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N-Acetyllactosaminide Beta-1,6-N-Acetylglucosaminyl-Transferase (GCNT2) (IGnT)

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Handbook of Glycosyltransferases and Related Genes

Abstract

During the development, poly-N-acetyllactosamine in human erythrocytes changes from linear form, N-acetyllactosamine repeats (i-antigen), to branched form (I-antigen). This conversion takes place due to an appearance of N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase (I enzyme, also called I-branching enzyme, or GCNT2), transferring N-acetylglucosamine to galactose residue of poly-N-acetyllactosamine. The presence of I-enzyme was assumed based on a structural change, which was described in (Fukuda et al. 1979, Fig. 33.1). These carbohydrate structure i/I antigens and adult patients with antibodies reacting against i antigen were recognized. Antigen in those patients exhibited coagulation of blood cells when exposed to low temperature that caused cold hemolytic anemia. By using these antibodies, Chinese hamster ovary (CHO) cells that was transfected with polyoma large T antigen was used for expression cloning of I enzyme. Upon cloning of I-branching enzyme, the amino acid sequence of I-branching enzyme was found to be highly homologous to β-1,6-N-acetylglucosaminyltransferase (GCNT1) (C2GnT-1), which forms core2 branch of O-glycans. C2GnT-1 enzyme transfers N-acetylglucosamine to GalNAc residue of Galβ1-3GalNAc-Ser/Thr in β-1.6 linkage. These studies established that the carbohydrate structure similar to each other has similar enzyme protein structure; thus, the concept of the gene family in glycosyltransferases was established.

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References

  • Bierhuizen MFA, Mattei M-G, Fukuda M (1993) Expression of the developmental I antigen by a cloned human cDNA encoding a member of a β-1.6-N-acetylglucosaminyltransferase gene family. Genes Dev 7:468–478

    Article  CAS  PubMed  Google Scholar 

  • Borck G, Kakar N, Hoch J, Friedrich K, Freudenberg J, Nurnberg G, Yilmaz R, Daud S, Baloch DM, Nurnberg P, Oldenburg J, Ahmad J, Kubisch C (2012) An Alu repeat-mediated genomic GCNT2 deletion underlies congenital cataracts and adult I blood group. Hum Genet 131:209–216

    Article  CAS  PubMed  Google Scholar 

  • Chen G-Y, Kurosawa N, Muramatsu T (2000) A novel variant form of murine β-1,6-N-acetylglucosaminyltransferase forming branches in poly-N-acetyllactosamines. Glycobiology 10:1001–1011

    Article  CAS  PubMed  Google Scholar 

  • Chen G-Y, Muramatsu H, Kondo M, Kurosawa N, Miyake Y, Takeda N, Muramatsu T (2005) Abnormalities caused by carbohydrate alterations in Iβ6-N-acetylglucosaminyltransferase-deficient mice. Mol Cell Biol 25:7828–7838

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Fukuda M, Fukuda MN, Hakomori S (1979) Developmental change and genetic defect in the carbohydrate structure of band 3 glycoprotein of human erythrocyte membrane. J Biol Chem 254:3700–3703

    CAS  PubMed  Google Scholar 

  • Fukuda M, Dell A, Oates JE, Fukuda MN (1984) Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes. J Biol Chem 259:8260–8273

    CAS  PubMed  Google Scholar 

  • Fukuda MN, Dell A, Oates JE, Fukuda M (1985) Embryonal lactosaminoglycan. The structure of branched lactosaminoglycans with novel disialosyl (sialyl α2,9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells. J Biol Chem 260:6623–6631

    CAS  PubMed  Google Scholar 

  • Gu J, Nishikawa A, Fujii S, Gasa S, Taniguchi N (1992) Biosynthesis of blood group I and i antigens in rat tissues. Identification of a novel β-1,6-N-acetylglucosaminyltransferase. J Biol Chem 267:2994–2999

    CAS  PubMed  Google Scholar 

  • Leppanen A, Zhu Y, Maaheimo H, Helin J, Lehtonen E, Renkonen O (1998) Biosynthesis of branched polylactosaminoglycans. Embryonal carcinoma cells express midchain β1,6-N-acetylglucosaminyltransferase activity that generates branches to preformed linear backbones. J Biol Chem 273:17399–17405

    Article  CAS  PubMed  Google Scholar 

  • Lin-Chu M, Broadberry RE, Okubo Y, Tanaka M (1991) The i phenotype and congenital cataracts among Chinese in Taiwan (Letter). Transfusion 31:676–677

    Article  CAS  PubMed  Google Scholar 

  • Mattila P, Salminen H, Hirvas L, Niittymaki J, Salo H, Niemela R, Fukuda M, Renkonen O, Renkonen R (1998) The centrally acting b1,6N-acetylglucosaminyltransferase (GlcNAc to gal). Functional expression, purification, and acceptor specificity of a human enzyme involved in midchain branching of linear poly-N-acetyllactosamines. J Biol Chem 273:27633–27639

    Article  CAS  PubMed  Google Scholar 

  • Marsh WL (1961) Anti-i: a cold antibody defining the Ii relationship in human red cells. Br J Haematol 7:200–209

    Article  CAS  PubMed  Google Scholar 

  • Ogata H, Okubo Y, Akabane T (1979) Phenotype i associated with congenital cataract in Japanese. Transfusion 19:166–168

    Article  CAS  PubMed  Google Scholar 

  • Piller F, Cartron JP, Maranduba A, Veyrieres A, Leroy Y, Fournet B (1984) Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc: GlcNAc b1-3Gal(-R) b1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J Biol Chem 259:13385–13390

    CAS  PubMed  Google Scholar 

  • Romans DG et al (1980) Monogamous bivalency of IgG antibodies. I. Deficiency of branched ABHI-active oligosaccharide chains on red cells of infants causes the weak antiglobulin reactions in hemolytic disease of the newborn due to ABO incompatibility. J Immunol 124(6):2807–2811

    CAS  PubMed  Google Scholar 

  • Ropp PA, Little MR, Cheng PW (1991) Mucin biosynthesis: purification and characterization of a mucin b6 N-acetylglucosaminyltransferase. J Biol Chem 266:23863–23871

    CAS  PubMed  Google Scholar 

  • Sakamoto Y, Taguchi T, Tano Y, Ogawa T, Leppanen A, Kinnunen M, Aitio O, Parmanne P, Renkonen O, Taniguchi N (1998) Purification and characterization of UDP-GlcNAc:Galβ1–4GlcNAcβ1–3*Galβ1–4Glc(NAc)-R(GlcNAc to *Gal) β1,6N-acetylglucosaminyltransferase from hog small intestine. J Bio Chem 273:27625–27632

    Article  CAS  Google Scholar 

  • Schwientek T, Nomoto M, Levery SB, Merkx G, van Kessel AG, Bennett EP, Hollingsworth MA, Clausen H (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

    Article  CAS  PubMed  Google Scholar 

  • Ujita M, McAuliffe J, Suzuki M, Hindsgaul O, Clausen H, Fkuda MN, Fukuda M (1999) Regulation of I-branched poly-N-acetyllactosamine synthesis. – Concerted actions by i-extension enzyme, I-branching enzyme, and b1,4-galactosyltransferase I. J Biol Chem 274:9296–9304

    Article  CAS  PubMed  Google Scholar 

  • Watanabe K, Hakomori SI, Childs RA, Feizi T (1979) Characterization of a blood group I-active ganglioside. Structural requirements for I and i specificities. J Biol Chem 254:3221–3228

    CAS  PubMed  Google Scholar 

  • Wiener AS et al (1956) Type-specific cold auto-antibodies as a cause of acquired hemolytic anemia and hemolytic transfusion reactions: biologic test with bovine red cells. Ann Intern Med 44(2):221–240

    Article  CAS  PubMed  Google Scholar 

  • Yeh J-C, Ong E, Fukuda M (1999) Molecular cloning and expression of a novel b-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J Biol Chem 274:3215–3221

    Article  CAS  PubMed  Google Scholar 

  • Yu L-C, Twu Y-C, Chou M-L, Reid ME, Gray AR, Moulds JM, Chang C-Y, Lin M (2003) The molecular genetics of the human I locus and molecular background explain the partial association of the adult i phenotype with congenital cataracts. Blood 101:2081–2088

    Article  CAS  PubMed  Google Scholar 

  • Zhang H, Meng F, Wu S, Kreike B, Sethi S, Chen W, Miller FR, Wo G (2011) Engagement of I-branching β-1,6-N-acetylglucosaminyltransferase 2 in breast cancer metastasis and TGF-β signaling. Cancer Res 71:4846–4856

    Article  CAS  PubMed Central  PubMed  Google Scholar 

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Author information

Authors and Affiliations

  1. Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037-1005, USA

    Prof. Minoru Fukuda

  2. Tumor Microenvironment Program, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037-1005, USA

    Dr. Misa Suzuki-Anekoji

Authors
  1. Prof. Minoru Fukuda
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  2. Dr. Misa Suzuki-Anekoji
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Corresponding author

Correspondence to Minoru Fukuda .

Editor information

Editors and Affiliations

  1. RIKEN-Max-Planck Joint Research Center for Systems Chemical Biology, RIKEN, Wako, Saitama, Japan

    Naoyuki Taniguchi

  2. Department of Biochemistry, Kochi University, Medical School, Nankoku, Kochi, Japan

    Koichi Honke

  3. Sanford Burnham Medical Research Institute, La Jolla, California, USA

    Minoru Fukuda

  4. Research Center for Medical Glycoscience (RCMG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan

    Hisashi Narimatsu

  5. RIKEN-Max-Planck Joint Research Center for Systems Chemical Biology, RIKEN, Wako, Saitama, Japan

    Yoshiki Yamaguchi

  6. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan

    Takashi Angata

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© 2014 Springer Japan

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Fukuda, M., Suzuki-Anekoji, M. (2014). N-Acetyllactosaminide Beta-1,6-N-Acetylglucosaminyl-Transferase (GCNT2) (IGnT). In: Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (eds) Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54240-7_24

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