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Journal articles on the topic 'GlcNAc-bisecting'

Author: Grafiati

Published: 24 April 2022

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1

Ohkawa, Yuki, Yasuhiko Kizuka, Misaki Takata, Miyako Nakano, Emi Ito, Sushil K. Mishra, Haruna Akatsuka, Yoichiro Harada, and Naoyuki Taniguchi. "Peptide Sequence Mapping around Bisecting GlcNAc-Bearing N-Glycans in Mouse Brain." International Journal of Molecular Sciences 22, no. 16 (August 9, 2021): 8579. http://dx.doi.org/10.3390/ijms22168579.

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N-glycosylation is essential for many biological processes in mammals. A variety of N-glycan structures exist, of which, the formation of bisecting N-acetylglucosamine (GlcNAc) is catalyzed by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene). We previously identified various bisecting GlcNAc-modified proteins involved in Alzheimer’s disease and cancer. However, the mechanisms by which GnT-III acts on the target proteins are unknown. Here, we performed comparative glycoproteomic analyses using brain membranes of wild type (WT) and Mgat3-deficient mice. Target glycoproteins of GnT-III were enriched with E4-phytohemagglutinin (PHA) lectin, which recognizes bisecting GlcNAc, and analyzed by liquid chromatograph-mass spectrometry. We identified 32 N-glycosylation sites (Asn-Xaa-Ser/Thr, Xaa ≠ Pro) that were modified with bisecting GlcNAc. Sequence alignment of identified N-glycosylation sites that displayed bisecting GlcNAc suggested that GnT-III does not recognize a specific primary amino acid sequence. The molecular modeling of GluA1 as one of the good cell surface substrates for GnT-III in the brain, indicated that GnT-III acts on N-glycosylation sites located in a highly flexible and mobile loop of GluA1. These results suggest that the action of GnT-III is partially affected by the tertiary structure of target proteins, which can accommodate bisecting GlcNAc that generates a bulky flipped-back conformation of the modified glycans.

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2

Kizuka, Yasuhiko, Miyako Nakano, Shinobu Kitazume, Takashi Saito, Takaomi C. Saido, and Naoyuki Taniguchi. "Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stress conditions." Biochemical Journal 473, no. 1 (December 9, 2015): 21–30. http://dx.doi.org/10.1042/bj20150607.

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BACE1 is a protease essential for amyloid-β production in Alzheimer's disease. We report that bisecting GlcNAc modification on BACE1 stabilizes BACE1 protein under oxidative stress conditions. This suggests that bisecting GlcNAc is a therapeutic target for Alzheimer's disease.

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3

Kawade, Haruka, Jyoji Morise, Sushil K. Mishra, Shuta Tsujioka, Shogo Oka, and Yasuhiko Kizuka. "Tissue-Specific Regulation of HNK-1 Biosynthesis by Bisecting GlcNAc." Molecules 26, no. 17 (August 26, 2021): 5176. http://dx.doi.org/10.3390/molecules26175176.

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Human natural killer—1 (HNK-1) is a sulfated glyco-epitope regulating cell adhesion and synaptic functions. HNK-1 and its non-sulfated forms, which are specifically expressed in the brain and the kidney, respectively, are distinctly biosynthesized by two homologous glycosyltransferases: GlcAT-P in the brain and GlcAT-S in the kidney. However, it is largely unclear how the activity of these isozymes is regulated in vivo. We recently found that bisecting GlcNAc, a branching sugar in N-glycan, suppresses both GlcAT-P activity and HNK-1 expression in the brain. Here, we observed that the expression of non-sulfated HNK-1 in the kidney is unexpectedly unaltered in mutant mice lacking bisecting GlcNAc. This suggests that the biosynthesis of HNK-1 in the brain and the kidney are differentially regulated by bisecting GlcNAc. Mechanistically, in vitro activity assays demonstrated that bisecting GlcNAc inhibits the activity of GlcAT-P but not that of GlcAT-S. Furthermore, molecular dynamics simulation showed that GlcAT-P binds poorly to bisected N-glycan substrates, whereas GlcAT-S binds similarly to bisected and non-bisected N-glycans. These findings revealed the difference of the highly homologous isozymes for HNK-1 synthesis, highlighting the novel mechanism of the tissue-specific regulation of HNK-1 synthesis by bisecting GlcNAc.

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4

Kizuka, Yasuhiko, and Naoyuki Taniguchi. "Neural functions of bisecting GlcNAc." Glycoconjugate Journal 35, no. 4 (June 16, 2018): 345–51. http://dx.doi.org/10.1007/s10719-018-9829-4.

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5

Narasimhan, S., J. W. W. Lee, R. K. Cheung, E. W. Gelfand, and H. Schachter. "β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase III activity in human B and T lymphocyte lines and in tonsillar B and T lymphocytes." Biochemistry and Cell Biology 66, no. 8 (August 1, 1988): 889–900. http://dx.doi.org/10.1139/o88-101.

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β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase III (GlcNAc-T III) catalyzes the incorporation of a "bisecting" N-acetylglucosamine (GlcNAc) residue in β1—4 linkage to the β-linked mannose of the core of asparagine linked–protein bound oligosaccharides (N-glycans). The activity of GlcNAc-T III was determined in Triton X-100 extracts of four human Epstein-Barr virus (EBV)-infected B-cell lines, in four T-cell lines originally established from lymphocytes of patients with acute lymphatic leukemia, and in human tonsillar B and T lymphocytes. The four EBV-transformed B-cell lines showed appreciable GlcNAc-T III activities (ranging from 3.4 to 19.0 nmol∙h−1∙mg protein−1), while the tonsillar resting B lymphocytes had much less activity (0.68 nmol∙h−1∙mg protein−1). The four T-cell lines and the tonsillar T lymphocytes had negligible GlcNAc-T III activities (ranging from 0.02 to 0.25 nmol∙h−1∙mg protein−1). Enzyme product was identified by high resolution proton nuclear magnetic resonance spectroscopy and methylation analysis. This is the first demonstration of GlcNAc-T III activity in human lymphocytes. The presence of GlcNAc-T III in B-cell lines correlates with the reported occurrence of bisecting GlcNAc residues in the oligosaccharides of human immunoglobulins G, A1, M, and D, tonsillar class II antigens, and membrane glycoproteins from B lymphocytes. The negligible GlcNAc-T III activity of the four human T-cell lines and of tonsillar T lymphocytes agrees with the reported absence of bisected structures in N-glycans from human T lymphocyte membrane glycoproteins.

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6

Isaji, Tomoya, Jianguo Gu, Ryoko Nishiuchi, Yanyang Zhao, Motoko Takahashi, Eiji Miyoshi, Koichi Honke, Kiyotoshi Sekiguchi, and Naoyuki Taniguchi. "Introduction of Bisecting GlcNAc into Integrin α5β1Reduces Ligand Binding and Down-regulates Cell Adhesion and Cell Migration." Journal of Biological Chemistry 279, no. 19 (March 3, 2004): 19747–54. http://dx.doi.org/10.1074/jbc.m311627200.

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The enzyme β1,4-N-acetylglucosaminyltransferase III (GnT-III) catalyzes the addition of a bisecting GlcNAc residue to glycoproteins, resulting in a modulation in biological function. Our previous studies showed that the transfection of the GnT-III gene into B16 melanoma cells results in a suppression of invasive ability and lung colonization. The suppression has been postulated to be due to an increased level of E-cadherin expression on the cell surface, which in turn leads to the up-regulation of cell-cell adhesion. In this study, we report on the effects of overexpression of GnT-III on cell-matrix adhesion. The overexpression of GnT-III, but not that of an enzymatic inactive GnT-III (D323A), inhibits cell spreading and migration on fibronectin, a specific ligand for integrin α5β1, and the focal adhesion kinase phosphorylation. E4-PHA lectin blot analyses showed that the levels of bisecting GlcNAc structures on the integrin α5subunit as well as α2and α3subunits immunoprecipitated from GnT-III transfectants were substantially increased. In addition, the affinity of the binding of integrin α5β1to fibronectin was significantly reduced by the introduction of the bisecting GlcNAc, to the α5subunit. These findings suggest that the modification ofN-glycan of integrin by GnT-III inhibits its ligand binding ability, subsequently leading to the down-regulation of integrin-mediated signaling.

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7

Hanashima, Shinya, Akitsugu Suga, and Yoshiki Yamaguchi. "Bisecting GlcNAc restricts conformations of branches in model N -glycans with GlcNAc termini." Carbohydrate Research 456 (February 2018): 53–60. http://dx.doi.org/10.1016/j.carres.2017.12.002.

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8

Fukuta, Kazuhiro, Reiko Abe, Tomoko Yokomatsu, Fumio Omae, Mineko Asanagi, and Tadashi Makino. "Control of Bisecting GlcNAc Addition toN-Linked Sugar Chains." Journal of Biological Chemistry 275, no. 31 (May 17, 2000): 23456–61. http://dx.doi.org/10.1074/jbc.m002693200.

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9

Nakano, Miyako, Sushil K. Mishra, Yuko Tokoro, Keiko Sato, Kazuki Nakajima, Yoshiki Yamaguchi, Naoyuki Taniguchi, and Yasuhiko Kizuka. "Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan." Molecular & Cellular Proteomics 18, no. 10 (August 2, 2019): 2044–57. http://dx.doi.org/10.1074/mcp.ra119.001534.

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Glycoproteins are decorated with complex glycans for protein functions. However, regulation mechanisms of complex glycan biosynthesis are largely unclear. Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1. Expression of these epitopes in N-glycan was elevated in mice lacking the biosynthetic enzyme of bisecting GlcNAc, GnT-III, and was conversely suppressed by GnT-III overexpression in cells. Many glycosyltransferases for N-glycan terminals were revealed to prefer a nonbisected N-glycan as a substrate to its bisected counterpart, whereas no up-regulation of their mRNAs was found. This indicates that the elevated expression of the terminal N-glycan epitopes in GnT-III-deficient mice is attributed to the substrate specificity of the biosynthetic enzymes. Molecular dynamics simulations further confirmed that nonbisected glycans were preferentially accepted by those glycosyltransferases. These findings unveil a new regulation mechanism of protein N-glycosylation.

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10

Gao, Cong-xiao, Eiji Miyoshi, Naofumi Uozumi, Rina Takamiya, Xiangchun Wang, Katsuhisa Noda, Jianguo Gu, Koichi Honke, Yoshinao Wada, and Naoyuki Taniguchi. "Bisecting GlcNAc mediates the binding of annexin V to Hsp47." Glycobiology 15, no. 11 (July 6, 2005): 1067–75. http://dx.doi.org/10.1093/glycob/cwj005.

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11

Miwa, Hazuki E., Yinghui Song, Richard Alvarez, Richard D. Cummings, and Pamela Stanley. "The bisecting GlcNAc in cell growth control and tumor progression." Glycoconjugate Journal 29, no. 8-9 (April 4, 2012): 609–18. http://dx.doi.org/10.1007/s10719-012-9373-6.

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12

Eller, Steffen, Ralf Schuberth, Gislinde Gundel, Joachim Seifert, and Carlo Unverzagt. "Synthesis of Pentaantennary N-Glycans with Bisecting GlcNAc and Core Fucose." Angewandte Chemie International Edition 46, no. 22 (May 25, 2007): 4173–75. http://dx.doi.org/10.1002/anie.200604788.

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13

Manabe, Yoshiyuki, Hiroki Shomura, Naoya Minamoto, Masahiro Nagasaki, Yohei Takakura, Katsunori Tanaka, Alba Silipo, Antonio Molinaro, and Koichi Fukase. "Convergent Synthesis of a Bisecting N -Acetylglucosamine (GlcNAc)-Containing N-Glycan." Chemistry - An Asian Journal 13, no. 12 (May 25, 2018): 1544–51. http://dx.doi.org/10.1002/asia.201800367.

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14

Eller, Steffen, Ralf Schuberth, Gislinde Gundel, Joachim Seifert, and Carlo Unverzagt. "Synthese von pentaantennären N-Glycanen mit Bisecting-GlcNAc und Core-Fucose." Angewandte Chemie 119, no. 22 (May 25, 2007): 4251–53. http://dx.doi.org/10.1002/ange.200604788.

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15

Yang, Weizhun, Sherif Ramadan, Jared Orwenyo, Tayeb Kakeshpour, Thomas Diaz, Yigitcan Eken, Miloslav Sanda, James E. Jackson, Angela K. Wilson, and Xuefei Huang. "Chemoenzymatic synthesis of glycopeptides bearing rare N-glycan sequences with or without bisecting GlcNAc." Chemical Science 9, no. 43 (2018): 8194–206. http://dx.doi.org/10.1039/c8sc02457j.

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16

NAKAGAWA, Manabu, Hiromasa TOJO, and Shigeru FUJII. "A Glycan of Ψ-Factor fromDictyostelium discoideumContains a Bisecting-GlcNAc, an Intersecting-GlcNAc, and a Core α-1,6-Fucose." Bioscience, Biotechnology, and Biochemistry 75, no. 10 (October 23, 2011): 1964–70. http://dx.doi.org/10.1271/bbb.110369.

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17

Kariya, Yoshinobu, Chihiro Kawamura, Toshiki Tabei, and Jianguo Gu. "Bisecting GlcNAc Residues on Laminin-332 Down-regulate Galectin-3-dependent Keratinocyte Motility." Journal of Biological Chemistry 285, no. 5 (November 25, 2009): 3330–40. http://dx.doi.org/10.1074/jbc.m109.038836.

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18

Ruhaak, L. Renee, Hae-Won Uh, Marian Beekman, Carolien A. M. Koeleman, Cornelis H. Hokke, Rudi G. J. Westendorp, Manfred Wuhrer, Jeanine J. Houwing-Duistermaat, P. Eline Slagboom, and André M. Deelder. "Decreased Levels of Bisecting GlcNAc Glycoforms of IgG Are Associated with Human Longevity." PLoS ONE 5, no. 9 (September 7, 2010): e12566. http://dx.doi.org/10.1371/journal.pone.0012566.

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19

Weiss, Michael, Dimitri Ott, Theodoros Karagiannis, Markus Weishaupt, Mathäus Niemietz, Steffen Eller, Marie Lott, et al. "Efficient Chemoenzymatic Synthesis of N‐Glycans with a β1,4‐Galactosylated Bisecting GlcNAc Motif." ChemBioChem 21, no. 22 (August 19, 2020): 3212–15. http://dx.doi.org/10.1002/cbic.202000268.

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20

Zhang, Min, Meirong Wang, Rufei Gao, Xueqing Liu, Xuemei Chen, Yanqing Geng, Yubin Ding, Yingxiong Wang, and Junlin He. "Altered β1,6-GlcNAc and bisecting GlcNAc-branched N-glycan on integrin β1 are associated with early spontaneous miscarriage in humans." Human Reproduction 30, no. 9 (June 24, 2015): 2064–75. http://dx.doi.org/10.1093/humrep/dev153.

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21

Wang, Meng, Feng Zheng, Ting Wang, Yong-Mei Lyu, Matthew Alteen, Zhi-Peng Cai, Zhong-Li Cui, Li Liu, and Josef Voglmeir. "Characterization of Stackebrandtia nassauensis GH 20 Beta-Hexosaminidase, a Versatile Biocatalyst for Chitobiose Degradation." International Journal of Molecular Sciences 20, no. 5 (March 12, 2019): 1243. http://dx.doi.org/10.3390/ijms20051243.

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An unstudied β-N-acetylhexosaminidase (SnHex) from the soil bacterium Stackebrandtia nassauensis was successfully cloned and subsequently expressed as a soluble protein in Escherichia coli. Activity tests and the biochemical characterization of the purified protein revealed an optimum pH of 6.0 and a robust thermal stability at 50 °C within 24 h. The addition of urea (1 M) or sodium dodecyl sulfate (1% w/v) reduced the activity of the enzyme by 44% and 58%, respectively, whereas the addition of divalent metal ions had no effect on the enzymatic activity. PUGNAc (O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate) strongly inhibited the enzyme in sub-micromolar concentrations. The β-N-acetylhexosaminidase was able to hydrolyze β1,2-linked, β1,3-linked, β1,4-linked, and β1,6-linked GlcNAc residues from the non-reducing end of various tested glycan standards, including bisecting GlcNAc from one of the tested hybrid-type N-glycan substrates. A mutational study revealed that the amino acids D306 and E307 bear the catalytically relevant side acid/base side chains. When coupled with a chitinase, the β-N-acetylhexosaminidase was able to generate GlcNAc directly from colloidal chitin, which showed the potential of this enzyme for biotechnological applications.

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22

Zhao, Yanyang, Takatoshi Nakagawa, Satsuki Itoh, Kei-ichiro Inamori, Tomoya Isaji, Yoshinobu Kariya, Akihiro Kondo, et al. "N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on α3β1 Integrin-mediated Cell Migration." Journal of Biological Chemistry 281, no. 43 (August 28, 2006): 32122–30. http://dx.doi.org/10.1074/jbc.m607274200.

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N-Acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of β1,6-GlcNAc branching of N-glycans, which contributes to metastasis. N-Acetylglucosaminyltransferase III (GnT-III) catalyzes the formation of a bisecting GlcNAc structure in N-glycans, resulting in the suppression of metastasis. It has long been hypothesized that the suppression of GnT-V product formation by the action of GnT-III would also exist in vivo, which will consequently lead to the inhibition of biological functions of GnT-V. To test this, we draw a comparison among MKN45 cells, which were transfected with GnT-III, GnT-V, or both, respectively. We found that α3β1 integrin-mediated cell migration on laminin 5 was greatly enhanced in the case of GnT-V transfectant. This enhanced cell migration was significantly blocked after the introduction of GnT-III. Consistently, an increase in bisected GlcNAc but a decrease in β1,6-GlcNAc-branched N-glycans on integrin α3 subunit was observed in the double transfectants of GnT-III and GnT-V. Conversely, GnT-III knockdown resulted in increased migration on laminin 5, concomitant with an increase in β1,6-GlcNAc-branched N-glycans on the α3 subunit in CHP134 cells, a human neuroblastoma cell line. Therefore, in this study, the priority of GnT-III for the modification of the α3 subunit may be an explanation for why GnT-III inhibits GnT-V-induced cell migration. Taken together, our results demonstrate for the first time that GnT-III and GnT-V can competitively modify the same target glycoprotein and furthermore positively or negatively regulate its biological functions.

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23

Kohler, Reto S., Merrina Anugraham, Mónica Núñez López, Christina Xiao, Andreas Schoetzau, Timm Hettich, Goetz Schlotterbeck, André Fedier, Francis Jacob, and Viola Heinzelmann-Schwarz. "Epigenetic activation of MGAT3 and corresponding bisecting GlcNAc shortens the survival of cancer patients." Oncotarget 7, no. 32 (July 12, 2016): 51674–86. http://dx.doi.org/10.18632/oncotarget.10543.

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24

Li, Wei, Motoko Takahashi, Yukinao Shibukawa, Shunichi Yokoe, Jianguo Gu, Eiji Miyoshi, Koichi Honke, Yoshitaka Ikeda, and Naoyuki Taniguchi. "Introduction of bisecting GlcNAc in N-glycans of adenylyl cyclase III enhances its activity." Glycobiology 17, no. 6 (February 26, 2007): 655–62. http://dx.doi.org/10.1093/glycob/cwm022.

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25

Akasaka-Manya, K., H. Manya, Y. Sakurai, B. S. Wojczyk, Y. Kozutsumi, Y. Saito, N. Taniguchi, S. Murayama, S. L. Spitalnik, and T. Endo. "Protective effect of N-glycan bisecting GlcNAc residues on -amyloid production in Alzheimer's disease." Glycobiology 20, no. 1 (September 23, 2009): 99–106. http://dx.doi.org/10.1093/glycob/cwp152.

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26

Luber, Thomas, Mathäus Niemietz, Theodoros Karagiannis, Manuel Mönnich, Dimitri Ott, Lukas Perkams, Janika Walcher, et al. "A Single Route to Mammalian N-Glycans Substituted with Core Fucose and Bisecting GlcNAc." Angewandte Chemie 130, no. 44 (October 11, 2018): 14751–57. http://dx.doi.org/10.1002/ange.201807742.

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27

Luber, Thomas, Mathäus Niemietz, Theodoros Karagiannis, Manuel Mönnich, Dimitri Ott, Lukas Perkams, Janika Walcher, et al. "A Single Route to Mammalian N-Glycans Substituted with Core Fucose and Bisecting GlcNAc." Angewandte Chemie International Edition 57, no. 44 (October 11, 2018): 14543–49. http://dx.doi.org/10.1002/anie.201807742.

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28

Poola, I., and S. Narasimhan. "Interaction of asparagine-linked oligosaccharides with an immobilized rice (Oryza sativa) lectin column." Biochemical Journal 250, no. 1 (February 15, 1988): 117–24. http://dx.doi.org/10.1042/bj2500117.

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The carbohydrate-binding specificity of rice (Oryza sativa) lectin was investigated by testing the ability of radioactively labelled glycopeptides and oligosaccharides to bind to a rice lectin-Sepharose 4B column. Rice lectin binds asparagine-linked oligosaccharides through the core NN′-diacetylchitobiose moiety. Whereas beta 1-4-mannose enhances the binding strength only to a small extent, alpha 1-3-linked core mannose increases it considerably. A core alpha 1-6-linked mannose residue has a slightly inhibitory effect. Binding is not affected when one or both of the alpha-mannose residues are substituted with mannose at C-2, C-3 and C-6 or with N-acetylglucosamine (GlcNAc) at C-2 positions. The presence of an alpha 1-6-fucose residue attached to the asparagine-linked GlcNAc also does not affect the binding. The binding of complex biantennary glycopeptides is not altered by the presence of one or two galactose residues in the non-reducing terminus, but the presence of one or two sialic acid residues decreases the binding capacity. A bisecting beta 1-4-linked GlcNAc attached to beta-linked mannose residue enhances the binding of sialo, asialo and asialoagalacto complex biantennary-type glycopeptides. Bisected hybrid-type glycopeptides bind very tightly to a rice lectin-Sepharose 4B column: Substitution of alpha 1-3-mannose residue at C-2 and C-4 with GlcNAc completely inhibits the binding of both bisected and non-bisected complex asparagine-linked glycopeptides. O-Glycosidically linked oligosaccharides containing GlcNAc bind very weakly to a rice lectin column. The applicability of immobilized rice lectin columns in the fractionation of asparagine-linked oligosaccharides is discussed.

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29

Eller, Steffen, Claudia Raps, Mathäus Niemietz, and Carlo Unverzagt. "Convenient introduction of a bisecting GlcNAc residue into multiantennary N-glycans as the ultimate residue." Tetrahedron Letters 51, no. 19 (May 2010): 2648–51. http://dx.doi.org/10.1016/j.tetlet.2010.03.031.

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30

Song, Yinghui, Jason A. Aglipay, Joshua D. Bernstein, Sumanta Goswami, and Pamela Stanley. "The Bisecting GlcNAc on N-Glycans Inhibits Growth Factor Signaling and Retards Mammary Tumor Progression." Cancer Research 70, no. 8 (April 14, 2010): 3361–71. http://dx.doi.org/10.1158/0008-5472.can-09-2719.

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31

Helm, Johannes, Lena Hirtler, and Friedrich Altmann. "Towards Mapping of the Human Brain N-Glycome with Standardized Graphitic Carbon Chromatography." Biomolecules 12, no. 1 (January 6, 2022): 85. http://dx.doi.org/10.3390/biom12010085.

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The brain N-glycome is known to be crucial for many biological functions, including its involvement in neuronal diseases. Although large structural studies of brain N-glycans were recently carried out, a comprehensive isomer-specific structural analysis has still not been achieved, as indicated by the recent discovery of novel structures with galactosylated bisecting GlcNAc. Here, we present a detailed, isomer-specific analysis of the human brain N-glycome based on standardized porous graphitic carbon (PGC)-LC-MS/MS. To achieve this goal, we biosynthesized glycans with substitutions typically occurring in the brain N-glycome and acquired their normalized retention times. Comparison of these values with the standardized retention times of neutral and desialylated N-glycan fractions of the human brain led to unambiguous isomer specific assignment of most major peaks. Profound differences in the glycan structures between naturally neutral and desialylated glycans were found. The neutral and sialylated N-glycans derive from diverging biosynthetic pathways and are biosynthetically finished end products, rather than just partially processed intermediates. The focus on structural glycomics defined the structure of human brain N-glycans, amongst these are HNK-1 containing glycans, a bisecting sialyl-lactose and structures with fucose and N-acetylgalactosamine on the same arm, the so-called LDNF epitope often associated with parasitic worms.

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32

Sasai, Ken, Yoshitaka Ikeda, Hironobu Eguchi, Takeo Tsuda, Koichi Honke, and Naoyuki Taniguchi. "The action ofN-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step." FEBS Letters 522, no. 1-3 (June 9, 2002): 151–55. http://dx.doi.org/10.1016/s0014-5793(02)02916-2.

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33

YOSHIMURA, Masafumi, Yoshito IHARA, Tetsuo NISHIURA, Yu OKAJIMA, Megumu OGAWA, Hitoshi YOSHIDA, Misao SUZUKI, et al. "Bisecting GlcNAc structure is implicated in suppression of stroma-dependent haemopoiesis in transgenic mice expressing N-acetylglucosaminyltransferase III." Biochemical Journal 331, no. 3 (May 1, 1998): 733–42. http://dx.doi.org/10.1042/bj3310733.

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Several sugar structures have been reported to be necessary for haemopoiesis. We analysed the haematological phenotypes of transgenic mice expressing β-1,4 N-acetylglucosaminyltransferase III (GnT-III), which forms bisecting N-acetylglucosamine on asparagine-linked oligosaccharides. In the transgenic mice, the GnT-III activity was elevated in bone marrow, spleen and peripheral blood and in isolated mononuclear cells from these tissues, whereas no activity was found in these tissues of wild-type mice. Stromal cells after long-term cultures of transgenic-derived bone marrow and spleen cells also showed elevated GnT-III activity, compared with an undetectable activity in wild-type stromal cells. As judged by HPLC analysis, lectin blotting and lectin cytotoxicity assay, bisecting GlcNAc residues were increased on both blood cells and stromal cells from bone marrow and spleen in transgenic mice. The transgenic mice displayed spleen atrophy, hypocellular bone marrow and pancytopenia. Bone marrow cells and spleen cells from transgenic mice produced fewer haemopoietic colonies. After lethal irradiation followed by bone marrow transplantation, transgenic recipient mice showed pancytopenia compared with wild-type recipient mice. Bone marrow cells from transgenic donors gave haematological reconstitution at the same level as wild-type donor cells. In addition, non-adherent cell production was decreased in long-term bone marrow cell cultures of transgenic mice. Collectively these results indicate that the stroma-supported haemopoiesis is compromised in transgenic mice expressing GnT-III, providing the first demonstration that the N-glycans have some significant roles in stroma-dependent haemopoiesis.

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Chatterjee, Sayantani, Rebeca Kawahara, Harry C. Tjondro, David R. Shaw, Marni A. Nenke, David J. Torpy, and Morten Thaysen-Andersen. "Serum N-Glycomics Stratifies Bacteremic Patients Infected with Different Pathogens." Journal of Clinical Medicine 10, no. 3 (February 1, 2021): 516. http://dx.doi.org/10.3390/jcm10030516.

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Bacteremia—i.e., the presence of pathogens in the blood stream—is associated with long-term morbidity and is a potential precursor condition to life-threatening sepsis. Timely detection of bacteremia is therefore critical to reduce patient mortality, but existing methods lack precision, speed, and sensitivity to effectively stratify bacteremic patients. Herein, we tested the potential of quantitative serum N-glycomics performed using porous graphitized carbon liquid chromatography tandem mass spectrometry to stratify bacteremic patients infected with Escherichia coli (n = 11), Staphylococcus aureus (n = 11), Pseudomonas aeruginosa (n = 5), and Streptococcus viridans (n = 5) from healthy donors (n = 39). In total, 62 N-glycan isomers spanning 41 glycan compositions primarily comprising complex-type core fucosylated, bisecting N-acetylglucosamine (GlcNAc), and α2,3-/α2,6-sialylated structures were profiled across all samples using label-free quantitation. Excitingly, unsupervised hierarchical clustering and principal component analysis of the serum N-glycome data accurately separated the patient groups. P. aeruginosa-infected patients displayed prominent N-glycome aberrations involving elevated levels of fucosylation and bisecting GlcNAcylation and reduced sialylation relative to other bacteremic patients. Notably, receiver operating characteristic analyses demonstrated that a single N-glycan isomer could effectively stratify each of the four bacteremic patient groups from the healthy donors (area under the curve 0.93–1.00). Thus, the serum N-glycome represents a new hitherto unexplored class of potential diagnostic markers for bloodstream infections.

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Stanley, P. "Molecular analysis of three gain-of-function CHO mutants that add the bisecting GlcNAc to N-glycans." Glycobiology 15, no. 1 (August 25, 2004): 43–53. http://dx.doi.org/10.1093/glycob/cwh136.

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Reinke, Stefan O., Marion Bayer, Markus Berger, Stephan Hinderlich, and Véronique Blanchard. "The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern." Biological Chemistry 393, no. 8 (August 1, 2012): 731–47. http://dx.doi.org/10.1515/hsz-2012-0195.

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Abstract Human cell lines are often different in their features and present variations in the glycosylation patterns of cell membrane proteins. Protein glycosylation is the most common posttranslational modification and plays a particular role in functionality and bioactivity. The key approach of this study is the comparative analysis of five hematopoietic cell lines for their N-glycosylation pattern. The N-glycans of membrane proteins were elucidated by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and MALDI-TOF/TOF-MS analyses. Furthermore, the expression of a set of glycosyltransferases was determined via RT-PCR. The B-lymphoma BJA-B and promyelocytic HL-60 cell lines distinguish in levels and linkages of glycan-bound sialic acids. Furthermore, subclones of BJA-B and HL-60 cells, which completely lack UDP-N-acetylglucosamine 2-ēpimerase/N-acetylmannosamine kinase (GNE), the key enzyme of sialic acid biosynthesis, contained almost no sialylated N-glycans. Compared to wild-type cells, the GNE-deficient cells pres\xadented a similar cell surface N-glycosylation pattern in terms of antennarity and fucosylation. The Jurkat T-cell line revealed only partially sialylated N-glycans. Additionally, the different hematopoietic cell lines vary in their level of bisecting GlcNAcylation and antennary fucosylation with the quantities of bisecting N-acetylglucosamine (GlcNAc) and core fucose coinciding with the expression of GnT-III and FucT-VIII. Of note is the occurrence of N-acetyllactosamine (LacNAc) extensions on tetraantennary structures in GNE-deficient cell lines.

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Zappe, Andreas, Julia Rosenlöcher, Guido Kohla, Stephan Hinderlich, and Maria Kristina Parr. "Purification and Characterization of Antibodies Directed against the α-Gal Epitope." BioChem 1, no. 2 (August 2, 2021): 81–97. http://dx.doi.org/10.3390/biochem1020008.

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The α-Gal epitope is an immunogen trisaccharide structure consisting of N-acetylglucosamine (GlcNAc)β1,4-galactose (Gal)α1,3-Gal. It is presented as part of complex-type glycans on glycoproteins or glycolipids on cell surfaces of non-primate mammalians. About 1% of all antibodies in human sera are specific toward α1,3-Gal and are therefore named as anti-α-Gal antibodies. This work comprises the purification and characterization of anti-α-Gal antibodies from human immunoglobulin G (IgG). A synthetically manufactured α Gal epitope affinity resin was used to enrich anti-α-Gal antibodies. Selectivity experiments with purified antibodies were carried out using enzyme-linked immunosorbent assays (ELISA), Western blotting, and erythrocyte agglutination. Furthermore, binding affinities toward α-Gal were determined by surface plasmon resonance (SPR) and the IgG distribution of anti α Gal antibodies (83% IgG2, 14% IgG1, 2% IgG3, 1% IgG4) was calculated applying ELISA and immunodiffusion. A range of isoelectric points from pH 6 to pH 8 was observed in 2D gel electrophoresis. Glycan profiling of anti α Gal antibodies revealed complex biantennary structures with high fucosylation grades (86%). Additionally, low amounts of bisecting GlcNAc (15%) and sialic acids (13%) were detected. The purification of anti-α-Gal antibodies from human IgG was successful, and their use as detection antibodies for α Gal-containing structures was evaluated.

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André, Sabine, Tibor Kožár, Ralf Schuberth, Carlo Unverzagt, Shuji Kojima, and Hans-Joachim Gabius. "Substitutions in theN-Glycan Core as Regulators of Biorecognition: The Case of Core-Fucose and Bisecting GlcNAc Moieties†." Biochemistry 46, no. 23 (June 2007): 6984–95. http://dx.doi.org/10.1021/bi7000467.

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Nishima, Wataru, Naoyuki Miyashita, Yoshiki Yamaguchi, Yuji Sugita, and Suyong Re. "Effect of Bisecting GlcNAc and Core Fucosylation on Conformational Properties of Biantennary Complex-Type N-Glycans in Solution." Journal of Physical Chemistry B 116, no. 29 (May 2, 2012): 8504–12. http://dx.doi.org/10.1021/jp212550z.

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40

Sultan, Ahmed S., Eiji Miyoshi, Yoshito Ihara, Atsushi Nishikawa, Yutaka Tsukada, and Naoyuki Taniguchi. "Bisecting GlcNAc Structures Act as Negative Sorting Signals for Cell Surface Glycoproteins in Forskolin-treated Rat Hepatoma Cells." Journal of Biological Chemistry 272, no. 5 (January 31, 1997): 2866–72. http://dx.doi.org/10.1074/jbc.272.5.2866.

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Gu, Jianguo, Yuya Sato, Yoshinobu Kariya, Tomoya Isaji, Naoyuki Taniguchi, and Tomohiko Fukuda. "A Mutual Regulation between Cell−Cell Adhesion and N-Glycosylation: Implication of the Bisecting GlcNAc for Biological Functions." Journal of Proteome Research 8, no. 2 (February 6, 2009): 431–35. http://dx.doi.org/10.1021/pr800674g.

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42

Takahashi, Motoko, Yoshio Kuroki, Kazuaki Ohtsubo, and Naoyuki Taniguchi. "Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins." Carbohydrate Research 344, no. 12 (August 2009): 1387–90. http://dx.doi.org/10.1016/j.carres.2009.04.031.

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43

Oda-Sakurai, Risako, Hiroshi Yoshitake, Yoshiki Miura, Saiko Kazuno, Takashi Ueno, Akiko Hasegawa, Kenji Yamatoya, et al. "NUP62: the target of an anti-sperm auto-monoclonal antibody during testicular development." Reproduction 158, no. 6 (December 2019): 503–16. http://dx.doi.org/10.1530/rep-19-0333.

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Ts4, an autosperm-monoclonal antibody (mAb), reacts with a specific oligosaccharide (OS) of glycoproteins containing bisecting N-acetylglucosamine residues. Ts4 reactivity was observed against epididymal spermatozoa, testicular germ cells, and the early embryo, but not against major organs in adult mice. In mature testis, Ts4 exhibits immunoreactivity with a germ cell-specific glycoprotein, TEX101, whereas the mAb immunoreacts with alpha-N-acetylglucosaminidase in the acrosomal region of cauda epididymal spermatozoa. Thus, Ts4 seems to react against different molecules throughout spermiogenesis via binding to its OS epitope. Since the Ts4-epitope OS is observed only in reproduction-related regions, the Ts4-reactive OS may play a role in the reproductive process. The aim of this study is to investigate the characteristics of the Ts4-reactive molecule(s) during testicular development. Ts4 reactivity was observed in testes from the prenatal period; however, its distribution changed according to the stage of maturation and was identical to that of the adult testes after 29-day-postpartum (dpp). Ts4 immunoreactivity was detected against a protein with 63 kDa in testis from 1 to 29 dpp. In contrast, Ts4 showed reactivity against some other glycoproteins after 29 dpp, including TEX101 at the 5-week-old stage and onward. To identify the Ts4-reactive 63 kDa molecule, we identified NUP62 as the target of Ts4 in 22 dpp testis using liquid chromatography-tandem mass spectrometry analysis. Because NUP62 has been known to play active roles in a variety of cellular processes including mitosis and cell migration, the bisecting GlcNAc recognized by Ts4 on NUP62 may play a role in regulating the early development of germ cells in male gonadal organs.

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de-Freitas-Junior, Julio Cesar Madureira, Sandra Carvalho, Ana M. Dias, Patrícia Oliveira, Joana Cabral, Raquel Seruca, Carla Oliveira, José Andrés Morgado-Díaz, Celso A. Reis, and Salomé S. Pinho. "Insulin/IGF-I Signaling Pathways Enhances Tumor Cell Invasion through Bisecting GlcNAc N-glycans Modulation. An Interplay with E-Cadherin." PLoS ONE 8, no. 11 (November 25, 2013): e81579. http://dx.doi.org/10.1371/journal.pone.0081579.

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45

Rouwendal, Gerard J. A., Manfred Wuhrer, Dion E. A. Florack, Carolien A. M. Koeleman, André M. Deelder, Hans Bakker, Geert M. Stoopen, et al. "Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III." Glycobiology 17, no. 3 (December 19, 2006): 334–44. http://dx.doi.org/10.1093/glycob/cwl078.

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46

Oswald, Douglas M., Mark B. Jones, and Brian A. Cobb. "Modulation of hepatocyte sialylation drives spontaneous fatty liver disease and inflammation." Glycobiology 30, no. 5 (November 29, 2019): 346–59. http://dx.doi.org/10.1093/glycob/cwz096.

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Abstract Circulatory protein glycosylation is a biomarker of multiple disease and inflammatory states and has been applied in the clinic for liver dysfunction, heart disease and diabetes. With the notable exception of antibodies, the liver produces most of the circulatory glycoproteins, including the acute phase proteins released as a function of the inflammatory response. Among these proteins is β-galactoside α2,6-sialyltransferase (ST6Gal1), an enzyme required for α2,6-linked sialylation of glycoproteins. Here, we describe a hepatocyte-specific conditional knockout of ST6Gal1 (H-cKO) using albumin promoter-driven Cre-lox recombination. We confirm the loss of circulatory glycoprotein α2,6 sialylation and note no obvious dysfunction or pathology in young H-cKO mice, yet these mice show robust changes in plasma glycoprotein fucosylation, branching and the abundance of bisecting GlcNAc and marked changes in a number of metabolic pathways. As H-cKO mice aged, they spontaneously developed fatty liver disease characterized by the buildup of fat droplets in the liver, inflammatory cytokine production and a shift in liver leukocyte phenotype away from anti-inflammatory Kupffer cells and towards proinflammatory M1 macrophages. These findings connect hepatocyte and circulatory glycoprotein sialylation to the regulation of metabolism and inflammation, potentially identifying the glycome as a new target for liver-driven disease.

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Singh, Sunny S., Ralph Heijmans, Claudia K. E. Meulen, Aloysius G. Lieverse, Olga Gornik, Eric J. G. Sijbrands, Gordan Lauc, and Mandy van Hoek. "Association of the IgG N-glycome with the course of kidney function in type 2 diabetes." BMJ Open Diabetes Research & Care 8, no. 1 (April 2020): e001026. http://dx.doi.org/10.1136/bmjdrc-2019-001026.

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IntroductionInflammatory processes are thought to be involved in kidney function decline in individuals with type 2 diabetes. Glycosylation of immunoglobulin G (IgG) is an important post-translation process affecting the inflammatory potential of IgG. We investigated the prospective relationship between IgG N-glycosylation patterns and kidney function in type 2 diabetes.Research design and methodsIn the DiaGene study, an all-lines-of-care case–control study (n=1886) with mean prospective follow-up of 7.0 years, the association between 58 IgG N-glycan profiles and estimated glomerular filtration rate (eGFR) and albumin-to-creatinine ratio (ACR) per year and during total follow-up was analyzed. Models were adjusted for clinical variables and multiple comparisons.ResultsEleven traits were significantly associated with eGFR change per year. Bisecting GlcNAc in fucosylated and fucosylated disialylated structures and monosialylation of fucosylated digalactosylated structures were associated with a faster decrease of eGFR. Fucosylation of neutral and monogalactosylated structures was associated with less eGFR decline per year. No significant associations between IgG glycans and ACR were found.ConclusionsIn type 2 diabetes, we found IgG N-glycosylation patterns associated with a faster decline of kidney function, reflecting a pro-inflammatory state of IgG. eGFR, but not ACR, was associated with IgG glycans, which suggests these associations may represent renal macroangiopathy rather than microvascular disease.

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Wang, Yifei, Qingxiang Li, Lixuan Niu, Le Xu, Yuxing Guo, Lin Wang, and Chuanbin Guo. "Suppression of G6PD induces the expression and bisecting GlcNAc-branched N-glycosylation of E-Cadherin to block epithelial-mesenchymal transition and lymphatic metastasis." British Journal of Cancer 123, no. 8 (July 28, 2020): 1315–25. http://dx.doi.org/10.1038/s41416-020-1007-3.

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49

Higashi, Mikito, Takeshi Yoshimura, Noriyoshi Usui, Yuichiro Kano, Akihiro Deguchi, Kazuhiro Tanabe, Youichi Uchimura, et al. "A Potential Serum N-glycan Biomarker for Hepatitis C Virus-Related Early-Stage Hepatocellular Carcinoma with Liver Cirrhosis." International Journal of Molecular Sciences 21, no. 23 (November 24, 2020): 8913. http://dx.doi.org/10.3390/ijms21238913.

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Detection of early-stage hepatocellular carcinoma (HCC) is beneficial for prolonging patient survival. However, the serum markers currently used show limited ability to identify early-stage HCC. In this study, we explored human serum N-glycans as sensitive markers to diagnose HCC in patients with cirrhosis. Using a simplified fluorescence-labeled N-glycan preparation method, we examined non-sialylated and sialylated N-glycan profiles from 71 healthy controls and 111 patients with hepatitis and/or liver cirrhosis (LC) with or without HCC. We found that the level of serum N-glycan A2G1(6)FB, a biantennary N-glycan containing core fucose and bisecting GlcNAc residues, was significantly higher in hepatitis C virus (HCV)-infected cirrhotic patients with HCC than in those without HCC. In addition, A2G1(6)FB was detectable in HCV-infected patients with early-stage HCC and could be a more accurate marker than alpha-fetoprotein (AFP) or protein induced by vitamin K absence or antagonists-II (PIVKA-II). Moreover, there was no apparent correlation between the levels of A2G1(6)FB and those of AFP or PIVKA-II. Thus, simultaneous use of A2G1(6)FB and traditional biomarkers could improve the accuracy of HCC diagnosis in HCV-infected patients with LC, suggesting that A2G1(6)FB may be a reliable biomarker for early-stage HCC patients.

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Canis, Kevin, Thomas A. J. McKinnon, Agata Nowak, Stuart M. Haslam, Maria Panico, Howard R. Morris, Mike A. Laffan, and Anne Dell. "Mapping the N-glycome of human von Willebrand factor." Biochemical Journal 447, no. 2 (September 26, 2012): 217–28. http://dx.doi.org/10.1042/bj20120810.

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vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury. There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function. Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood. The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues. We estimate that some 300 N-glycan structures are carried by human vWF. Glycoproteomics analyses mapped ten of the consensus sites known to carry N-glycans. Glycan populations were found to be distinct, although many structural features were shared across all sites. Notably, the H antigen is not restricted to particular N-glycosylation sites. Also, the Asn2635 site, previously designated as unoccupied, was found to be highly glycosylated. The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.

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