메뉴 건너뛰기




Volumn 11, Issue 2, 2003, Pages 147-153

Co-effect of HLA-G1 and glycosyltransferases in reducing NK cell-mediated pig endothelial cell lysis

Author keywords

Glycosyltransferase; HLA G; Natural killer cell; Pig endothelial cell; Remodeling of glycoantigen

Indexed keywords

ALPHA GALACTOSE EPITOPE; BETA 2 MICROGLOBULIN; GALACTOSE ALPHA 1,3 GALACTOSE BETA 1,4 N ACETYLGLUCOSAMINE; GLYCOSYLTRANSFERASE; HLA ANTIGEN; HLA G1 ANTIGEN; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 0038376184     PISSN: 09663274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-3274(02)00151-X     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 0031570476 scopus 로고    scopus 로고
    • Natural killer cell- and macrophage-mediated rejection of concordant xenografts in the absence of T and B cell responses
    • Lin Y, Vandeputte M, Waer M. Natural killer cell- and macrophage-mediated rejection of concordant xenografts in the absence of T and B cell responses. J Immunol 1997;158:5658-5667.
    • (1997) J Immunol , vol.158 , pp. 5658-5667
    • Lin, Y.1    Vandeputte, M.2    Waer, M.3
  • 2
    • 0031906108 scopus 로고    scopus 로고
    • Induction of specific transplantation tolerance across xenogenic barriers in the T-independent immune compartment
    • Lin Y, Goebels J, Xia G, Ji P, Vandeputte M, Waer M. Induction of specific transplantation tolerance across xenogenic barriers in the T-independent immune compartment. Nature Med 1998;4:173-180.
    • (1998) Nature Med , vol.4 , pp. 173-180
    • Lin, Y.1    Goebels, J.2    Xia, G.3    Ji, P.4    Vandeputte, M.5    Waer, M.6
  • 3
    • 0034777554 scopus 로고    scopus 로고
    • The possible use of HLA-G1 and G3 in the inhibition of NK cell mediated swine endothelial cell lysis
    • Matsunami K, Miyagawa S, Nakai R, Murase A, Shirakura R. The possible use of HLA-G1 and G3 in the inhibition of NK cell mediated swine endothelial cell lysis. Clin Exp Immunol 2001;126:165-172.
    • (2001) Clin Exp Immunol , vol.126 , pp. 165-172
    • Matsunami, K.1    Miyagawa, S.2    Nakai, R.3    Murase, A.4    Shirakura, R.5
  • 4
    • 0037182112 scopus 로고    scopus 로고
    • Modulation of the leader peptide sequence of the HLA-E gene upregulates its expression and downregulates NK cell-mediated swine endothelial cell lysis
    • Matsunami K, Miyagawa S, Koyota-Nakai R, Yamada M, Shirakura R. Modulation of the leader peptide sequence of the HLA-E gene upregulates its expression and downregulates NK cell-mediated swine endothelial cell lysis. Transplantation 2002;73:1582-1589.
    • (2002) Transplantation , vol.73 , pp. 1582-1589
    • Matsunami, K.1    Miyagawa, S.2    Koyota-Nakai, R.3    Yamada, M.4    Shirakura, R.5
  • 5
    • 0033556548 scopus 로고    scopus 로고
    • HLA-G expression protects porcine endothelial cells against natural killer cell-mediated xenogenic cytotoxicity
    • Sasaki H, Xu X, Smith DM, Howard T, Mohanakumar T. HLA-G expression protects porcine endothelial cells against natural killer cell-mediated xenogenic cytotoxicity. Transplantation 1999;67:31-37.
    • (1999) Transplantation , vol.67 , pp. 31-37
    • Sasaki, H.1    Xu, X.2    Smith, D.M.3    Howard, T.4    Mohanakumar, T.5
  • 8
    • 0030612605 scopus 로고    scopus 로고
    • The alpha1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors?
    • Rouas FN, Marchal RE, Kirszenbaum M, Dausset J, Carosella ED. The alpha1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: Is HLA-G the public ligand for natural killer cell inhibitory receptors? Proc Natl Acad Sci USA 1997;94:5249-5254.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5249-5254
    • Rouas, F.N.1    Marchal, R.E.2    Kirszenbaum, M.3    Dausset, J.4    Carosella, E.D.5
  • 10
    • 0030990751 scopus 로고    scopus 로고
    • Human natural killer lymphocytes directly recognize evolutionarily conserved oligosaccharide ligands expressed by xenogenic tissues
    • Inverardi L, Clissi B, Stolzer AL, Bender JR, Sandrin MS, Pardi R. Human natural killer lymphocytes directly recognize evolutionarily conserved oligosaccharide ligands expressed by xenogenic tissues. Transplantation 1997;63:1318-1330.
    • (1997) Transplantation , vol.63 , pp. 1318-1330
    • Inverardi, L.1    Clissi, B.2    Stolzer, A.L.3    Bender, J.R.4    Sandrin, M.S.5    Pardi, R.6
  • 11
    • 0028037079 scopus 로고
    • Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity
    • Bezouska K, Yuen C, O'Brien J, et al. Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity. Nature 1994;372:150-157.
    • (1994) Nature , vol.372 , pp. 150-157
    • Bezouska, K.1    Yuen, C.2    O'Brien, J.3
  • 12
    • 0028239798 scopus 로고
    • Rat natural killer cell antigen, NKR-P1, related to C-type animal lectins is a carbohydrate-binding protein
    • Bezouska K, Vlahas G, Horvath O, et al. Rat natural killer cell antigen, NKR-P1, related to C-type animal lectins is a carbohydrate-binding protein. J Biol Chem 1994;269:16945-16952.
    • (1994) J Biol Chem , vol.269 , pp. 16945-16952
    • Bezouska, K.1    Vlahas, G.2    Horvath, O.3
  • 13
    • 0027392862 scopus 로고
    • Role of target cell glycoproteins in sensitivity to natural killer cell lysis
    • Ahrens PB. Role of target cell glycoproteins in sensitivity to natural killer cell lysis. J Biol Chem 1993;268:385-391.
    • (1993) J Biol Chem , vol.268 , pp. 385-391
    • Ahrens, P.B.1
  • 14
    • 0033388438 scopus 로고    scopus 로고
    • Regulation of natural killer cell-mediated swine endothelial cell lysis by the genetic remodeling of a glycoantigen
    • Miyagawa S, Nakai R, Yamada M, et al. Regulation of natural killer cell-mediated swine endothelial cell lysis by the genetic remodeling of a glycoantigen. J Biochem 1999;126:1067-1073.
    • (1999) J Biochem , vol.126 , pp. 1067-1073
    • Miyagawa, S.1    Nakai, R.2    Yamada, M.3
  • 15
    • 0033574673 scopus 로고    scopus 로고
    • Target cell susceptibility to lysis by human natural killer cells is augmented by α(1,3)-galactosyltransferase and reduced by α(1,2)-fucosyltransferase
    • Artrip JH, Kwiatkowski P, Michler RE, et al. Target cell susceptibility to lysis by human natural killer cells is augmented by α(1,3)-galactosyltransferase and reduced by α(1,2)-fucosyltransferase. J Biol Chem 1999;274:10717-10722.
    • (1999) J Biol Chem , vol.274 , pp. 10717-10722
    • Artrip, J.H.1    Kwiatkowski, P.2    Michler, R.E.3
  • 16
    • 0033966610 scopus 로고    scopus 로고
    • HLA-G inhibits the transendothelial migration of human NK cells
    • Dorling A, Monk NJ, Lechler RI. HLA-G inhibits the transendothelial migration of human NK cells. Eur J Immunol 2000;30:586-593.
    • (2000) Eur J Immunol , vol.30 , pp. 586-593
    • Dorling, A.1    Monk, N.J.2    Lechler, R.I.3
  • 17
    • 0028117561 scopus 로고
    • Effects of transfected complement regulatory proteins, MCP, DAF, MCP/DAF hybrid, on complement-mediated swine endothelial cell lysis
    • Miyagawa S, Shirakura R, Iwata K, et al. Effects of transfected complement regulatory proteins, MCP, DAF, MCP/DAF hybrid, on complement-mediated swine endothelial cell lysis. Transplantation 1994;58:834-840.
    • (1994) Transplantation , vol.58 , pp. 834-840
    • Miyagawa, S.1    Shirakura, R.2    Iwata, K.3
  • 18
    • 0021949046 scopus 로고
    • TCGF (IL-2)-receptor inducing factor(s). I. Regulation of IL-2 receptor on natural killer-like cell line (YT cells)
    • Yodoi J, Teshigawara K, Nikaido T, et al. TCGF (IL-2)-receptor inducing factor(s). I. Regulation of IL-2 receptor on natural killer-like cell line (YT cells). J Immunol 1985;134:1623-1630.
    • (1985) J Immunol , vol.134 , pp. 1623-1630
    • Yodoi, J.1    Teshigawara, K.2    Nikaido, T.3
  • 19
    • 0027289374 scopus 로고
    • cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III)
    • Ihara Y, Nishikawa A, Tohma T, Soejima H, Niikawa N, Taniguchi N. cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J Biochem 1993;113:692-698.
    • (1993) J Biochem , vol.113 , pp. 692-698
    • Ihara, Y.1    Nishikawa, A.2    Tohma, T.3    Soejima, H.4    Niikawa, N.5    Taniguchi, N.6
  • 20
    • 0033852762 scopus 로고    scopus 로고
    • Reduction of the major xenoantigen on glycosphingolipids of swine endothelial cells by various glycosyltransferases
    • Koma M, Miyagawa S, Honke K, et al. Reduction of the major xenoantigen on glycosphingolipids of swine endothelial cells by various glycosyltransferases. Glycobiology 2000;10:745-751.
    • (2000) Glycobiology , vol.10 , pp. 745-751
    • Koma, M.1    Miyagawa, S.2    Honke, K.3
  • 21
    • 0028811673 scopus 로고
    • Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis
    • Sandrin MS, Fodor WL, Mouhtouris E, et al. Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis. Nat Med 1995;1:1261-1267.
    • (1995) Nat Med , vol.1 , pp. 1261-1267
    • Sandrin, M.S.1    Fodor, W.L.2    Mouhtouris, E.3
  • 22
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukariotic vector
    • Niwa H, Yamamura K, Miyazaki J. Efficient selection for high-expression transfectants with a novel eukariotic vector. Gene 1991;108:193-200.
    • (1991) Gene , vol.108 , pp. 193-200
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 23
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase S, Ibuki T, Ikenaka T. Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J Biochem 1984;95:197-203.
    • (1984) J Biochem , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 24
    • 0025477749 scopus 로고
    • Improved method for fluorescence labeling of sugar chains with sialic acid residues
    • Kondo A, Suzuki J, Kuraya N, Hase S, Kato I, Ikenaka T. Improved method for fluorescence labeling of sugar chains with sialic acid residues. Agric Biol Chem 1990;54:2169-2170.
    • (1990) Agric Biol Chem , vol.54 , pp. 2169-2170
    • Kondo, A.1    Suzuki, J.2    Kuraya, N.3    Hase, S.4    Kato, I.5    Ikenaka, T.6
  • 25
    • 0031577182 scopus 로고    scopus 로고
    • Significant downregulation of the major swine xenoantigen by N-acetylglucosaminyltransferase III gene transfection
    • Tanemura M, Miyagawa S, Ihara Y, Matsuda H, Shirakura R, Taniguchi N. Significant downregulation of the major swine xenoantigen by N-acetylglucosaminyltransferase III gene transfection. Biochem Biophys Res Commun 1997;235:359-364.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 359-364
    • Tanemura, M.1    Miyagawa, S.2    Ihara, Y.3    Matsuda, H.4    Shirakura, R.5    Taniguchi, N.6
  • 26
    • 0034851054 scopus 로고    scopus 로고
    • The α-gal epitope (the Galα1-3 Galβ1-4 GlcNAc-R) in xenotransplantation
    • Galili U. The α-gal epitope (the Galα1-3 Galβ1-4 GlcNAc-R) in xenotransplantation. Biochimie 2001;83:557-563.
    • (2001) Biochimie , vol.83 , pp. 557-563
    • Galili, U.1
  • 27
    • 0002719184 scopus 로고    scopus 로고
    • Introduction of α(1,2)-fucosyltransferase and its effect on α-Gal epitopes in transgenic pig
    • Koike C, Kannnagi R, Takuma Y, et al. Introduction of α(1,2)-fucosyltransferase and its effect on α-Gal epitopes in transgenic pig. Xonotransplant 1996;3:81-86.
    • (1996) Xonotransplant , vol.3 , pp. 81-86
    • Koike, C.1    Kannnagi, R.2    Takuma, Y.3
  • 28
    • 0033208674 scopus 로고    scopus 로고
    • Expression of the human α1,2-fucosyltransferase in transgenic pigs modifies the cell surface carbohydrase phenotype and confers resistance to human serum-mediated cytolysis
    • Costa C, Zhao L, Burton WV, et al. Expression of the human α1,2-fucosyltransferase in transgenic pigs modifies the cell surface carbohydrase phenotype and confers resistance to human serum-mediated cytolysis. FASB J 1999;13:1762-1773.
    • (1999) FASB J , vol.13 , pp. 1762-1773
    • Costa, C.1    Zhao, L.2    Burton, W.V.3
  • 29
    • 0035914389 scopus 로고    scopus 로고
    • Remodeling of the major pig xenoantigen by N-acetylglucosaminyltransferase III in transgenic pig
    • Miyagawa S, Murakam H, Takahagi Y, et al. Remodeling of the major pig xenoantigen by N-acetylglucosaminyltransferase III in transgenic pig. J Biol Chem 2001;276:39310-39319.
    • (2001) J Biol Chem , vol.276 , pp. 39310-39319
    • Miyagawa, S.1    Murakam, H.2    Takahagi, Y.3
  • 30
    • 0032170361 scopus 로고    scopus 로고
    • The monoclonal antibody HCA2 recognises a broadly shared epitope on selected classical as well as several non-classical HLA-class I molecules
    • Seitz C, Uchanska-Ziegler B, Zank A, Ziegler A. The monoclonal antibody HCA2 recognises a broadly shared epitope on selected classical as well as several non-classical HLA-class I molecules. Mol Immunol 1998;35:819-827.
    • (1998) Mol Immunol , vol.35 , pp. 819-827
    • Seitz, C.1    Uchanska-Ziegler, B.2    Zank, A.3    Ziegler, A.4
  • 31
    • 9244233286 scopus 로고    scopus 로고
    • Unusual uniformity of the N-linked oligosaccharides of HLA-A, B, and C glycoproteins
    • Barber LD, Patel TP, Percival L, et al. Unusual uniformity of the N-linked oligosaccharides of HLA-A, B, and C glycoproteins. J Immunol 1996;156:3275-3284.
    • (1996) J Immunol , vol.156 , pp. 3275-3284
    • Barber, L.D.1    Patel, T.P.2    Percival, L.3
  • 32
    • 0026575821 scopus 로고
    • Alternative splicing of HLA-G transcripts yields proteins with primary structures resembling both class I and class II antigens
    • Ishitani A, Geraghty DE. Alternative splicing of HLA-G transcripts yields proteins with primary structures resembling both class I and class II antigens. Proc Natl Acad Sci USA 1992;89:3947-3951.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3947-3951
    • Ishitani, A.1    Geraghty, D.E.2
  • 33
    • 0029956556 scopus 로고    scopus 로고
    • Remodeling of cell surface glycoproteins by N-acetylglucosaminyltransferase III gene transfection: Modulation of metastatic potentials and down regulation of hepatitis B virus replication
    • Taniguchi N, Yoshimura M, Miyoshi E, Ihara Y, Nishikawa A, Fujii S. Remodeling of cell surface glycoproteins by N-acetylglucosaminyltransferase III gene transfection: Modulation of metastatic potentials and down regulation of hepatitis B virus replication. Glycobiology 1996;6:691-694.
    • (1996) Glycobiology , vol.6 , pp. 691-694
    • Taniguchi, N.1    Yoshimura, M.2    Miyoshi, E.3    Ihara, Y.4    Nishikawa, A.5    Fujii, S.6
  • 34


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.