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Volumn 17, Issue 6, 2010, Pages 440-448

Deficiency of N-glycolylneuraminic acid and Galα1-3Galβ1-4GlcNAc epitopes in xenogeneic cells attenuates cytotoxicity of human natural antibodies

Author keywords

complement dependent cytotoxicity; natural antibody; xenoantibody xenoantigen; xenotransplantation

Indexed keywords

ALPHA 1,3 GALACTOSYLTRANSFERASE; CARBOHYDRATE ANTIGEN; CHROMIUM 51; CYTIDINE MONOPHOSPHO N ACETYLNEURAMINIC ACID HYDROXYLASE; EPITOPE; GALACTOSYLGALACTOSE; GALACTOSYLGALACTOSE BETA 1; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; N GLYCOLOYLNEURAMINIC ACID; OXYGENASE; UNCLASSIFIED DRUG;

EID: 78650670892     PISSN: 0908665X     EISSN: 13993089     Source Type: Journal    
DOI: 10.1111/j.1399-3089.2010.00610.x     Document Type: Article
Times cited : (39)

References (33)
  • 1
    • 0028171348 scopus 로고
    • Gal alpha (1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies
    • Sandrin MS, McKenzie IF,. Gal alpha (1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies. Immunol Rev 1994; 141: 169-190.
    • (1994) Immunol Rev , vol.141 , pp. 169-190
    • Sandrin, M.S.1    McKenzie, I.F.2
  • 2
    • 0024297335 scopus 로고
    • Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells
    • Galili U, Shohet SB, Kobrin E, et al. Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells. J Biol Chem 1988; 263: 17755-17762.
    • (1988) J Biol Chem , vol.263 , pp. 17755-17762
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3
  • 3
    • 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
  • 4
    • 0037039771 scopus 로고    scopus 로고
    • Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning
    • Lai L, Kolber-Simonds D, Park K, et al. Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning. Science 2002; 295: 1089-1092.
    • (2002) Science , vol.295 , pp. 1089-1092
    • Lai, L.1    Kolber-Simonds, D.2    Park, K.3
  • 5
    • 13444282227 scopus 로고    scopus 로고
    • Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: Initial experience
    • Kuwaki K, Tseng Y, Dor FJMF, 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.2    Dor, F.3
  • 6
    • 13444269248 scopus 로고    scopus 로고
    • Marked prolongation of porcine renal xenograft survival in baboons through the use of alpha1,3-galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue
    • Yamada K, Yazawa K, Shimizu A, et al. Marked prolongation of porcine renal xenograft survival in baboons through the use of alpha1,3- galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue. Nat Med 2005; 11: 32-34.
    • (2005) Nat Med , vol.11 , pp. 32-34
    • Yamada, K.1    Yazawa, K.2    Shimizu, A.3
  • 8
    • 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
  • 9
    • 0017665490 scopus 로고
    • Antigen of "serum sickness" type of heterophile antibodies in human sera: Identification as gangliosides with N-glycolylneuraminic acid
    • Higashi H, Naiki M, Matuo S, et al. Antigen of "serum sickness" type of heterophile antibodies in human sera: identification as gangliosides with N-glycolylneuraminic acid. Biochem Biophys Res Commun 1977; 79: 388-395.
    • (1977) Biochem Biophys Res Commun , vol.79 , pp. 388-395
    • Higashi, H.1    Naiki, M.2    Matuo, S.3
  • 10
    • 0018152253 scopus 로고
    • Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid
    • Merrick JM, Zadarlik K, Milgrom F,. Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid. Int Arch Allergy Appl Immunol 1978; 57: 477-480.
    • (1978) Int Arch Allergy Appl Immunol , vol.57 , pp. 477-480
    • Merrick, J.M.1    Zadarlik, K.2    Milgrom, F.3
  • 11
    • 0032546785 scopus 로고    scopus 로고
    • The molecular basis for the absence of N-glycolylneuraminic acid in humans
    • Irie A, Koyama S, Kozutsumi Y, et al. The molecular basis for the absence of N-glycolylneuraminic acid in humans. J Biol Chem 1998; 273: 15866-15871.
    • (1998) J Biol Chem , vol.273 , pp. 15866-15871
    • Irie, A.1    Koyama, S.2    Kozutsumi, Y.3
  • 12
    • 0036872920 scopus 로고    scopus 로고
    • Anti-N-glycolylneuraminic acid antibodies identified in healthy human serum
    • Zhu A, Hurst R,. Anti-N-glycolylneuraminic acid antibodies identified in healthy human serum. Xenotransplantation 2002; 9: 376-381.
    • (2002) Xenotransplantation , vol.9 , pp. 376-381
    • Zhu, A.1    Hurst, R.2
  • 13
    • 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
  • 14
    • 0001918159 scopus 로고    scopus 로고
    • Loss of N-glycolylneuraminic acid in humans: Mechanisms, consequences, and implications for hominid evolution
    • Varki A,. Loss of N-glycolylneuraminic acid in humans: mechanisms, consequences, and implications for hominid evolution. Am J Phys Anthropol 2001; 33: 54-69.
    • (2001) Am J Phys Anthropol , vol.33 , pp. 54-69
    • Varki, A.1
  • 15
    • 77951889356 scopus 로고    scopus 로고
    • Immunological property of antibodies against N-glycolylneuraminic acid epitopes in cytidine monophospho-N-acetylneuraminic acid hydroxylase-deficient mice
    • Tahara H, Ide K, Basnet NB, et al. Immunological property of antibodies against N-glycolylneuraminic acid epitopes in cytidine monophospho-N- acetylneuraminic acid hydroxylase-deficient mice. J Immunol 2010; 184: 3269-3275.
    • (2010) J Immunol , vol.184 , pp. 3269-3275
    • Tahara, H.1    Ide, K.2    Basnet, N.B.3
  • 16
    • 34250187766 scopus 로고    scopus 로고
    • N-glycolylneuraminic acid deficiency in mice: Implications for human biology and evolution
    • Hedlund M, Tangvoranuntakul P, Takematsu H, et al. N-glycolylneuraminic acid deficiency in mice: implications for human biology and evolution. Mol Cell Biol 2007; 27: 4340-4346.
    • (2007) Mol Cell Biol , vol.27 , pp. 4340-4346
    • Hedlund, M.1    Tangvoranuntakul, P.2    Takematsu, H.3
  • 17
    • 0028982258 scopus 로고
    • Oocyte Gal alpha 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall AD, Malý P, Lowe JB,. Oocyte Gal alpha 1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J Biol Chem 1995; 270: 21437-21440.
    • (1995) J Biol Chem , vol.270 , pp. 21437-21440
    • Thall, A.D.1    Malý, P.2    Lowe, J.B.3
  • 18
    • 0028414765 scopus 로고
    • Detection of N-glycolylneuraminic acid-containing glycoproteins from various animal erythrocytes by chicken monoclonal antibody against Hanganutziu-Deicher antigens
    • Asaoka H, Matsuda H,. Detection of N-glycolylneuraminic acid-containing glycoproteins from various animal erythrocytes by chicken monoclonal antibody against Hanganutziu-Deicher antigens. J Vet Med Sci 1994; 56: 375-377.
    • (1994) J Vet Med Sci , vol.56 , pp. 375-377
    • Asaoka, H.1    Matsuda, H.2
  • 19
    • 0027944492 scopus 로고
    • Characterization and affinity isolation of xenoreactive human natural antibodies
    • Parker W, Bruno D, Holzknecht Z, et al. Characterization and affinity isolation of xenoreactive human natural antibodies. J Immunol 1994; 153: 3791-3803. (Pubitemid 24313885)
    • (1994) Journal of Immunology , vol.153 , Issue.8 , pp. 3791-3803
    • Parker, W.1    Bruno, D.2    Holzknecht, Z.E.3    Platt, J.L.4
  • 20
    • 0027517325 scopus 로고
    • Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes
    • Sandrin MS, Vaughan HA, Dabkowski PL, et al. Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes. Proc Natl Acad Sci USA 1993; 90: 11391-11395.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11391-11395
    • Sandrin, M.S.1    Vaughan, H.A.2    Dabkowski, P.L.3
  • 21
    • 53049100695 scopus 로고    scopus 로고
    • Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease
    • Padler-Karavani V, Yu H, Cao H, et al. Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 2008; 18: 818-830.
    • (2008) Glycobiology , vol.18 , pp. 818-830
    • Padler-Karavani, V.1    Yu, H.2    Cao, H.3
  • 22
    • 2442538314 scopus 로고    scopus 로고
    • Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation?
    • 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.
    • (2004) Xenotransplantation , vol.11 , pp. 247-253
    • Miwa, Y.1    Kobayashi, T.2    Nagasaka, T.3
  • 23
    • 33748467172 scopus 로고    scopus 로고
    • Xenotransplantation and ABO incompatible transplantation: The similarities they share
    • Galili U,. Xenotransplantation and ABO incompatible transplantation: the similarities they share. Transfus Apher Sci 2006; 35: 45-58.
    • (2006) Transfus Apher Sci , vol.35 , pp. 45-58
    • Galili, U.1
  • 24
    • 0030852712 scopus 로고    scopus 로고
    • Relationship between ABO blood group and levels of Gal alpha,3Galactose-reactive human immunoglobulin G
    • McMorrow IM, Comrack CA, Nazarey PP, et al. Relationship between ABO blood group and levels of Gal alpha,3Galactose-reactive human immunoglobulin G. Transplantation 1997; 64: 546-549.
    • (1997) Transplantation , vol.64 , pp. 546-549
    • McMorrow, I.M.1    Comrack, C.A.2    Nazarey, P.P.3
  • 25
    • 0035147607 scopus 로고    scopus 로고
    • Both IgG and IgM anti-pig antibodies induce complement activation and cytotoxicity
    • Roos A, Essers M, Van Gijlswijk-Janssen D, et al. Both IgG and IgM anti-pig antibodies induce complement activation and cytotoxicity. Xenotransplantation 2001; 8: 3-14.
    • (2001) Xenotransplantation , vol.8 , pp. 3-14
    • Roos, A.1    Essers, M.2    Van Gijlswijk-Janssen, D.3
  • 26
    • 0028254250 scopus 로고
    • Cytolytic effect of human anti-Gal IgM and complement on porcine endothelial cells: A kinetic analysis
    • Borche L, Thibaudeau K, Navenot J, et al. Cytolytic effect of human anti-Gal IgM and complement on porcine endothelial cells: a kinetic analysis. Xenotransplantation 1994; 1: 125-131.
    • (1994) Xenotransplantation , vol.1 , pp. 125-131
    • Borche, L.1    Thibaudeau, K.2    Navenot, J.3
  • 27
    • 0034936968 scopus 로고    scopus 로고
    • Role of natural and immune IgM antibodies in immune responses
    • Boes M,. Role of natural and immune IgM antibodies in immune responses. Mol Immunol 2000; 37: 1141-1149.
    • (2000) Mol Immunol , vol.37 , pp. 1141-1149
    • Boes, M.1
  • 28
    • 0026654128 scopus 로고
    • Mechanism of complement activation in the hyperacute rejection of porcine organs transplanted into primate recipients
    • Dalmasso A, Vercellotti G, Fischel R, et al. Mechanism of complement activation in the hyperacute rejection of porcine organs transplanted into primate recipients. Am J Pathol 1992; 140: 1157-1166.
    • (1992) Am J Pathol , vol.140 , pp. 1157-1166
    • Dalmasso, A.1    Vercellotti, G.2    Fischel, R.3
  • 29
    • 0034650236 scopus 로고    scopus 로고
    • Differential expression of alpha-GAL epitopes (Galalpha1-3Galbeta1- 4GlcNAc-R) on pig and mouse organs
    • Tanemura M, Maruyama S, Galili U,. Differential expression of alpha-GAL epitopes (Galalpha1-3Galbeta1-4GlcNAc-R) on pig and mouse organs. Transplantation 2000; 69: 187-190.
    • (2000) Transplantation , vol.69 , pp. 187-190
    • Tanemura, M.1    Maruyama, S.2    Galili, U.3
  • 30
    • 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
  • 31
    • 2442568013 scopus 로고    scopus 로고
    • A study of the xenoantigenicity of adult pig islets cells
    • Komoda H, Miyagawa S, Kubo T, et al. A study of the xenoantigenicity of adult pig islets cells. Xenotransplantation 2004; 11: 237-246.
    • (2004) Xenotransplantation , vol.11 , pp. 237-246
    • Komoda, H.1    Miyagawa, S.2    Kubo, T.3
  • 32
    • 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 Y, Harvey DJ, Yang Y, 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.1    Harvey, D.J.2    Yang, Y.3
  • 33
    • 0028351036 scopus 로고
    • Antibody-dependent cell-mediated cytotoxicity against porcine endothelium induced by a majority of human sera
    • Schaapherder AF, Daha MR, Te Bulte MT, et al. Antibody-dependent cell-mediated cytotoxicity against porcine endothelium induced by a majority of human sera. Transplantation 1994; 57: 1376-1382.
    • (1994) Transplantation , vol.57 , pp. 1376-1382
    • Schaapherder, A.F.1    Daha, M.R.2    Te Bulte, M.T.3


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