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Volumn 427, Issue 1, 2010, Pages 179-188

Cloning and functional characterization of pig CMP- N-acetylneuraminic acid hydroxylase for the synthesis of N-glycolylneuraminic acid as the xenoantigenic determinant in pig-human xenotransplantation

Author keywords

CMP N acetylneuraminic acid hydroxylase; Hanganutziu Deicher; Human serum mediated cytotoxicity; Hyperacute rejection; N glycolylneuraminic acid

Indexed keywords

COLON TISSUES; ECTOPIC EXPRESSIONS; EXPRESSION PATTERNS; FUNCTIONAL CHARACTERIZATION; HANGANUTZIU-DEICHER; HYDROXYLASES; KEY ENZYMES; N-ACETYLNEURAMINIC ACID; N-GLYCOLYLNEURAMINIC ACID; OPEN READING FRAME; PIG KIDNEY; SHORT HAIRPIN RNA; SMALL INTESTINE; TRANSFECTANTS; TRANSFECTED CELLS; XENOTRANSPLANTATION;

EID: 77950874526     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090835     Document Type: Article
Times cited : (49)

References (41)
  • 1
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Kelm, S. and Schauer, R. (1997) Sialic acids in molecular and cellular interactions. Int. Rev. Cytol. 175, 137-240
    • (1997) Int. Rev. Cytol. , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 2
    • 0032443144 scopus 로고    scopus 로고
    • Structure, function and metabolism of sialic acids
    • Traving, C. and Schauer, R. (1998) Structure, function and metabolism of sialic acids. Cell. Mol. Life Sci. 54, 1330-1349
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1330-1349
    • Traving, C.1    Schauer, R.2
  • 3
    • 0026541128 scopus 로고
    • Diversity in the sialic acids
    • Varki, A. (1992) Diversity in the sialic acids. Glycobiology 2, 25-40
    • (1992) Glycobiology , vol.2 , pp. 25-40
    • Varki, A.1
  • 5
    • 0032551747 scopus 로고    scopus 로고
    • CMP- N-acetylneuraminic acid hydroxylase is exclusively inactive in humans. Biochem
    • Irie, A. and Suzuki, A. (1998) CMP- N-acetylneuraminic acid hydroxylase is exclusively inactive in humans. Biochem. Biophys. Res. Commun. 248, 330-333
    • (1998) Biophys. Res. Commun. , vol.248 , pp. 330-333
    • Irie, A.1    Suzuki, A.2
  • 7
    • 0029000263 scopus 로고
    • Molecular cloning of cytidine monophospho- N-acetylneuraminic acid hydroxylase: Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid
    • Kawano, T., Koyama, S., Takematsu, H., Kozutsumi, Y., Kawasaki, H., Kawashima, S., Kawasaki, T. and Suzuki, A. (1995) Molecular cloning of cytidine monophospho- N-acetylneuraminic acid hydroxylase: regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270, 16458-16463
    • (1995) J. Biol. Chem. , vol.270 , pp. 16458-16463
    • Kawano, T.1    Koyama, S.2    Takematsu, H.3    Kozutsumi, Y.4    Kawasaki, H.5    Kawashima, S.6    Kawasaki, T.7    Suzuki, A.8
  • 8
    • 0025520584 scopus 로고
    • Participation of cytochrome b5 in CMP- N-acetylneuraminic acid hydroxylation in mouse liver cytosol
    • Kozutsumi, Y., Kawano, T., Yamakawa, T. and Suzuki, A. (1990) Participation of cytochrome b5 in CMP- N-acetylneuraminic acid hydroxylation in mouse liver cytosol. J. Biochem. 108, 704-706
    • (1990) J. Biochem. , vol.108 , pp. 704-706
    • Kozutsumi, Y.1    Kawano, T.2    Yamakawa, T.3    Suzuki, A.4
  • 9
    • 0024391058 scopus 로고
    • Biosynthesis of N-glycolyneuraminic acid: The primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool
    • Muchmore, E. A., Milewski, M., Varki, A. and Diaz, S. (1989) Biosynthesis of N-glycolyneuraminic acid: the primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool. J. Biol. Chem. 264, 20216-20223
    • (1989) J. Biol. Chem. , vol.264 , pp. 20216-20223
    • Muchmore, E.A.1    Milewski, M.2    Varki, A.3    Diaz, S.4
  • 10
    • 0023824137 scopus 로고
    • The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid
    • Shaw, L. and Schauer, R. (1988) The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol. Chem. Hoppe Seyler 369, 477-486
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 477-486
    • Shaw, L.1    Schauer, R.2
  • 11
    • 0001202397 scopus 로고
    • Über die Erzeugung heterospezifischer Hämagglutinine durch Injektion artfremden Serums
    • Deicher, H. (1926) Über die Erzeugung heterospezifischer Hämagglutinine durch Injektion artfremden Serums. Z. Hyg. 106, 561-579
    • (1926) Z. Hyg. , vol.106 , pp. 561-579
    • Deicher, H.1
  • 12
    • 0001316176 scopus 로고
    • Hémagglutinines hétérogénétiques aprés injection de sérum de cheval
    • Hanganutziu, M. (1924) Hémagglutinines hété rogénétiques aprés injection de sérum de cheval. C.R. Séances Soc. Biol. 91, 1457-1459
    • (1924) C.R. Séances Soc. Biol. , vol.91 , pp. 1457-1459
    • Hanganutziu, M.1
  • 13
    • 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. and Okouchi, K. (1977) Antigen of "serum sickness" type of heterophile antibodies in human sera: identification as gangliosides with N-glycolylneuraminic acid. Biochem. Biophys. Res. Commun. 79, 388-395
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 388-395
    • Higashi, H.1    Naiki, M.2    Matuo, S.3    Okouchi, K.4
  • 14
    • 0018152253 scopus 로고
    • Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid
    • Merrick, J. M., Zadarlik, K. and Milgrom, F. (1978) Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid. Int. Arch. Allergy Appl. Immunol. 57, 477-480
    • (1978) Int. Arch. Allergy Appl. Immunol. , vol.57 , pp. 477-480
    • Merrick, J.M.1    Zadarlik, K.2    Milgrom, F.3
  • 15
    • 21244478903 scopus 로고    scopus 로고
    • Effects of natural human antibodies against a nonhuman sialic acid that metabolically incorporates into activated and malignant immune cells
    • Nguyen, D. H., Tangvoranuntakul, P. and Varki, A. (2005) Effects of natural human antibodies against a nonhuman sialic acid that metabolically incorporates into activated and malignant immune cells. J. Immunol. 175, 228-236 (Pubitemid 40884323)
    • (2005) Journal of Immunology , vol.175 , Issue.1 , pp. 228-236
    • Nguyen, D.H.1    Tangvoranuntakul, P.2    Varki, A.3
  • 16
    • 33645532616 scopus 로고    scopus 로고
    • Hypoxic culture induces expression of sialin, a sialic acid transporter, and cancer-associated gangliosides containing non-human sialic acid on human cancer cells
    • Yin, J., Hashimoto, A., Izawa, M., Miyazaki, K., Chen, G. Y., Takematsu, H., Kozutsumi, Y., Suzuki, A., Furuhata, K., Cheng, F. L. et al. (2006) Hypoxic culture induces expression of sialin, a sialic acid transporter, and cancer-associated gangliosides containing non-human sialic acid on human cancer cells. Cancer Res. 66, 2937-2945
    • (2006) Cancer Res. , vol.66 , pp. 2937-2945
    • Yin, J.1    Hashimoto, A.2    Izawa, M.3    Miyazaki, K.4    Chen, G.Y.5    Takematsu, H.6    Kozutsumi, Y.7    Suzuki, A.8    Furuhata, K.9    Cheng, F.L.10
  • 17
    • 0026090165 scopus 로고
    • Accommodation: A working paradigm for progressing toward clinical discordant xenografting
    • Bach, F. H., Turman, M. A., Vercellotti, G. M., Platt, J. L. and Dalmasso, A. P. (1991) Accommodation: a working paradigm for progressing toward clinical discordant xenografting. Transplant Proc. 23, 205-207
    • (1991) Transplant Proc. , vol.23 , pp. 205-207
    • Bach, F.H.1    Turman, M.A.2    Vercellotti, G.M.3    Platt, J.L.4    Dalmasso, A.P.5
  • 18
    • 0028171342 scopus 로고
    • Oligosaccharides and discordant xenotransplantation
    • Cooper, D. K., Koren, E. and Oriol, R. (1994) Oligosaccharides and discordant xenotransplantation. Immunol. Rev. 141, 31-58
    • (1994) Immunol. Rev. , vol.141 , pp. 31-58
    • Cooper, D.K.1    Koren, E.2    Oriol, R.3
  • 19
    • 0033054877 scopus 로고    scopus 로고
    • Significance of anti-Gal IgG in chronic xenograft rejection
    • Galili, U. (1999) Significance of anti-Gal IgG in chronic xenograft rejection. Transplant Proc. 31, 940-941
    • (1999) Transplant Proc. , vol.31 , pp. 940-941
    • Galili, U.1
  • 21
    • 2442538314 scopus 로고    scopus 로고
    • Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation?
    • Miwa, Y., Kobayashi, T., Nagasaka, T., Liu, D., Yu, M., Yokoyama, I., Suzuki, A. and Nakao, A. (2004) Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation? Xenotransplantation 11, 247-253
    • (2004) Xenotransplantation , vol.11 , pp. 247-253
    • Miwa, Y.1    Kobayashi, T.2    Nagasaka, T.3    Liu, D.4    Yu, M.5    Yokoyama, I.6    Suzuki, A.7    Nakao, A.8
  • 23
    • 0034787250 scopus 로고    scopus 로고
    • Cloning and expression of a membrane-bound CMP- N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens
    • Martensen, I., Schauer, R. and Shaw, L. (2001) Cloning and expression of a membrane-bound CMP- N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens. Eur. J. Biochem. 268, 5157-5166
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5157-5166
    • Martensen, I.1    Schauer, R.2    Shaw, L.3
  • 24
    • 0029941677 scopus 로고    scopus 로고
    • CMP- N-acetylneuraminic acid hydroxylase: The first cytosolic Rieske iron-sulphur protein to be described in Eukarya
    • Schlenzka, W., Shaw, L., Kelm, S., Schmidt, C. L., Bill, E., Trautwein, A. X., Lottspeich, F. and Schauer, R. (1996) CMP- N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya. FEBS Lett. 385, 197-200
    • (1996) FEBS Lett. , vol.385 , pp. 197-200
    • Schlenzka, W.1    Shaw, L.2    Kelm, S.3    Schmidt, C.L.4    Bill, E.5    Trautwein, A.X.6    Lottspeich, F.7    Schauer, R.8
  • 25
    • 0027945344 scopus 로고
    • Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands
    • Schlenzka, W., Shaw, L., Schneckenburger, P. and Schauer, R. (1994) Purification and characterization of CMP- N-acetylneuraminic acid hydroxylase from pig submandibular glands. Glycobiology 4, 675-683 (Pubitemid 24327733)
    • (1994) Glycobiology , vol.4 , Issue.5 , pp. 675-683
    • Schlenzka, W.1    Shaw, L.2    Schneckenburger, P.3    Schauer, R.4
  • 26
    • 0024851291 scopus 로고
    • Separation of oligosaccharides using high-performance anion-exchange chromatography with pulsed amperometric detection
    • Townsend, R. R., Hardy, M. R. and Lee, Y. C. (1989) Separation of oligosaccharides using high-performance anion-exchange chromatography with pulsed amperometric detection. Methods Enzymol. 179, 65-76
    • (1989) Methods Enzymol. , vol.179 , pp. 65-76
    • Townsend, R.R.1    Hardy, M.R.2    Lee, Y.C.3
  • 29
    • 33747603226 scopus 로고    scopus 로고
    • A study of the xenoantigenicity of neonatal porcine islet-like cell clusters (NPCC) and the efficiency of adenovirus-mediated DAF (CD55) expression
    • Omori, T., Nishida, T., Komoda, H., Fumimoto, Y., Ito, T., Sawa, Y., Gao, C., Nakatsu, S., Shirakura, R. and Miyagawa, S. (2006) A study of the xenoantigenicity of neonatal porcine islet-like cell clusters (NPCC) and the efficiency of adenovirus-mediated DAF (CD55) expression. Xenotransplantation 13, 455-464
    • (2006) Xenotransplantation , vol.13 , pp. 455-464
    • Omori, T.1    Nishida, T.2    Komoda, H.3    Fumimoto, Y.4    Ito, T.5    Sawa, Y.6    Gao, C.7    Nakatsu, S.8    Shirakura, R.9    Miyagawa, S.10
  • 30
    • 0017376971 scopus 로고
    • Biosynthesis of N-glycolylneuraminic acid in porcine submandibular glands: Subcellular site of hydroxylation of N-acetylneuraminic acid in the course of glycoprotein biosynthesis
    • Buscher, H. P., Casals-Stenzel, J., Schauer, R. and Mestres-Ventura, P. (1977) Biosynthesis of N-glycolylneuraminic acid in porcine submandibular glands: subcellular site of hydroxylation of N-acetylneuraminic acid in the course of glycoprotein biosynthesis. Eur. J. Biochem. 77, 297-310
    • (1977) Eur. J. Biochem. , vol.77 , pp. 297-310
    • Buscher, H.P.1    Casals-Stenzel, J.2    Schauer, R.3    Mestres-Ventura, P.4
  • 31
    • 0015136395 scopus 로고
    • Hydroxylation and O-acetylation of N-acetylneuraminic acid bound to glycoproteins of isolated subcellular membranes from porcine and bovine submaxillary glands
    • Schauer, R. and Wember, M. (1971) Hydroxylation and O-acetylation of N-acetylneuraminic acid bound to glycoproteins of isolated subcellular membranes from porcine and bovine submaxillary glands. Hoppe Seylers Z. Physiol. Chem. 352, 1282-1290
    • (1971) Hoppe Seylers Z. Physiol. Chem. , vol.352 , pp. 1282-1290
    • Schauer, R.1    Wember, M.2
  • 32
    • 0026774530 scopus 로고
    • Developmental sialic acid modifications in rat organs
    • Muchmore, E. A. (1992) Developmental sialic acid modifications in rat organs. Glycobiology 2, 337-343
    • (1992) Glycobiology , vol.2 , pp. 337-343
    • Muchmore, E.A.1
  • 33
    • 0032411429 scopus 로고    scopus 로고
    • The role of CMP- N-acetylneuraminic acid hydroxylase in determining the level of N-glycolylneuraminic acid in porcine tissues
    • Malykh, Y. N., Shaw, L. and Schauer, R. (1998) The role of CMP- N-acetylneuraminic acid hydroxylase in determining the level of N-glycolylneuraminic acid in porcine tissues. Glycoconjugate J. 15, 885-893
    • (1998) Glycoconjugate J. , vol.15 , pp. 885-893
    • Malykh, Y.N.1    Shaw, L.2    Schauer, R.3
  • 34
    • 0037338532 scopus 로고    scopus 로고
    • Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine
    • Malykh, Y. N., King, T. P., Logan, E., Kelly, D., Schauer, R. and Shaw, L. (2003) Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine. Biochem. J. 370, 601-607
    • (2003) Biochem. J. , vol.370 , pp. 601-607
    • Malykh, Y.N.1    King, T.P.2    Logan, E.3    Kelly, D.4    Schauer, R.5    Shaw, L.6
  • 35
    • 0027160902 scopus 로고
    • Characterization of ganglioside expression in human melanoma cells: Immunological and biochemical analysis
    • Kawashima, I., Ozawa, H., Kotani, M., Suzuki, M., Kawano, T., Gomibuchi, M. and Tai, T. (1993) Characterization of ganglioside expression in human melanoma cells: immunological and biochemical analysis. J. Biochem. 114, 186-193
    • (1993) J. Biochem. , vol.114 , pp. 186-193
    • Kawashima, I.1    Ozawa, H.2    Kotani, M.3    Suzuki, M.4    Kawano, T.5    Gomibuchi, M.6    Tai, T.7
  • 36
    • 0028811673 scopus 로고
    • Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis
    • Sandrin, M. S., Fodor, W. L., Mouhtouris, E., Osman, N., Cohney, S., Rollins, S. A., Guilmette, E. R., Setter, E., Squinto, S. P. and McKenzie, I. F. (1995) Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis. Nat. Med. 1, 1261-1267
    • (1995) Nat. Med. , vol.1 , pp. 1261-1267
    • Sandrin, M.S.1    Fodor, W.L.2    Mouhtouris, E.3    Osman, N.4    Cohney, S.5    Rollins, S.A.6    Guilmette, E.R.7    Setter, E.8    Squinto, S.P.9    McKenzie, I.F.10
  • 37
    • 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. and Taniguchi, N. (1997) Significant downregulation of the major swine xenoantigen by N-acetylglucosaminyltransferase III gene transfection. Biochem. Biophys. Res. Commun. 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
  • 39
    • 0028351036 scopus 로고
    • Antibody-dependent cell-mediated cytotoxicity against porcine endothelium induced by a majority of human sera
    • Schaapherder, A. F., Daha, M. R., te Bulte, M. T., van der Woude, F. J. and Gooszen, H. G. (1994) Antibody-dependent cell-mediated cytotoxicity against porcine endothelium induced by a majority of human sera. Transplantation 57, 1376-1382
    • (1994) Transplantation , vol.57 , pp. 1376-1382
    • Schaapherder, A.F.1    Daha, M.R.2    Te Bulte, M.T.3    Van Der Woude, F.J.4    Gooszen, H.G.5
  • 40
    • 0030852709 scopus 로고    scopus 로고
    • Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(α1,3)Galactose epitope
    • McMorrow, I. M., Comrack, C. A., Sachs, D. H. and DerSimonian, H. (1997) Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(α1,3)Galactose epitope. Transplantation 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
  • 41
    • 20944446027 scopus 로고    scopus 로고
    • Reducing Gal expression on the pig organ: A retrospective review
    • Ezzelarab, M. and Cooper, D. K. (2005) Reducing Gal expression on the pig organ: a retrospective review. Xenotransplantation 12, 278-285
    • (2005) Xenotransplantation , vol.12 , pp. 278-285
    • Ezzelarab, M.1    Cooper, D.K.2


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