Glycosyltransferase Function in Core 2-Type Protein O Glycosylation

REFERENCES

• Altschuler, Y., C. L. Kinlough, P. A. Poland, J. B. Bruns, G. Apodaca, O. A. Weisz, and R. P. Hughey. 2000. Clathrin-mediated endocytosis of MUC1 is modulated by its glycosylation state. Mol. Biol. Cell 11:819–831.
   PubMed Web of Science ®Google Scholar
• An, G., B. Wei, B. Xia, J. M. McDaniel, T. Ju, R. D. Cummings, J. Braun, and L. Xia. 2007. Increased susceptibility to colitis and colorectal tumors in mice lacking core 3-derived O-glycans. J. Exp. Med. 204:1417–1429.
   PubMed Web of Science ®Google Scholar
• Arkan, M. C., A. L. Hevener, F. R. Greten, S. Maeda, Z. W. Li, J. M. Long, A. Wynshaw-Boris, G. Poli, J. Olefsky, and M. Karin. 2005. IKK0beta links inflammation to obesity-induced insulin resistance. Nat. Med. 11:191–198.
   PubMed Web of Science ®Google Scholar
• Aronson, L. 1998. Animal behavior case of the month. Aggression directed toward other horses. J. Am. Vet. Med. Assoc. 213:358–359.
   PubMedGoogle Scholar
• Ashida, H., R. Maki, Y. H. Ozawa, Tani, M. Kiyohara, M. Fujita, A. Imamura, H. Ishida, M. Kiso, and K. Yamamoto. 2008. Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18:727–734.
   PubMed Web of Science ®Google Scholar
• Baum, L. G. 2002. Developing a taste for sweets. Immunity 16:5–8.
   PubMed Web of Science ®Google Scholar
• Bierhuizen, M. F., and M. Fukuda. 1992. Expression cloning of a cDNA encoding UDP-GlcNAc:Gal β1-3-GalNAc-R (GlcNAc to GalNAc) β1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen. Proc. Natl. Acad. Sci. USA 89:9326–9330.
   PubMedGoogle Scholar
• Carlow, D. A., B. Ardman, and H. J. Ziltener. 1999. A novel CD8 T cell-restricted CD45RB epitope shared by CD43 is differentially affected by glycosylation. J. Immunol. 163:1441–1448.
   PubMedGoogle Scholar
• Cho, J. H. 2008. The genetics and immunopathogenesis of inflammatory bowel disease. Nat. Rev. Immunol. 8:458–466.
   PubMed Web of Science ®Google Scholar
• Crawley, J. N. 2007. What's wrong with my mouse? Behavioral phenotyping of transgenic and knockout mice. Wiley Interscience, New York, NY.
   Google Scholar
• Dahl, G. E., N. P. Evans, L. A. Thrun, and F. J. Karsch. 1994. A central negative feedback action of thyroid hormones on thyrotropin-releasing hormone secretion. Endocrinology 135:2392–2397.
   PubMedGoogle Scholar
• Dodman, N. H., P. A. Mertens, and L. P. Aronson. 1995. Animal behavior case of the month: dogs were evaluated because of aggression. J. Am. Vet. Med. Assoc. 207:1168–1171.
   PubMedGoogle Scholar
• deVos, T., and T. A. Dick. 1991. A rapid method to determine the isotype and specificity of coproantibodies in mice infected with Trichinella or fed cholera toxin. J. Immunol. Methods 141:285–288.
   PubMedGoogle Scholar
• Ellies, L. G., S. Tsuboi, B. Petryniak, J. B. Lowe, M. Fukuda, and J. D. Marth. 1998. Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation. Immunity 9:881–890.
   PubMed Web of Science ®Google Scholar
• Fatjo, J., M. Amat, and X. Manteca. 2003. Animal behavior case of the month: aggression in dogs. J. Am. Vet. Med. Assoc. 223:623–626.
   PubMedGoogle Scholar
• Fliers, E., U. A. Unmehopa, and A. Alkemade. 2006. Functional neuroanatomy of thyroid hormone feedback in the human hypothalamus and pituitary gland. Mol. Cell Endocrinol. 251:1–8.
   PubMed Web of Science ®Google Scholar
• Furuta, G. T., J. R. Turner, C. T. Taylor, R. M. Hershberg, K. Comerford, S. Narravula, D. K. Podolsky, and S. P. Colgan. 2001. Hypoxia-inducible factor 1-dependent induction of intestinal trefoil factor protests barrier function during hypoxia. J. Exp. Med. 193:1027–1034.
   PubMed Web of Science ®Google Scholar
• Gauguet, J. M., S. D. Rosen, J. D. Marth, and U. H. von Andrian. 2004. Core 2 branching β1,6-N-acetylglucosaminyltransferase and high endothelial cell N-acetylglucosamine-6-sulfotransferase exert differential control over B- and T-lymphocyte homing to peripheral lymph nodes. Blood 104:4104–4112.
   PubMedGoogle Scholar
• Grewal, P. K., S. Uchiyama, D. Ditto, N. Varki, D. T. Le, V. Nizet, and J. D. Marth. 2008. The Ashwell receptor mitigates the lethal coagulopathy of sepsis. Nat. Med. 14:648–655.
   PubMed Web of Science ®Google Scholar
• Hassan, H., C. A. Reis, E. P. Bennett, E. Mirgorodskaya, P. Roepstorff, M. A. Hollingsworth, J. Burchell, J. Taylor-Papadimitriou, and H. Clausen. 2000. The lectin domain of UDP-N-acetyl-d-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. J. Biol. Chem. 275:38197–38205.
   PubMedGoogle Scholar
• Hiraoka, N., H. Kawashima, B. Petryniak, J. Nakayama, J. Mitoma, J. D. Marth, J. B. Lowe, and M. Fukuda. 2004. Core 2 branching β1,6-N-acetylglucosaminyltransferase and high endothelial venule-restricted sulfotransferase collaboratively control lymphocyte homing. J. Biol. Chem. 279:3058–3067.
   PubMedGoogle Scholar
• Ho, S. B., L. A. Dvorak, R. E. Moor, A. C. Jacobson, M. R. Frey, J. Corredor, D. B. Polk, and L. L. Shekels. 2006. Cysteine-rich domains of Muc3 intestinal mucin promote cell migration, inhibit apoptosis, and accelerate wound healing. Gastroenterology 131:1501–1517.
   PubMedGoogle Scholar
• Homeister, J. W., A. D. Thall, B. Petryniak, P. Maly, C. E. Rogers, P. L. Smith, R. J. Kelly, K. M. Gersten, S. W. Askari, G. Cheng, G. Smithson, R. M. Marks, A. K. Misra, O. Hindsgaul, U. H. von Andrian, and J. B. Lowe. 2001. The α(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative control over selectin-dependent leukocyte recruitment and lymphocyte homing. Immunity 15:115–126.
   PubMed Web of Science ®Google Scholar
• Iwai, T., N. Inaba, A. Naundorf, Y. Zhang, M. Gotoh, H. Iwasaki, T. Kudo, A. Togayachi, Y. Ishizuka, H. Nakanishi, and H. Narimatsu. 2002. Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide β1,3-N-acetylglucosaminyltransferase (β3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans. J. Biol. Chem. 277:12802–12809.
   PubMedGoogle Scholar
• Jang-Lee, J., S. J. North, M. Sutton-Smith, D. Goldberg, M. Panico, H. Morris, S. Haslam, and A. Dell. 2006. Glycomic profiling of cells and tissues by mass spectrometry: fingerprinting and sequencing methodologies. Methods Enzymol. 415:59–86.
   PubMed Web of Science ®Google Scholar
• Ju, T., K. Brewer, A. D'Souza, R. D. Cummings, and W. M. Canfield. 2002. Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277:178–186.
   PubMedGoogle Scholar
• Kawakubo, Y. M., Ito, Y. Okimura, M. Kobayashi, K. Sakura, S. Kasama, M. N. Fukuda, M. Fukuda, T. Katsuyama, and J. Nakayama. 2004. Natural antibiotic function of a human gastric mucin against Helicobacter pylori infection. Science 305:1003–1006.
   PubMed Web of Science ®Google Scholar
• Long, J. M., P. LaPorte, S. Merscher, B. Funke, B. Saint-Jore, A. Puech, R. Kucherlapati, B. E. Morrow, A. I. Skoultchi, and A. Wynshaw-Boris. 2006. Behavior of mice with mutations in the conserved region deleted in velocardiofacial/DiGeorge syndrome. Neurogenetics 7:247–257.
   PubMedGoogle Scholar
• Long, J. M., P. LaPorte, R. Paylor, and A. Wynshaw-Boris. 2004. Expanded characterization of the social interaction abnormalities in mice lacking Dvl1. Genes Brain Behav. 3:51–62.
   PubMedGoogle Scholar
• Lowe, J. B. 2001. Glycosylation, immunity, and autoimmunity. Cell 104:809–812.
   PubMed Web of Science ®Google Scholar
• Lowe, J. B., and J. D. Marth. 2003. A genetic approach to mammalian glycan function. Annu. Rev. Biochem. 72:643–691.
   PubMed Web of Science ®Google Scholar
• Magnet, A. D., and M. Fukuda. 1997. Expression of the large I antigen forming β-1,6-N-acetylglucosaminyltransferase in various tissues of adult mice. Glycobiology 7:285–295.
   PubMedGoogle Scholar
• Mankertz, J., and J. D. Schulzke. 2007. Altered permeability in inflammatory bowel disease: pathophysiology and clinical implications. Curr. Opin. Gasteroenterol. 23:379–383.
   PubMed Web of Science ®Google Scholar
• Marians, R. C., L. Ng, H. C. Blair, P. Unger, P. N. Graves, and T. F. Davies. 2002. Defining thyrotropin-dependent and -independent steps of thyroid hormone synthesis by using thyrotropin receptor-null mice. Proc. Natl. Acad. Sci. USA 99:15776–15781.
   PubMed Web of Science ®Google Scholar
• Marth, J. D. and P. K. Grewal. 2008. Mammalian glycosylation in immunity. Nat. Rev. Immunol. 8:874–887.
   PubMed Web of Science ®Google Scholar
• Merzaban, J. S., J. Zuccolo, S. Y. Corbel, M. J. Williams, and H. J. Ziltener. 2005. An alternate Core 2β1,6-N-acetylglucosaminyltransferase selectively contributes to P-selectin ligand formation in activated CD8 T cells. J. Immunol. 174:4051–4059.
   PubMedGoogle Scholar
• Murthy, A. K., C. N. Dubose, J. A. Banas, J. J. Coalson, and B. P. Arulanandam. 2006. Contribution of polymeric immunoglobulin receptor to regulation of intestinal inflammation in dextran sulfate sodium-induced colitis. Gastroenterology 26:1372–1380.
   Google Scholar
• Murthy, S. N., H. S. Cooper, H. Shim, R. S. Shah, S. A. Ibrahim, and D. J. Sedergran. 1993. Treatment of dextran sulfate sodium-induced murine colitis by intracolonic cyclosporine. Dig. Dis. Sci. 38:1722–1734.
   PubMed Web of Science ®Google Scholar
• Nagy, A., J. Rossant, R. Nagy, W. Abramow-Newerly, and J. C. Roder. 1993. Derivation of completely cell culture-derived mice from early-passage embryonic stem cells. Proc. Natl. Acad. Sci. USA 90:8424–8428.
   PubMed Web of Science ®Google Scholar
• Okayasu, I., S. Hatakeyama, M. Yamada, T. Ohkusa, Y. Inagaki, and R. Nakaya. 1990. A novel method in the induction of reliable experimental acute and chronic ulcerative colitis in mice. Gastroenterology 98:694–702.
   PubMed Web of Science ®Google Scholar
• Oliveira, K. J., T. M. Ortiga-Carvalho, A. Cabanelas, M. A. Veiga, K. Aoki, H. Ohki-Hamazaki, K. Wada, E. Wada, and C. C. Pazos-Moura. 2006. Disruption of neuromedin B receptor gene results in dysregulation of the pituitary-thyroid axis. J. Mol. Endocrinol. 36:73–80.
   PubMedGoogle Scholar
• Perez-Vilar, J., and R. L. Hill. 1999. The structure and assembly of secreted mucins. J. Biol. Chem. 274:31751–31754.
   PubMed Web of Science ®Google Scholar
• Peterson, D. A., D. N. Frank, N. R. Pace, and J. I. Gordon. 2008. Metagenomic approaches for defining the pathogenesis of inflammatory bowel disease. Cell Host Microbe 3:417–427.
   PubMed Web of Science ®Google Scholar
• Raman, J., T. A. Fritz, T. A. Gerken, O. Jamison, D. Live, M. Liu, and L. A. Tabak. 2008. The catalytic and lectin domains of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferasae function in concert to direct glycosylation site selection. J. Biol. Chem. 283:22942–22951.
   PubMedGoogle Scholar
• Rosen, S. D. 2004. Ligands for L-selectin: homing, inflammation, and beyond. Annu. Rev. Immunol. 22:129–156.
   PubMed Web of Science ®Google Scholar
• Rossi, F. M. V., S. Y. Corbel, J. S. Merzaban, D. A. Carlow, K. Gossens, J. Duenas, L. So, L. Yi, and H. J. Ziltener. 2005. Recruitment of adult thymic progenitors is regulated by P-selectin and its ligand PSGL-1. Nat. Immunol. 6:626–634.
   PubMed Web of Science ®Google Scholar
• Satsangi, J., M. Parkes, E. Louis, L. Hashimoto, N. Kato, K. Welsh, J. D. Terwilliger, G. M. Lathrop, J. I. Bell, and D. P. Jewell. 1996. Two stage genome-wide search in inflammatory bowel disease provides evidence for susceptibility loci on chromosomes 3, 7, and 12. Nat. Genet. 14:199–202.
   PubMed Web of Science ®Google Scholar
• Schachter, H. 2000. The joys of HexNAc: the synthesis and function of N- and O-glycan branches. Glycoconj. J. 17:465–483.
   PubMed Web of Science ®Google Scholar
• Schachter, H., and I. Brockhausen. 1989. The biosynthesis of branched O-glycans. Symp. Soc. Exp. Biol. 43:1–26.
   PubMedGoogle Scholar
• Schwientek, T., M. Nomoto, S. B. Levery, G. Merkx, A. G. van Kessel, E. P. Bennett, M. A. Hollingsworth, and H. Clausen. 1999. Control of O-glycan branch formation: molecular cloning of human cDNA encoding a novel β1,6-N-acetylglucosaminyltransferase forming core 2 and core 4. J. Biol. Chem. 274:4504–4512.
   PubMedGoogle Scholar
• Schwientek, T., J. C. Yeh, S. B. Levery, B. Keck, G. Merkx, A. G. van Kessel, M. Fukuda, and H. Clausen. 2000. Control of O-glycan branch formation: molecular cloning and characterization of a novel thymus-associated Core 2 β1,6-N-acteylglucosaminyltransferase. J. Biol. Chem. 275:11106–11113.
   PubMedGoogle Scholar
• Shafi, R., S. P. Iyer, L. G. Ellies, N. O'Donnell, K. W. Marek, D. Chui, G. W. Hart, and J. D. Marth. 2000. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc. Natl. Acad. Sci. USA 97:5735–5739.
   PubMed Web of Science ®Google Scholar
• Simmons, P. J., J. Levesque, and D. N. Haylock. 2001. Mucin-like molecules as modulators of the survival and proliferation of primitive hematopoietic cells. Ann. N. Y. Acad. Sci. 938:196–207.
   PubMed Web of Science ®Google Scholar
• Stanley, P. 2007. Regulation of Notch signaling by glycosylation. Curr. Opin. Struct. Biol. 17:530–535.
   PubMedGoogle Scholar
• Stein, J., J. Ries, and K. B. Barrett. 1998. Disruption of intestinal barrier function associated with experimental colitis: possible role of mast cells. Am. J. Physiol. 274:G203–G209.
   PubMedGoogle Scholar
• Sutton-Smith, M., H. R. Morris, and A. Dell. 2000. A rapid mass spectrometric strategy suitable for the investigation of glycan alterations in knockout mice. Tetrahedron Asymmetry 11:363–369.
   Google Scholar
• Tarp, M. A., and H. Clausen. 2008. Mucin-type O glycosylation and its potential use in drug and vaccine development. Biochim. Biophys. Acta 1780:546–563.
   PubMed Web of Science ®Google Scholar
• Ten Hagen, K. G., T. A. Fritz, and L. A. Tabak. 2003. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13:1R–16R.
   PubMedGoogle Scholar
• Tenno, M., K. Ohtsubo, F. K. Hagen, D. Ditto, A. Zarbock, P. Schaerli, U. H. von Andrian, K. Ley, D. Le, L. A. Tabak, and J. D. Marth. 2007. Initiation of protein O glycosylation by polypeptide GalNAcT-1 in vascular biology and humoral immunity. Mol. Cell. Biol. 27:8783–8796.
   PubMedGoogle Scholar
• van der Sluis, M., B. A. E. de Koning, A. C. J. M. de Bruijn, A. Velcich, J. P. P. Meijerink, J. B. van Goudoever, H. A. Buller, and A. W. C. Einerhand. 2006. Muc2-deficient mice spontaneously develop colitis, indicating that Muc2 is critical for colonic protection. Gastroenterology 131:117–129.
   PubMed Web of Science ®Google Scholar
• Varki, A. 2006. Nothing in glycobiology makes sense, except in the light of evolution. Cell 126:841–845.
   PubMed Web of Science ®Google Scholar
• Venero, C., A. Guadano-Ferraz, A. I. Herrero, K. Nordstrom, J. Manzano, G. M. de Escobar, J. Bernal, and B. Vennstrom. 2005. Anxiety, memory impairment, and locomotor dysfunction caused by a mutant thyroid hormone receptor α1 can be ameliorated by T3 treatment. Genes Dev. 19:2152–2163.
   PubMed Web of Science ®Google Scholar
• Verfaillie, C. M. 1998. Adhesion receptors as regulators of the hematopoietic process. Blood 92:2609–2612.
   PubMed Web of Science ®Google Scholar
• Wang, H., R. Tang, W. Zhang, K. Amirikian, Z. Geng, J. Geng, R. P. Hebbel, L. Xia, J. D. Marth, M. Fukuda, S. Katoh, and Y. Huo. 2009 Core 2 1-6-N-glucosaminyltransferase-I is crucial for the formation of atherosclerotic lesions in apolipoprotein E-deficient mice. Arterioscler. Thromb. Vasc. Biol. 29:180–187.
   PubMedGoogle Scholar
• Weninger, W., L. H. Ulfman, G. Cheng, N. Souchkova, E. J. Quackenbush, J. B. Lowe, and U. H. von Andrian. 2000. Specialized contributions by α(1,3)-fucosyltransferase-IV and FucT-VII during leukocyte rolling in dermal microvessels. Immunity 12:665–676.
   PubMed Web of Science ®Google Scholar
• Xavier, R. J., and D. K. Podolsky. 2007. Unraveling the pathogenesis of inflammatory bowel disease. Nature 448:427–434.
   PubMed Web of Science ®Google Scholar
• Yamada, M., Y. Saga, N. Shibusawa, J. Hirato, M. Murakami, T. Iwasaki, K. Hashimoto, T. Satoh, K. Wakabayashi, M. M. Taketo, and M. Mori. 1997. Tertiary hypothyroidism and hyperglycemia in mice with targeted disruption of the thyrotropin-releasing hormone gene. Proc. Natl. Acad. Sci. USA 94:10862–10867.
   PubMedGoogle Scholar
• Yeh, J. C., N. Hiraoka, B. Petryniak, J. Nakayama, L. G. Ellies, D. Rabuka, O. Hindsgaul, J. D. Marth, J. B. Lowe, and M. Fukuda. 2001. Novel sulfated lymphocyte homing receptors and their control by a Core1 extension β1,3,-N-acetylglucosaminyltransferase. Cell 105:957–969.
   PubMed Web of Science ®Google Scholar
• Yeh, J. C., E. Ong, and M. Fukuda. 1999. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms Core 2, Core 4, and I branches. J. Biol. Chem. 274:3215–3221.
   PubMedGoogle Scholar
• Yoshida, A., K. Kobayashi, H. Manya, K. Taniguchi, H. Kano, M. Mizuno, T. Inazu, H. Mitsuhashi, S. Takahashi, M. Takeuchi, R. Herrmann, V. Straub, B. Talim, T. Voit, H. Topaloglu, T. Toda, and T. Endo. 2001. Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev. Cell 1:717–724.
   PubMed Web of Science ®Google Scholar
• Zachara, N. E., and G. W. Hart. 2006. Cell signaling, the essential role of O-GlcNAc. Biochim. Biophys. Acta 1761:599–617.
   PubMed Web of Science ®Google Scholar
• Zhang, W., D. Betel, and H. Schachter. 2002. Cloning and expression of a novel UDP-GlcNAc:α-3-d-mannoside β1,2-N-acetylglucosaminyltransferase I. Biochem. J. 361:153–162.
   PubMedGoogle Scholar