Log in

Relevant bibliographies by topics / GlcNAc-bisecting

Contents

Journal articles
Book chapters
Conference papers

Academic literature on the topic 'GlcNAc-bisecting'

Author: Grafiati

Published: 24 April 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'GlcNAc-bisecting.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "GlcNAc-bisecting"

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Book chapters on the topic "GlcNAc-bisecting"

1

Isaji, Tomoya, Yoshinobu Kariya, Qingsong Xu, Tomohiko Fukuda, Naoyuki Taniguchi, and Jianguo Gu. "Functional Roles of the Bisecting GlcNAc in Integrin-Mediated Cell Adhesion." In Methods in Enzymology, 445–59. Elsevier, 2010. http://dx.doi.org/10.1016/s0076-6879(10)80019-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "GlcNAc-bisecting"

1

Jacob, Francis, Merrina Anugraham, Reto Kohler, Sheri Nixdorf, Arun Vijay Everest-Dass, André Fedier, Viola Heinzelmann-Schwarz, and Nicolle H. Packer. "Abstract POSTER-BIOL-1323: Elevated MGAT3 expression in ovarian cancer cells is epigenetically regulated and correlates with expression of bisecting GlcNAc-modified proteins." In Abstracts: 10th Biennial Ovarian Cancer Research Symposium; September 8-9, 2014; Seattle, WA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3265.ovcasymp14-poster-biol-1323.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!