메뉴 건너뛰기




Volumn 80, Issue 3, 2005, Pages 344-352

Terminal sialic acid residues on human glycophorin A are recognized by porcine Kupffer cells

Author keywords

Extracorporeal perfusion; Glycophorin A; N acetylneuraminic acid; Sialic acid; Xenogeneic

Indexed keywords

BLOOD GROUP A ANTIGEN; BLOOD GROUP B ANTIGEN; CARBOHYDRATE; EPITOPE; ERYTHROCYTE CR 51; GLYCOPHORIN A; GLYCOPROTEIN; GLYCOSIDASE; HYALURONIC ACID; LACTOSE; LIGAND; MONOSACCHARIDE; MUCIN; N ACETYLNEURAMINIC ACID; NEURAMINIC ACID; NEURAMINYL LACTOSE; O ANTIGEN; PROTEOGLYCAN; PROTEOGLYCAN N LINKED GLYCOSIDASE F; RECEPTOR; SIALIC ACID; SIALIDASE A; SIALIDASE INHIBITOR; TRISACCHARIDE; UNCLASSIFIED DRUG;

EID: 23744432758     PISSN: 00411337     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.TP.0000162974.94890.9F     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 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(19): 7335.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.19 , pp. 7335
    • Kolber-Simonds, D.1    Lai, L.2    Watt, S.R.3
  • 2
    • 3142717365 scopus 로고    scopus 로고
    • alpha1,3-Galactosyltransferase gene-knockout miniature swine produce natural cytotoxic anti-Gal antibodies
    • Dor FJ, Tseng YL, Cheng J, et al. alpha1,3-Galactosyltransferase gene-knockout miniature swine produce natural cytotoxic anti-Gal antibodies. Transplantation 2004; 78(1): 15.
    • (2004) Transplantation , vol.78 , Issue.1 , pp. 15
    • Dor, F.J.1    Tseng, Y.L.2    Cheng, J.3
  • 3
    • 12144268640 scopus 로고    scopus 로고
    • A novel role for lectins in xenotransplantation
    • Rees MA. A novel role for lectins in xenotransplantation. Xenotransplantation 2005; 12(1): 7.
    • (2005) Xenotransplantation , vol.12 , Issue.1 , pp. 7
    • Rees, M.A.1
  • 5
    • 0022801910 scopus 로고
    • High frequency antigens of human erythrocyte membrane sialoglycoproteins, III. Studies on the EnaFR, Wrb and Wra antigens
    • Dahr W, Wilkinson S, Issitt PD, et al. High frequency antigens of human erythrocyte membrane sialoglycoproteins, III. Studies on the EnaFR, Wrb and Wra antigens. Biol Chem Hoppe Seyler 1986; 367( 10): 1033.
    • (1986) Biol Chem Hoppe Seyler , vol.367 , Issue.10 , pp. 1033
    • Dahr, W.1    Wilkinson, S.2    Issitt, P.D.3
  • 6
    • 0024433989 scopus 로고
    • Epitopes on sialoglycoprotein alpha: Evidence for heterogeneity in the molecule
    • Gardner B, Parsons SF, Merry AH, et al. Epitopes on sialoglycoprotein alpha: evidence for heterogeneity in the molecule. Immunology 1989; 68(2): 283.
    • (1989) Immunology , vol.68 , Issue.2 , pp. 283
    • Gardner, B.1    Parsons, S.F.2    Merry, A.H.3
  • 7
    • 0015243455 scopus 로고
    • A major protein which spans the human erythrocyte membrane
    • Bretscher MS. A major protein which spans the human erythrocyte membrane. J Mol Biol 1971; 59(2): 351.
    • (1971) J Mol Biol , vol.59 , Issue.2 , pp. 351
    • Bretscher, M.S.1
  • 8
    • 0017104316 scopus 로고
    • Heterogeneity of human cell membrane sialoglycoproteins
    • Dahr W, Uhlenbruck G, Janssen E, et al. Heterogeneity of human cell membrane sialoglycoproteins. Blut 1976; 32(3): 171.
    • (1976) Blut , vol.32 , Issue.3 , pp. 171
    • Dahr, W.1    Uhlenbruck, G.2    Janssen, E.3
  • 9
    • 0006777243 scopus 로고
    • Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin
    • Tomita M, Marchesi VT. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A 1975; 72(8): 2964.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , Issue.8 , pp. 2964
    • Tomita, M.1    Marchesi, V.T.2
  • 10
    • 0018127764 scopus 로고
    • Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence
    • Tomita M, Furthmayr H, Marchesi VT. Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence. Biochemistry 1978; 17(22): 4756.
    • (1978) Biochemistry , vol.17 , Issue.22 , pp. 4756
    • Tomita, M.1    Furthmayr, H.2    Marchesi, V.T.3
  • 11
    • 0027374888 scopus 로고
    • Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A
    • Pisano A, Redmond JW, Williams KL, et al. Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A. Glycobiology 1993; 3(5): 429.
    • (1993) Glycobiology , vol.3 , Issue.5 , pp. 429
    • Pisano, A.1    Redmond, J.W.2    Williams, K.L.3
  • 12
    • 0014670772 scopus 로고
    • Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides
    • Thomas DB, Winzler RJ. Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides. J Biol Chem 1969; 244(21): 5943.
    • (1969) J Biol Chem , vol.244 , Issue.21 , pp. 5943
    • Thomas, D.B.1    Winzler, R.J.2
  • 13
    • 0018978140 scopus 로고
    • Comparison of alkal-labile oligosaccharide chains of M and N blood-group glycopeptides from human erythrocyte membrane
    • Lisowska E, Duk M, Dahr W. Comparison of alkal-labile oligosaccharide chains of M and N blood-group glycopeptides from human erythrocyte membrane. Carbohydr Res 1980; 79(1): 103.
    • (1980) Carbohydr Res , vol.79 , Issue.1 , pp. 103
    • Lisowska, E.1    Duk, M.2    Dahr, W.3
  • 14
    • 0023646827 scopus 로고
    • Alkali-labile oligosaccharide units of a sialoglycoprotein from rabbit erythrocyte membranes
    • Fukuda K, Honma K, Manabe H, et al. Alkali-labile oligosaccharide units of a sialoglycoprotein from rabbit erythrocyte membranes. Biochim Biophys Acta 1987; 926(2): 132.
    • (1987) Biochim Biophys Acta , vol.926 , Issue.2 , pp. 132
    • Fukuda, K.1    Honma, K.2    Manabe, H.3
  • 15
    • 0020612780 scopus 로고
    • A carbohydrate structural variant of MM glycoprotein (glycophorin A)
    • Adamany AM, Blumenfeld OO, Sabo B, et al. A carbohydrate structural variant of MM glycoprotein (glycophorin A). J Biol Chem 1983; 258(19): 11537.
    • (1983) J Biol Chem , vol.258 , Issue.19 , pp. 11537
    • Adamany, A.M.1    Blumenfeld, O.O.2    Sabo, B.3
  • 16
    • 0018169814 scopus 로고
    • The sugar chain structures of ABO blood group active glycoproteins obtained from human erythrocyte membrane
    • Takasaki S, Yamashita K, Kobata A. The sugar chain structures of ABO blood group active glycoproteins obtained from human erythrocyte membrane. J Biol Chem 1978; 253(17): 6086.
    • (1978) J Biol Chem , vol.253 , Issue.17 , pp. 6086
    • Takasaki, S.1    Yamashita, K.2    Kobata, A.3
  • 17
    • 0021112121 scopus 로고
    • Primary structure of the oligosaccharide determinant of blood group Cad specificity
    • Blanchard D, Cartron JP, Fournet B, et al. Primary structure of the oligosaccharide determinant of blood group Cad specificity. J Biol Chem 1983; 258(12): 7691.
    • (1983) J Biol Chem , vol.258 , Issue.12 , pp. 7691
    • Blanchard, D.1    Cartron, J.P.2    Fournet, B.3
  • 18
    • 0019333158 scopus 로고
    • Structures of the asparagine-linked sugar chains of glycophorin A
    • Yoshima H, Furthmayr H, Kobata A. Structures of the asparagine-linked sugar chains of glycophorin A. J Biol Chem 1980; 255(20): 9713.
    • (1980) J Biol Chem , vol.255 , Issue.20 , pp. 9713
    • Yoshima, H.1    Furthmayr, H.2    Kobata, A.3
  • 19
    • 3042540715 scopus 로고
    • Adhesion and erythrophagocytosis of human senescent erythrocytes by autologous monocytes and their inhibition by beta-galactosyl derivatives
    • Vaysse J, Gattegno L, Bladier D, et al. Adhesion and erythrophagocytosis of human senescent erythrocytes by autologous monocytes and their inhibition by beta-galactosyl derivatives. Proc Natl Acad Sci U S A 1986; 83(5): 1339.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , Issue.5 , pp. 1339
    • Vaysse, J.1    Gattegno, L.2    Bladier, D.3
  • 20
    • 0023694256 scopus 로고
    • Red cell aging results in a change of cell surface carbohydrate epitopes allowing for recognition by galactose-specific receptors of rat liver macrophages
    • Schlepper-Schafer J, Kolb-Bachofen V. Red cell aging results in a change of cell surface carbohydrate epitopes allowing for recognition by galactose-specific receptors of rat liver macrophages. Blood Cells 1988; 14(1): 259.
    • (1988) Blood Cells , vol.14 , Issue.1 , pp. 259
    • Schlepper-Schafer, J.1    Kolb-Bachofen, V.2
  • 21
    • 0023476526 scopus 로고
    • Recognition of xenogeneic erythrocytes: The GalNAc/Gal-partide receptor of rat liver macrophages mediates or participates in recognition
    • Mohr M, Kolb H, Kolb-Bachofen V, et al. Recognition of xenogeneic erythrocytes: the GalNAc/Gal-partide receptor of rat liver macrophages mediates or participates in recognition. Biol Cell 1987; 60(3): 217.
    • (1987) Biol Cell , vol.60 , Issue.3 , pp. 217
    • Mohr, M.1    Kolb, H.2    Kolb-Bachofen, V.3
  • 22
    • 0037093485 scopus 로고    scopus 로고
    • Porcine livers perfused with human blood mount a graft-versus- "host" reaction
    • Rees MA, Butler AJ, Davies HF, et al. Porcine livers perfused with human blood mount a graft-versus-"host" reaction. Transplantation 2002; 73(9): 1460.
    • (2002) Transplantation , vol.73 , Issue.9 , pp. 1460
    • Rees, M.A.1    Butler, A.J.2    Davies, H.F.3
  • 23
    • 12144280270 scopus 로고    scopus 로고
    • Evidence of macrophage receptors capable of direct recognition of xenogeneic epitopes without opsonization
    • Rees MA, Butler AJ, Brons IG, et al. Evidence of macrophage receptors capable of direct recognition of xenogeneic epitopes without opsonization. Xenotransplantation 2005; 12(1): 13.
    • (2005) Xenotransplantation , vol.12 , Issue.1 , pp. 13
    • Rees, M.A.1    Butler, A.J.2    Brons, I.G.3
  • 24
    • 0026574251 scopus 로고
    • Chromium-51 labeling of sheep red blood cells
    • Morrissey GJ, Gravelle DR, Lo J, et al. Chromium-51 labeling of sheep red blood cells. Lab Anim Sci 1992; 42(1): 70.
    • (1992) Lab Anim Sci , vol.42 , Issue.1 , pp. 70
    • Morrissey, G.J.1    Gravelle, D.R.2    Lo, J.3
  • 25
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge JT, Mitchell C, Hanahan DJ. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 1963; 100: 119.
    • (1963) Arch Biochem Biophys , vol.100 , pp. 119
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 26
    • 0015230696 scopus 로고
    • Glycoproteins: Isolation from cell membranes with lithium diiodosalicylate
    • Marchesi VT, Andrews EP. Glycoproteins: isolation from cell membranes with lithium diiodosalicylate. Science 1971; 174(15): 1247.
    • (1971) Science , vol.174 , Issue.15 , pp. 1247
    • Marchesi, V.T.1    Andrews, E.P.2
  • 27
    • 0015353592 scopus 로고
    • Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane
    • Marchesi VT, Tillack TW, Jackson RL, et al. Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane. Proc Natl Acad Sci U S A 1972; 69(6): 1445.
    • (1972) Proc Natl Acad Sci U S A , vol.69 , Issue.6 , pp. 1445
    • Marchesi, V.T.1    Tillack, T.W.2    Jackson, R.L.3
  • 28
    • 33645168678 scopus 로고
    • Effect of sialidase on blood group specificity of hog submaxillary glycoproteins
    • Aminoff D, Morrow MP. Effect of sialidase on blood group specificity of hog submaxillary glycoproteins. FEBS Lett 1970; 8(6): 353.
    • (1970) FEBS Lett , vol.8 , Issue.6 , pp. 353
    • Aminoff, D.1    Morrow, M.P.2
  • 29
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A. Sialic acids as ligands in recognition phenomena. Faseb J 1997; 11(4): 248.
    • (1997) Faseb J , vol.11 , Issue.4 , pp. 248
    • Varki, A.1
  • 30
    • 0035043468 scopus 로고    scopus 로고
    • Differences in sialic acid density in pathogenic and non-pathogenic Aspergillus species
    • Wasylnka JA, Simmer MI, Moore MM. Differences in sialic acid density in pathogenic and non-pathogenic Aspergillus species. Microbiology 2001; 147(Pt 4): 869.
    • (2001) Microbiology , vol.147 , Issue.PART 4 , pp. 869
    • Wasylnka, J.A.1    Simmer, M.I.2    Moore, M.M.3
  • 31
    • 0023276640 scopus 로고
    • The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by cross-reactivity between natural anti-Gal and anti-B antibodies
    • Galili U, Buehler J, Shohet SB, et al. The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by cross-reactivity between natural anti-Gal and anti-B antibodies. J Exp Med 1987; 165(3): 693.
    • (1987) J Exp Med , vol.165 , Issue.3 , pp. 693
    • Galili, U.1    Buehler, J.2    Shohet, S.B.3
  • 32
    • 0019325032 scopus 로고
    • Analysis of lectin-dependent recognition of desialylated erythrocytes by Kupffer cells
    • Schlepper-Schafer J, Kolb-Bachofen V, Kolb H. Analysis of lectin-dependent recognition of desialylated erythrocytes by Kupffer cells. Biochem J 1980; 186(3): 827.
    • (1980) Biochem J , vol.186 , Issue.3 , pp. 827
    • Schlepper-Schafer, J.1    Kolb-Bachofen, V.2    Kolb, H.3
  • 33
    • 0031461225 scopus 로고    scopus 로고
    • Comparison between intact and desialylated human serum amyloid P component by laser photo CI-DNP (chemically induced dynamic nuclear polarization) technique: An indication for a conformational impact of sialic acid
    • Siebert HC, Andre S, Reuter G, et al. Comparison between intact and desialylated human serum amyloid P component by laser photo CI-DNP (chemically induced dynamic nuclear polarization) technique: an indication for a conformational impact of sialic acid. Glycoconj J 1997; 14(8): 945.
    • (1997) Glycoconj J , vol.14 , Issue.8 , pp. 945
    • Siebert, H.C.1    Andre, S.2    Reuter, G.3
  • 34
    • 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; Suppl 33:54.
    • (2001) Am J Phys Anthropol , Issue.SUPPL. 33 , pp. 54
    • Varki, A.1
  • 35
    • 0034844959 scopus 로고    scopus 로고
    • N-Glycolylneuraminic acid in human tumours
    • Malykh YN, Schauer R, Shaw L. N-Glycolylneuraminic acid in human tumours. Biochimie 2001; 83(7): 623.
    • (2001) Biochimie , vol.83 , Issue.7 , pp. 623
    • Malykh, Y.N.1    Schauer, R.2    Shaw, L.3
  • 36
    • 84882765158 scopus 로고
    • Isolation and characterization of gangliosides from pig lymphocytes
    • Hueso P, Reglero A, Rodrigo M, et al. Isolation and characterization of gangliosides from pig lymphocytes. Biol Chem Hoppe Seyler 1985; 366(2): 167.
    • (1985) Biol Chem Hoppe Seyler , vol.366 , Issue.2 , pp. 167
    • Hueso, P.1    Reglero, A.2    Rodrigo, M.3
  • 37
    • 0032579245 scopus 로고    scopus 로고
    • Identification of oligo-N-glycolyl-neuraminic acid residues in mammal-derived glycoproteins by a newly developed immunochemical reagent and biochemical methods
    • Sato C, Kitajima K, Inoue S, et al. Identification of oligo-N-glycolyl-neuraminic acid residues in mammal-derived glycoproteins by a newly developed immunochemical reagent and biochemical methods. J Biol Chem 1998; 273(5): 2575.
    • (1998) J Biol Chem , vol.273 , Issue.5 , pp. 2575
    • Sato, C.1    Kitajima, K.2    Inoue, S.3
  • 38
    • 0037338532 scopus 로고    scopus 로고
    • Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine
    • Malykh YN, King TP, Logan E, et al. Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine. Biochem J 2003; 370(Pt 2): 601.
    • (2003) Biochem J , vol.370 , Issue.PART 2 , pp. 601
    • Malykh, Y.N.1    King, T.P.2    Logan, E.3
  • 39
    • 2442651473 scopus 로고    scopus 로고
    • Classical pathway complement destruction is not responsible for the loss of human erythrocytes during porcine liver perfusion
    • Rees MA, Butler AJ, Negus MC, et al. Classical pathway complement destruction is not responsible for the loss of human erythrocytes during porcine liver perfusion. Transplantation 2004; 77(9): 1416.
    • (2004) Transplantation , vol.77 , Issue.9 , pp. 1416
    • Rees, M.A.1    Butler, A.J.2    Negus, M.C.3
  • 40
    • 0034913685 scopus 로고    scopus 로고
    • Siglecs, sialic acids and innate immunity
    • Crocker PR, Varki A. Siglecs, sialic acids and innate immunity. Trends Immunol 2001; 22(6): 337.
    • (2001) Trends Immunol , vol.22 , Issue.6 , pp. 337
    • Crocker, P.R.1    Varki, A.2
  • 41
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution
    • May AP, Robinson RC, Vinson M, et al. Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution. Mol Cell 1998; 1(5): 719.
    • (1998) Mol Cell , vol.1 , Issue.5 , pp. 719
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3
  • 42
    • 0023003625 scopus 로고
    • Properties and distribution of a lectin-like hemagglutinin differentially expressed by murine stromal tissue macrophages
    • Crocker PR, Gordon S. Properties and distribution of a lectin-like hemagglutinin differentially expressed by murine stromal tissue macrophages. J Exp Med 1986; 164(6): 1862.
    • (1986) J Exp Med , vol.164 , Issue.6 , pp. 1862
    • Crocker, P.R.1    Gordon, S.2
  • 43
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • Angata T, Varki A. Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem Rev 2002; 102(2): 439.
    • (2002) Chem Rev , vol.102 , Issue.2 , pp. 439
    • Angata, T.1    Varki, A.2
  • 44
    • 0034613151 scopus 로고    scopus 로고
    • Immune inhibitory receptors
    • Ravetch JV, Lanier LL. Immune inhibitory receptors. Science 2000; 290(5489): 84.
    • (2000) Science , vol.290 , Issue.5489 , pp. 84
    • Ravetch, J.V.1    Lanier, L.L.2
  • 45
    • 0031714484 scopus 로고    scopus 로고
    • A structural difference between the cell surfaces of humans and the great apes
    • Muchmore EA, Diaz S, Varki A. A structural difference between the cell surfaces of humans and the great apes. Am J Phys Anthropol 1998; 107(2): 187.
    • (1998) Am J Phys Anthropol , vol.107 , Issue.2 , pp. 187
    • Muchmore, E.A.1    Diaz, S.2    Varki, A.3
  • 46
    • 17744416891 scopus 로고    scopus 로고
    • HLA-G inhibits the transendothelial cell migration of human NK cells: A strategy for inhibiting xenograft rejection
    • Dorling A, Monk N, Lechler R. HLA-G inhibits the transendothelial cell migration of human NK cells: a strategy for inhibiting xenograft rejection. Transplant Proc 2000; 32(5): 938.
    • (2000) Transplant Proc , vol.32 , Issue.5 , pp. 938
    • Dorling, A.1    Monk, N.2    Lechler, R.3
  • 47
    • 0035889898 scopus 로고    scopus 로고
    • HLA-G inhibits rolling adhesion of activated human NK cells on porcine endothelial cells
    • Forte P, Pazmany L, Matter-Reissmann UB, et al. HLA-G inhibits rolling adhesion of activated human NK cells on porcine endothelial cells. J Immunol 2001; 167(10): 6002.
    • (2001) J Immunol , vol.167 , Issue.10 , pp. 6002
    • Forte, P.1    Pazmany, L.2    Matter-Reissmann, U.B.3
  • 48
    • 0036533554 scopus 로고    scopus 로고
    • Genetically modified HLA class I molecules able to inhibit human NK cells without provoking alloreactive CD8+ CTLs
    • Sharland A, Patel A, Lee JH, et al. Genetically modified HLA class I molecules able to inhibit human NK cells without provoking alloreactive CD8+ CTLs. J Immunol 2002; 168(7): 3266.
    • (2002) J Immunol , vol.168 , Issue.7 , pp. 3266
    • Sharland, A.1    Patel, A.2    Lee, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.