for new anti-tumour strategies
    • Brooks SA, Carter TM, Royle L, et al. Altered glycosylation of proteins in cancer: what is the potential for new anti-tumour strategies. Anticancer Agents Med Chem 2008; 8: 2-21.
    • (2008) Anticancer Agents Med Chem , vol.8 , pp. 2-21
    • Brooks, S.A.1    Carter, T.M.2    Royle, L.3
  • 26
    • 0027348385 scopus 로고
    • Expression of alpha 2,6-sialylated sugar chains in normal and neoplastic colon tissues. Detection by digoxigenin-conjugated Sambucus nigra agglutinin
    • Dall'Olio F, Trere D,. Expression of alpha 2,6-sialylated sugar chains in normal and neoplastic colon tissues. Detection by digoxigenin-conjugated Sambucus nigra agglutinin. Eur J Histochem 1993: 37: 257-265.
    • (1993) Eur J Histochem , vol.37 , pp. 257-265
    • Dall'Olio, F.1    Trere, D.2
  • 27
    • 0024278682 scopus 로고
    • Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures
    • Passaniti A, Hart GW,. Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures. J Biol Chem 1988; 263: 7591-7603.
    • (1988) J Biol Chem , vol.263 , pp. 7591-7603
    • Passaniti, A.1    Hart, G.W.2
  • 28
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings RD,. The repertoire of glycan determinants in the human glycome. Mol BioSyst 2009; 5: 1087-1104.
    • (2009) Mol BioSyst , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 30
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra R, Wormald MR, Rudd PM, et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat Med 1995; 1: 237-243.
    • (1995) Nat Med , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3
  • 31
    • 0027458368 scopus 로고
    • Equine lutropin and chorionic gonadotropin bear oligosaccharides terminating with SO4-4-GalNAc and Sia alpha 2,3Gal, respectively
    • Smith PL, Bousfield GR, Kumar S, et al. Equine lutropin and chorionic gonadotropin bear oligosaccharides terminating with SO4-4-GalNAc and Sia alpha 2,3Gal, respectively. J Biol Chem 1993; 268: 795-802.
    • (1993) J Biol Chem , vol.268 , pp. 795-802
    • Smith, P.L.1    Bousfield, G.R.2    Kumar, S.3
  • 32
    • 0038732507 scopus 로고    scopus 로고
    • Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation i
    • Callewaert N, Schollen E, Vanhecke A, et al. Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I. Glycobiology 2003; 13: 367-375.
    • (2003) Glycobiology , vol.13 , pp. 367-375
    • Callewaert, N.1    Schollen, E.2    Vanhecke, A.3
  • 34
    • 0033048787 scopus 로고    scopus 로고
    • Clinical aspects of altered glycosylation of glycoproteins in cancer
    • Orntoft TF, Vestergaard EM,. Clinical aspects of altered glycosylation of glycoproteins in cancer. Electrophoresis 1999; 20: 362-371.
    • (1999) Electrophoresis , vol.20 , pp. 362-371
    • Orntoft, T.F.1    Vestergaard, E.M.2
  • 35
    • 58249096139 scopus 로고    scopus 로고
    • Prognostic utility of glycosyltransferase expression in breast cancer
    • Patani N, Jiang W, Mokbel K,. Prognostic utility of glycosyltransferase expression in breast cancer. Cancer Genomics Proteomics 2008; 5: 333-340.
    • (2008) Cancer Genomics Proteomics , vol.5 , pp. 333-340
    • Patani, N.1    Jiang, W.2    Mokbel, K.3
  • 36
    • 20144367969 scopus 로고    scopus 로고
    • Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells
    • Iwai T, Kudo T, Kawamoto R, et al. Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells. Proc Natl Acad Sci U S A 2005; 102: 4572-4577.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4572-4577
    • Iwai, T.1    Kudo, T.2    Kawamoto, R.3
  • 37
    • 27744597289 scopus 로고    scopus 로고
    • Prediction of glycan structures from gene expression data based on glycosyltransferase reactions
    • Kawano S, Hashimoto K, Miyama T, et al. Prediction of glycan structures from gene expression data based on glycosyltransferase reactions. Bioinformatics 2005; 21: 3976-3982.
    • (2005) Bioinformatics , vol.21 , pp. 3976-3982
    • Kawano, S.1    Hashimoto, K.2    Miyama, T.3
  • 38
    • 67650996838 scopus 로고    scopus 로고
    • Analysis of the human cancer glycome identifies a novel group of tumor-associated N-acetylglucosamine glycan antigens
    • Satomaa T, Heiskanen A, Leonardsson I, et al. Analysis of the human cancer glycome identifies a novel group of tumor-associated N-acetylglucosamine glycan antigens. Cancer Res 2009; 69: 5811-5819.
    • (2009) Cancer Res , vol.69 , pp. 5811-5819
    • Satomaa, T.1    Heiskanen, A.2    Leonardsson, I.3
  • 39
    • 77956303179 scopus 로고    scopus 로고
    • The N-glycome of human plasma
    • Stumpo KA, Reinhold VN,. The N-glycome of human plasma. J Proteome Res 2010; 9: 4823-4830.
    • (2010) J Proteome Res , vol.9 , pp. 4823-4830
    • Stumpo, K.A.1    Reinhold, V.N.2
  • 40
    • 70449338884 scopus 로고    scopus 로고
    • Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups
    • Pang PC, Tissot B, Drobnis EZ, et al. Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups. J Proteome Res 2009; 8: 4906-4915.
    • (2009) J Proteome Res , vol.8 , pp. 4906-4915
    • Pang, P.C.1    Tissot, B.2    Drobnis, E.Z.3
  • 41
    • 67649211352 scopus 로고    scopus 로고
    • The N-glycome of human embryonic stem cells
    • Satomaa T, Heiskanen A, Mikkola M, et al. The N-glycome of human embryonic stem cells. BMC Cell Biol 2009; 10: 42.
    • (2009) BMC Cell Biol , vol.10 , pp. 42
    • Satomaa, T.1    Heiskanen, A.2    Mikkola, M.3
  • 42
    • 0035170507 scopus 로고    scopus 로고
    • GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources
    • Cooper CA, Harrison MJ, Wilkins MR, Packer NH,. GlycoSuiteDB: a new curated relational database of glycoprotein glycan structures and their biological sources. Nucleic Acids Res 2001; 29: 332-335.
    • (2001) Nucleic Acids Res , vol.29 , pp. 332-335
    • Cooper, C.A.1    Harrison, M.J.2    Wilkins, M.R.3    Packer, N.H.4
  • 43
    • 0345863935 scopus 로고    scopus 로고
    • The KEGG resource for deciphering the genome
    • (Database issue).
    • Kanehisa M, Goto S, Kawashima S, et al. The KEGG resource for deciphering the genome. Nucleic Acids Res 2004: 32 (Database issue): D277-D280.
    • (2004) Nucleic Acids Res , vol.32
    • Kanehisa, M.1    Goto, S.2    Kawashima, S.3
  • 44
    • 38549146892 scopus 로고    scopus 로고
    • Glycoconjugate Data Bank: Structures-an annotated glycan structure database and N-glycan primary structure verification service
    • (Database issue).
    • Nakahara T, Hashimoto R, Nakagawa H, et al., Glycoconjugate Data Bank: Structures-an annotated glycan structure database and N-glycan primary structure verification service. Nucleic Acids Res 2008: 36 (Database issue): D368-D371.
    • (2008) Nucleic Acids Res , vol.36
    • Nakahara, T.1    Hashimoto, R.2    Nakagawa, H.3
  • 45
    • 0015539303 scopus 로고
    • Preformed natural antibodies in animals and man. Outlook on xenotransplantation
    • Hammer C, Chaussy C, Brendel W,. Preformed natural antibodies in animals and man. Outlook on xenotransplantation. Eur Surg Res 1973; 5: 162-166.
    • (1973) Eur Surg Res , vol.5 , pp. 162-166
    • Hammer, C.1    Chaussy, C.2    Brendel, W.3
  • 46
    • 0032617317 scopus 로고    scopus 로고
    • Evolution of alpha 1,3galactosyltransferase and of the alpha-Gal epitope
    • Galili U,. Evolution of alpha 1,3galactosyltransferase and of the alpha-Gal epitope. Subcell Biochem 1999; 32: 1-23.
    • (1999) Subcell Biochem , vol.32 , pp. 1-23
    • Galili, U.1
  • 47
    • 0027508081 scopus 로고
    • Interaction of the natural anti-Gal antibody with alpha-galactosyl epitopes: A major obstacle for xenotransplantation in humans
    • Galili U,. Interaction of the natural anti-Gal antibody with alpha-galactosyl epitopes: a major obstacle for xenotransplantation in humans. Immunol Today 1993; 14: 480-482.
    • (1993) Immunol Today , vol.14 , pp. 480-482
    • Galili, U.1
  • 48
    • 0022260876 scopus 로고
    • Human natural anti-alpha-galactosyl IgG. II. The specific recognition of alpha (1-3)-linked galactose residues
    • Galili U, Macher BA, Buehler J, Shohet SB,. Human natural anti-alpha-galactosyl IgG. II. The specific recognition of alpha (1-3)-linked galactose residues. J Exp Med 1985; 162: 573-582.
    • (1985) J Exp Med , vol.162 , pp. 573-582
    • Galili, U.1    MacHer, B.A.2    Buehler, J.3    Shohet, S.B.4
  • 49
    • 0027942758 scopus 로고
    • Monomorphic and polymorphic carbohydrate antigens on pig tissues: Implications for organ xenotransplantation in the pig-to-human model
    • Oriol R, Barthod F, Bergemer AM, et al. Monomorphic and polymorphic carbohydrate antigens on pig tissues: implications for organ xenotransplantation in the pig-to-human model. Transpl Int 1994; 7: 405-413.
    • (1994) Transpl Int , vol.7 , pp. 405-413
    • Oriol, R.1    Barthod, F.2    Bergemer, A.M.3
  • 50
    • 2442758069 scopus 로고    scopus 로고
    • In vivo immunoadsorption of antipig antibodies in baboons using a specific Gal(alpha)1-3Gal column
    • Taniguchi S, Neethling FA, Korchagina EY, et al. In vivo immunoadsorption of antipig antibodies in baboons using a specific Gal(alpha)1-3Gal column. Transplantation 1996; 62: 1379-1384.
    • (1996) Transplantation , vol.62 , pp. 1379-1384
    • Taniguchi, S.1    Neethling, F.A.2    Korchagina, E.Y.3
  • 51
    • 0037623766 scopus 로고    scopus 로고
    • Production of alpha 1,3-galactosyltransferase-knockout cloned pigs expressing human alpha 1,2-fucosylosyltransferase
    • Ramsoondar JJ, Machaty Z, Costa C, et al. Production of alpha 1,3-galactosyltransferase-knockout cloned pigs expressing human alpha 1,2-fucosylosyltransferase. Biol Reprod 2003; 69: 437-445.
    • (2003) Biol Reprod , vol.69 , pp. 437-445
    • Ramsoondar, J.J.1    MacHaty, Z.2    Costa, C.3
  • 53
    • 77953514286 scopus 로고    scopus 로고
    • Investigation of potential carbohydrate antigen targets for human and baboon antibodies
    • Yeh P, Ezzelarab M, Bovin N, et al. Investigation of potential carbohydrate antigen targets for human and baboon antibodies. Xenotransplantation 2010; 17: 197-206.
    • (2010) Xenotransplantation , vol.17 , pp. 197-206
    • Yeh, P.1    Ezzelarab, M.2    Bovin, N.3
  • 54
    • 50949088377 scopus 로고    scopus 로고
    • Proteomic identification of non-Gal antibody targets after pig-to-primate cardiac xenotransplantation
    • Byrne GW, Stalboerger PG, Davila E, et al. Proteomic identification of non-Gal antibody targets after pig-to-primate cardiac xenotransplantation. Xenotransplantation 2008; 15: 268-276.
    • (2008) Xenotransplantation , vol.15 , pp. 268-276
    • Byrne, G.W.1    Stalboerger, P.G.2    Davila, E.3
  • 55
    • 33644862221 scopus 로고    scopus 로고
    • The role of anti-non-Gal antibodies in the development of acute humoral xenograft rejection of hDAF transgenic porcine kidneys in baboons receiving anti-Gal antibody neutralization therapy
    • Chen G, Sun H, Yang H, et al. The role of anti-non-Gal antibodies in the development of acute humoral xenograft rejection of hDAF transgenic porcine kidneys in baboons receiving anti-Gal antibody neutralization therapy. Transplantation 2006; 81: 273-283.
    • (2006) Transplantation , vol.81 , pp. 273-283
    • Chen, G.1    Sun, H.2    Yang, H.3
  • 56
    • 7044235964 scopus 로고    scopus 로고
    • Anti-non-Gal porcine endothelial cell antibodies in acute humoral xenograft rejection of hDAF-transgenic porcine hearts in cynomolgus monkeys
    • Lam TT, Paniagua R, Shivaram G, et al. Anti-non-Gal porcine endothelial cell antibodies in acute humoral xenograft rejection of hDAF-transgenic porcine hearts in cynomolgus monkeys. Xenotransplantation 2004; 11: 531-535.
    • (2004) Xenotransplantation , vol.11 , pp. 531-535
    • Lam, T.T.1    Paniagua, R.2    Shivaram, G.3
  • 57
    • 0025371203 scopus 로고
    • Hanganutziu-Deicher antigen as a possible target for immunotherapy of melanoma
    • Nakarai H, Chandler PJ, Kano K, et al. Hanganutziu-Deicher antigen as a possible target for immunotherapy of melanoma. Int Arch Allergy Appl Immunol 1990; 91: 323-328.
    • (1990) Int Arch Allergy Appl Immunol , vol.91 , pp. 323-328
    • Nakarai, H.1    Chandler, P.J.2    Kano, K.3
  • 58
    • 0027096232 scopus 로고
    • Analysis of the expression of Hanganutziu-Deicher (HD) antigen in human malignant melanoma
    • Kawachi S, Saida T,. Analysis of the expression of Hanganutziu-Deicher (HD) antigen in human malignant melanoma. J Dermatol 1992; 19: 827-830.
    • (1992) J Dermatol , vol.19 , pp. 827-830
    • Kawachi, S.1    Saida, T.2
  • 59
    • 0028643579 scopus 로고
    • Potential use of specific human and chicken antibodies for detection of Hanganutziu-Deicher antigen(s) in sera of cancer patients
    • Mukuria CJ, Noguchi A, Suzuki E, Naiki M,. Potential use of specific human and chicken antibodies for detection of Hanganutziu-Deicher antigen(s) in sera of cancer patients. Jpn J Med Sci Biol 1994; 47: 253-264.
    • (1994) Jpn J Med Sci Biol , vol.47 , pp. 253-264
    • Mukuria, C.J.1    Noguchi, A.2    Suzuki, E.3    Naiki, M.4
  • 60
    • 0021967069 scopus 로고
    • Characterization of N-glycolylneuraminic acid-containing gangliosides as tumor-associated Hanganutziu-Deicher antigen in human colon cancer
    • Higashi H, Hirabayashi Y, Fukui Y, et al. Characterization of N-glycolylneuraminic acid-containing gangliosides as tumor-associated Hanganutziu-Deicher antigen in human colon cancer. Cancer Res 1985; 45: 3796-3802.
    • (1985) Cancer Res , vol.45 , pp. 3796-3802
    • Higashi, H.1    Hirabayashi, Y.2    Fukui, Y.3
  • 61
    • 78650670892 scopus 로고    scopus 로고
    • Deficiency of N-glycolylneuraminic acid and Galalpha1-3Galbeta1-4GlcNAc epitopes in xenogeneic cells attenuates cytotoxicity of human natural antibodies
    • Basnet NB, Ide K, Tahara H, et al. Deficiency of N-glycolylneuraminic acid and Galalpha1-3Galbeta1-4GlcNAc epitopes in xenogeneic cells attenuates cytotoxicity of human natural antibodies. Xenotransplantation 2010; 17: 440-448.
    • (2010) Xenotransplantation , vol.17 , pp. 440-448
    • Basnet, N.B.1    Ide, K.2    Tahara, H.3
  • 62
    • 79951516280 scopus 로고    scopus 로고
    • Identification of new carbohydrate and membrane protein antigens in cardiac xenotransplantation
    • Byrne GW, Stalboerger PG, Du Z, et al. Identification of new carbohydrate and membrane protein antigens in cardiac xenotransplantation. Transplantation 2011; 91: 287-292.
    • (2011) Transplantation , vol.91 , pp. 287-292
    • Byrne, G.W.1    Stalboerger, P.G.2    Du, Z.3
  • 63
    • 0742305869 scopus 로고    scopus 로고
    • Gal alpha 1,3Gal expression on porcine pancreatic islets, testis, spleen, and thymus
    • Dor FJ, Cheng J, Alt A, et al. Gal alpha 1,3Gal expression on porcine pancreatic islets, testis, spleen, and thymus. Xenotransplantation 2004; 11: 101-106.
    • (2004) Xenotransplantation , vol.11 , pp. 101-106
    • Dor, F.J.1    Cheng, J.2    Alt, A.3
  • 64
    • 0032586944 scopus 로고    scopus 로고
    • Expression of the GALalpha(1-3)GAL epitope on pig islets
    • Heald KA, Carless N, Jay TR, et al. Expression of the GALalpha(1-3)GAL epitope on pig islets. J Mol Med 1999; 77: 169-171.
    • (1999) J Mol Med , vol.77 , pp. 169-171
    • Heald, K.A.1    Carless, N.2    Jay, T.R.3
  • 65
    • 0036665048 scopus 로고    scopus 로고
    • Lectin interactions with alpha-galactosylated xenoantigens
    • Kirkeby S, Moe D,. Lectin interactions with alpha-galactosylated xenoantigens. Xenotransplantation 2002; 9: 260-267.
    • (2002) Xenotransplantation , vol.9 , pp. 260-267
    • Kirkeby, S.1    Moe, D.2
  • 66
    • 35948949131 scopus 로고    scopus 로고
    • Gal alpha(1-3)Gal expression of the cornea in vitro, in vivo and in xenotransplantation
    • Lee HI, Kim MK, Oh JY, et al. Gal alpha(1-3)Gal expression of the cornea in vitro, in vivo and in xenotransplantation. Xenotransplantation 2007; 14: 612-618.
    • (2007) Xenotransplantation , vol.14 , pp. 612-618
    • Lee, H.I.1    Kim, M.K.2    Oh, J.Y.3
  • 67
    • 0028341367 scopus 로고
    • Distribution of the major xenoantigen (gal (alpha 1-3)gal) for pig to human xenografts
    • McKenzie IF, Xing PX, Vaughan HA, et al. Distribution of the major xenoantigen (gal (alpha 1-3)gal) for pig to human xenografts. Transpl Immunol 1994; 2: 81-86.
    • (1994) Transpl Immunol , vol.2 , pp. 81-86
    • McKenzie, I.F.1    Xing, P.X.2    Vaughan, H.A.3
  • 68
    • 47249100755 scopus 로고    scopus 로고
    • Structural analysis of alpha-Gal and new non-Gal carbohydrate epitopes from specific pathogen-free miniature pig kidney
    • Kim YG, Gil GC, Harvey DJ, Kim BG,. Structural analysis of alpha-Gal and new non-Gal carbohydrate epitopes from specific pathogen-free miniature pig kidney. Proteomics 2008; 8: 2596-2610.
    • (2008) Proteomics , vol.8 , pp. 2596-2610
    • Kim, Y.G.1    Gil, G.C.2    Harvey, D.J.3    Kim, B.G.4
  • 69
    • 67650467775 scopus 로고    scopus 로고
    • Qualitative and quantitative comparison of N-glycans between pig endothelial and islet cells by high-performance liquid chromatography and mass spectrometry-based strategy
    • Kim YG, Gil GC, Jang KS, et al. Qualitative and quantitative comparison of N-glycans between pig endothelial and islet cells by high-performance liquid chromatography and mass spectrometry-based strategy. J Mass Spectrom 2009; 44: 1087-1104.
    • (2009) J Mass Spectrom , vol.44 , pp. 1087-1104
    • Kim, Y.G.1    Gil, G.C.2    Jang, K.S.3
  • 70
    • 70449509808 scopus 로고    scopus 로고
    • Identification of alpha-Gal and non-Gal epitopes in pig corneal endothelial cells and keratocytes by using mass spectrometry
    • Kim YG, Oh JY, Gil GC, et al. Identification of alpha-Gal and non-Gal epitopes in pig corneal endothelial cells and keratocytes by using mass spectrometry. Curr Eye Res 2009; 34: 877-895.
    • (2009) Curr Eye Res , vol.34 , pp. 877-895
    • Kim, Y.G.1    Oh, J.Y.2    Gil, G.C.3
  • 71
    • 65549136329 scopus 로고    scopus 로고
    • Glycomic analysis by capillary electrophoresis-mass spectrometry
    • Mechref Y, Novotny MV,. Glycomic analysis by capillary electrophoresis-mass spectrometry. Mass Spectrom Rev 2009; 28: 207-222.
    • (2009) Mass Spectrom Rev , vol.28 , pp. 207-222
    • Mechref, Y.1    Novotny, M.V.2
  • 72
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle W, Michalski JC,. Analysis of protein glycosylation by mass spectrometry. Nat Protoc 2007; 2: 1585-1602.
    • (2007) Nat Protoc , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.C.2
  • 73
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia J,. Mass spectrometry and the emerging field of glycomics. Chem Biol 2008; 15: 881-892.
    • (2008) Chem Biol , vol.15 , pp. 881-892
    • Zaia, J.1
  • 74
    • 77956045259 scopus 로고    scopus 로고
    • Mass spectrometry and glycomics
    • Zaia J,. Mass spectrometry and glycomics. OMICS 2010; 14: 401-418.
    • (2010) OMICS , vol.14 , pp. 401-418
    • Zaia, J.1
  • 75
    • 70349876393 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the glycosphingolipid-derived glycans from miniature pig endothelial cells and islets: Identification of NeuGc epitope in pig islets
    • Kim YG, Harvey DJ, Yang YH, et al. Mass spectrometric analysis of the glycosphingolipid-derived glycans from miniature pig endothelial cells and islets: identification of NeuGc epitope in pig islets. J Mass Spectrom 2009; 44: 1489-1499.
    • (2009) J Mass Spectrom , vol.44 , pp. 1489-1499
    • Kim, Y.G.1    Harvey, D.J.2    Yang, Y.H.3
  • 76
    • 33644541787 scopus 로고    scopus 로고
    • The identification and characterization of xenoantigenic nonhuman carbohydrate sequences in membrane proteins from porcine kidney
    • Kim YG, Kim SY, Hur YM, et al. The identification and characterization of xenoantigenic nonhuman carbohydrate sequences in membrane proteins from porcine kidney. Proteomics 2006; 6: 1133-1142.
    • (2006) Proteomics , vol.6 , pp. 1133-1142
    • Kim, Y.G.1    Kim, S.Y.2    Hur, Y.M.3
  • 77
    • 0034682757 scopus 로고    scopus 로고
    • Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids
    • Keusch JJ, Manzella SM, Nyame KA, et al. Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids. J Biol Chem 2000; 275: 25308-25314.
    • (2000) J Biol Chem , vol.275 , pp. 25308-25314
    • Keusch, J.J.1    Manzella, S.M.2    Nyame, K.A.3
  • 78
    • 32044445822 scopus 로고    scopus 로고
    • The molecular basis for galalpha(1,3)gal expression in animals with a deletion of the alpha1,3galactosyltransferase gene
    • Milland J, Christiansen D, Lazarus BD, et al. The molecular basis for galalpha(1,3)gal expression in animals with a deletion of the alpha1,3galactosyltransferase gene. J Immunol 2006; 176: 2448-2454.
    • (2006) J Immunol , vol.176 , pp. 2448-2454
    • Milland, J.1    Christiansen, D.2    Lazarus, B.D.3
  • 79
    • 76349109490 scopus 로고    scopus 로고
    • Structural characterization of alpha1,3-galactosyltransferase knockout pig heart and kidney glycolipids and their reactivity with human and baboon antibodies
    • Diswall M, Angstrom J, Karlsson H, et al. Structural characterization of alpha1,3-galactosyltransferase knockout pig heart and kidney glycolipids and their reactivity with human and baboon antibodies. Xenotransplantation 2010; 17: 48-60.
    • (2010) Xenotransplantation , vol.17 , pp. 48-60
    • Diswall, M.1    Angstrom, J.2    Karlsson, H.3
  • 80
    • 0033062487 scopus 로고    scopus 로고
    • Significance of histochemical expression of Hanganutziu-Deicher antigens in pig, baboon and human tissues
    • Morozumi K, Kobayashi T, Usami T, et al. Significance of histochemical expression of Hanganutziu-Deicher antigens in pig, baboon and human tissues. Transplant Proc 1999; 31: 942-944.
    • (1999) Transplant Proc , vol.31 , pp. 942-944
    • Morozumi, K.1    Kobayashi, T.2    Usami, T.3
  • 81
    • 0031048870 scopus 로고    scopus 로고
    • A novel glycosphingolipid expressed in pig kidney: Gal alpha 1-3Lewis(x) hexaglycosylceramide
    • Bouhours D, Liaigre J, Naulet J, et al. A novel glycosphingolipid expressed in pig kidney: Gal alpha 1-3Lewis(x) hexaglycosylceramide. Glycoconj J 1997; 14: 29-38.
    • (1997) Glycoconj J , vol.14 , pp. 29-38
    • Bouhours, D.1    Liaigre, J.2    Naulet, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.