메뉴 건너뛰기




Volumn 19, Issue 2, 2012, Pages 92-101

Identification of human preformed antibody targets in GTKO pigs

Author keywords

galactosyltransferase knockout pigs; Xenoantigens; Xenograft rejection; Xenotransplantation

Indexed keywords

ALPHA ENOLASE; DRUG; GALACTOSYLTRANSFERASE; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; MEMBRANE ANTIGEN; MEMBRANE PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UVOMORULIN;

EID: 84859854200     PISSN: 0908665X     EISSN: 13993089     Source Type: Journal    
DOI: 10.1111/j.1399-3089.2012.00695.x     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 0030716263 scopus 로고    scopus 로고
    • The role of natural anti-Gal alpha 1-3Gal antibodies in hyperacute rejection of pig-to-baboon cardiac xenotransplants
    • LIN SS, KOOYMAN DL, DANIELS LJ et al. The role of natural anti-Gal alpha 1-3Gal antibodies in hyperacute rejection of pig-to-baboon cardiac xenotransplants. Transpl Immunol 1997; 5: 212-218.
    • (1997) Transpl Immunol , vol.5 , pp. 212-218
    • Lin, S.S.1    Kooyman, D.L.2    Daniels, L.J.3
  • 2
    • 0029068597 scopus 로고
    • The generation of transgenic pigs as potential organ donors for humans
    • COZZI E, WHITE DJ. The generation of transgenic pigs as potential organ donors for humans. Nat Med 1995; 1: 964-966.
    • (1995) Nat Med , vol.1 , pp. 964-966
    • Cozzi, E.1    White, D.J.2
  • 3
    • 0037039771 scopus 로고    scopus 로고
    • Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning
    • LAI L, KOLBER-SIMONDS D, PARK KW 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.W.3
  • 4
    • 67349166987 scopus 로고    scopus 로고
    • Xenotransplantation of solid organs in the pig-to-primate model
    • EKSER B, RIGOTTI P, GRIDELLI B, COOPER DK. Xenotransplantation of solid organs in the pig-to-primate model. Transpl Immunol 2009; 21: 87-92.
    • (2009) Transpl Immunol , vol.21 , pp. 87-92
    • Ekser, B.1    Rigotti, P.2    Gridelli, B.3    Cooper, D.K.4
  • 5
    • 20244380021 scopus 로고    scopus 로고
    • Warfarin or low-molecular-weight heparin therapy does not prolong pig-to-primate cardiac xenograft function
    • BYRNE GW, SCHIRMER JM, FASS DN et al. Warfarin or low-molecular-weight heparin therapy does not prolong pig-to-primate cardiac xenograft function. Am J Transplant 2005; 5: 1011-1020.
    • (2005) Am J Transplant , vol.5 , pp. 1011-1020
    • Byrne, G.W.1    Schirmer, J.M.2    Fass, D.N.3
  • 7
    • 78349272828 scopus 로고    scopus 로고
    • The fate of human platelets perfused through the pig liver: Implications for xenotransplantation
    • BURLAK C, PARIS LL, CHIHARA RK et al. The fate of human platelets perfused through the pig liver: implications for xenotransplantation. Xenotransplantation 2010; 17: 350-361.
    • (2010) Xenotransplantation , vol.17 , pp. 350-361
    • Burlak, C.1    Paris, L.L.2    Chihara, R.K.3
  • 8
    • 34347373294 scopus 로고    scopus 로고
    • Swine generated by somatic cell nuclear transfer have increased incidence of intrauterine growth restriction (IUGR)
    • ESTRADA J, SOMMER J, COLLINS B et al. Swine generated by somatic cell nuclear transfer have increased incidence of intrauterine growth restriction (IUGR). Cloning Stem Cells 2007; 9: 229-236.
    • (2007) Cloning Stem Cells , vol.9 , pp. 229-236
    • Estrada, J.1    Sommer, J.2    Collins, B.3
  • 9
    • 81155148262 scopus 로고    scopus 로고
    • Gene Targeting and Cloning in Pigs Using Fetal Liver Derived Cells
    • WAGHMARE S, ESTRADA J, REYES L et al. Gene Targeting and Cloning in Pigs Using Fetal Liver Derived Cells. J Surg Res 2011; 171: e223-e229.
    • (2011) J Surg Res , vol.171
    • Waghmare, S.1    Estrada, J.2    Reyes, L.3
  • 10
    • 80051877742 scopus 로고    scopus 로고
    • ASGR1 expressed by porcine enriched liver sinusoidal endothelial cells mediates human platelet phagocytosis in vitro
    • PARIS LL, CHIHARA RK, REYES LM et al. ASGR1 expressed by porcine enriched liver sinusoidal endothelial cells mediates human platelet phagocytosis in vitro. Xenotransplantation 2011; 18: 245-251.
    • (2011) Xenotransplantation , vol.18 , pp. 245-251
    • Paris, L.L.1    Chihara, R.K.2    Reyes, L.M.3
  • 11
    • 0033529848 scopus 로고    scopus 로고
    • Mitotic recombination produces the majority of recessive fibroblast variants in heterozygous mice
    • SHAO C, DENG L, HENEGARIU O et al. Mitotic recombination produces the majority of recessive fibroblast variants in heterozygous mice. Proc Natl Acad Sci USA 1999; 96: 9230-9235.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9230-9235
    • Shao, C.1    Deng, L.2    Henegariu, O.3
  • 12
    • 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
  • 13
    • 0029944369 scopus 로고    scopus 로고
    • Characterization of porcine platelet glycoproteins recognized by human natural "anti-gal" antibodies
    • THIBAUDEAU K, BORCHE L, SOULILLOU JP, BLANCHARD D. Characterization of porcine platelet glycoproteins recognized by human natural "anti-gal" antibodies. Blood 1996; 87: 4636-4642.
    • (1996) Blood , vol.87 , pp. 4636-4642
    • Thibaudeau, K.1    Borche, L.2    Soulillou, J.P.3    Blanchard, D.4
  • 14
    • 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
  • 15
    • 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
  • 16
    • 49649085309 scopus 로고    scopus 로고
    • The anti-non-gal xenoantibody response to xenoantigens on gal knockout pig cells is encoded by a restricted number of germline progenitors
    • KIERNAN K, HARNDEN I, GUNTHART M, GREGORY C, MEISNER J, KEARNS-JONKER M. The anti-non-gal xenoantibody response to xenoantigens on gal knockout pig cells is encoded by a restricted number of germline progenitors. Am J Transplant 2008; 8: 1829-1839.
    • (2008) Am J Transplant , vol.8 , pp. 1829-1839
    • Kiernan, K.1    Harnden, I.2    Gunthart, M.3    Gregory, C.4    Meisner, J.5    Kearns-Jonker, M.6
  • 17
    • 34547643527 scopus 로고    scopus 로고
    • Characterization of natural human antinon- gal antibodies and their effect on activation of porcine gal-deficient endothelial cells
    • SAETHRE M, BAUMANN BC, FUNG M, SEEBACH JD, MOLLNES TE. Characterization of natural human antinon- gal antibodies and their effect on activation of porcine gal-deficient endothelial cells. Transplantation 2007; 84: 244-250.
    • (2007) Transplantation , vol.84 , pp. 244-250
    • Saethre, M.1    Baumann, B.C.2    Fung, M.3    Seebach, J.D.4    Mollnes, T.E.5
  • 18
    • 0027367160 scopus 로고
    • One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody
    • GALILI U, ANARAKI F, THALL A, HILL-BLACK C, RADIC M. One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody. Blood 1993; 82: 2485-2493.
    • (1993) Blood , vol.82 , pp. 2485-2493
    • Galili, U.1    Anaraki, F.2    Thall, A.3    Hill-Black, C.4    Radic, M.5
  • 19
    • 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
  • 20
    • 0030852709 scopus 로고    scopus 로고
    • Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(alpha1,3)Galactose epitope
    • MCMORROW IM, COMRACK CA, SACHS DH, DERSIMONIAN H. Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(alpha1,3)Galactose epitope. Transplantation 1997; 64: 501-510.
    • (1997) Transplantation , vol.64 , pp. 501-510
    • Mcmorrow, I.M.1    Comrack, C.A.2    Sachs, D.H.3    Dersimonian, H.4
  • 21
    • 50949088377 scopus 로고    scopus 로고
    • Proteomic identification of non-Gal antibody targets after pig-toprimate cardiac xenotransplantation
    • BYRNE GW, STALBOERGER PG, DAVILA E et al. Proteomic identification of non-Gal antibody targets after pig-toprimate 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
  • 22
    • 0028294159 scopus 로고
    • Porcine platelet antigens recognized by human xenoreactive natural antibodies
    • PLATT JL, HOLZKNECHT ZE. Porcine platelet antigens recognized by human xenoreactive natural antibodies. Transplantation 1994; 57: 327-335.
    • (1994) Transplantation , vol.57 , pp. 327-335
    • Platt, J.L.1    Holzknecht, Z.E.2
  • 24
    • 0033680465 scopus 로고    scopus 로고
    • Antibodies to streptococcal surface enolase react with human alpha-enolase: Implications in poststreptococcal sequelae
    • FONTAN PA, PANCHOLI V, NOCIARI MM, FISCHETTI VA. Antibodies to streptococcal surface enolase react with human alpha-enolase: implications in poststreptococcal sequelae. J Infect Dis 2000; 182: 1712-1721.
    • (2000) J Infect Dis , vol.182 , pp. 1712-1721
    • Fontan, P.A.1    Pancholi, V.2    Nociari, M.M.3    Fischetti, V.A.4
  • 25
    • 0026738431 scopus 로고
    • Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme
    • SUNDSTROM P, ALIAGA GR. Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme. J Bacteriol 1992; 174: 6789-6799.
    • (1992) J Bacteriol , vol.174 , pp. 6789-6799
    • Sundstrom, P.1    Aliaga, G.R.2
  • 27
    • 79952830765 scopus 로고    scopus 로고
    • Alpha-Enolase: A promising therapeutic and diagnostic tumor target
    • CAPELLO M, FERRI-BORGOGNO S, CAPPELLO P, NOVELLI F. alpha-Enolase: a promising therapeutic and diagnostic tumor target. FEBS J 2011; 278: 1064-1074.
    • (2011) FEBS J , vol.278 , pp. 1064-1074
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 28
    • 79951526292 scopus 로고    scopus 로고
    • Circulating autoantibodies to phosphorylated alpha-enolase are a hallmark of pancreatic cancer
    • TOMAINO B, CAPPELLO P, CAPELLO M et al. Circulating autoantibodies to phosphorylated alpha-enolase are a hallmark of pancreatic cancer. J Proteome Res 2011; 10: 105-112.
    • (2011) J Proteome Res , vol.10 , pp. 105-112
    • Tomaino, B.1    Cappello, P.2    Capello, M.3
  • 29
    • 78651341982 scopus 로고    scopus 로고
    • Seroreactivity against glycolytic enzymes in inflammatory bowel disease
    • VERMEULEN N, VERMEIRE S, ARIJS I et al. Seroreactivity against glycolytic enzymes in inflammatory bowel disease. Inflamm Bowel Dis 2011; 17: 557-564.
    • (2011) Inflamm Bowel Dis , vol.17 , pp. 557-564
    • Vermeulen, N.1    Vermeire, S.2    Arijs, I.3
  • 30
    • 84855175325 scopus 로고    scopus 로고
    • Alpha 1,3-galactosyltransferase deficiency in pigs increases sialyltransferase activities that potentially raise non-gal xenoantigenicity
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.