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Journal articles on the topic 'O-fucosylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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1

Holdener, Bernadette C., and Robert S. Haltiwanger. "Protein O-fucosylation: structure and function." Current Opinion in Structural Biology 56 (June 2019): 78–86. http://dx.doi.org/10.1016/j.sbi.2018.12.005.

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2

Ricketts, Lindsay M., Malgosia Dlugosz, Kelvin B. Luther, Robert S. Haltiwanger, and Elaine M. Majerus. "O-Fucosylation Is Required for ADAMTS13 Secretion." Journal of Biological Chemistry 282, no. 23 (2007): 17014–23. http://dx.doi.org/10.1074/jbc.m700317200.

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3

Verbij, Fabian C., Eva Stokhuijzen, Paul H. P. Kaijen, Floris van Alphen, Alexander B. Meijer, and Jan Voorberg. "Identification of glycans on plasma-derived ADAMTS13." Blood 128, no. 21 (2016): e51-e58. http://dx.doi.org/10.1182/blood-2016-06-720912.

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Key Points ADAMTS13 contains complex type N-linked glycans, which contain terminal mannose, sialic acids, and fucose residues. TSP1 repeats are modified by O-fucosylation and C-mannosylation; O-fucosylation was also observed in the disintegrin domain.

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4

Keeley, Tyler S., Shengyu Yang, and Eric Lau. "The Diverse Contributions of Fucose Linkages in Cancer." Cancers 11, no. 9 (2019): 1241. http://dx.doi.org/10.3390/cancers11091241.

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Fucosylation is a post-translational modification of glycans, proteins, and lipids that is responsible for many biological processes. Fucose conjugation via α(1,2), α(1,3), α(1,4), α(1,6), and O’- linkages to glycans, and variations in fucosylation linkages, has important implications for cancer biology. This review focuses on the roles that fucosylation plays in cancer, specifically through modulation of cell surface proteins and signaling pathways. How L-fucose and serum fucosylation patterns might be used for future clinical diagnostic, prognostic, and therapeutic approaches will be discuss

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5

Zhang, Ao, Steven J. Berardinelli, Christina Leonhard-Melief, et al. "O-Fucosylation of ADAMTSL2 is required for secretion and is impacted by geleophysic dysplasia-causing mutations." Journal of Biological Chemistry 295, no. 46 (2020): 15742–53. http://dx.doi.org/10.1074/jbc.ra120.014557.

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ADAMTSL2 mutations cause an autosomal recessive connective tissue disorder, geleophysic dysplasia 1 (GPHYSD1), which is characterized by short stature, small hands and feet, and cardiac defects. ADAMTSL2 is a matricellular protein previously shown to interact with latent transforming growth factor-β binding protein 1 and influence assembly of fibrillin 1 microfibrils. ADAMTSL2 contains seven thrombospondin type-1 repeats (TSRs), six of which contain the consensus sequence for O-fucosylation by protein O-fucosyltransferase 2 (POFUT2). O-fucose–modified TSRs are subsequently elongated to a gluco

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6

Lira-Navarrete, Erandi, Jessika Valero-González, Raquel Villanueva, et al. "Structural Insights into the Mechanism of Protein O-Fucosylation." PLoS ONE 6, no. 9 (2011): e25365. http://dx.doi.org/10.1371/journal.pone.0025365.

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7

Luo, Yi, and Robert S. Haltiwanger. "O-Fucosylation of Notch Occurs in the Endoplasmic Reticulum." Journal of Biological Chemistry 280, no. 12 (2005): 11289–94. http://dx.doi.org/10.1074/jbc.m414574200.

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8

Niwa, Yuki, Takehiro Suzuki, Naoshi Dohmae, and Siro Simizu. "O-fucosylation of CCN1 is required for its secretion." FEBS Letters 589, no. 21 (2015): 3287–93. http://dx.doi.org/10.1016/j.febslet.2015.09.012.

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9

Verbij, Fabian, Eva Stokhuijzen, Floris van Alphen, Paul Kaijen, Alexander Meijer, and Jan Voorberg. "Analysis of the Glycan Composition on Plasma Derived ADAMTS13 Employing Tandem Mass Spectrometry." Blood 126, no. 23 (2015): 1069. http://dx.doi.org/10.1182/blood.v126.23.1069.1069.

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Abstract Acquired thrombotic thrombocytopenic purpura (TTP) is a life-threatening disorder that results from the development of auto-antibodies against ADAMTS13 disrupting the binding of ADAMTS13 to von Willebrand factor and thereby preventing the proteinase activity and/or increasing the clearance from the circulation. Previous research from our department identified 9 O-linked glycosylation, 6 O-fucosylation and 2 C-mannosylation sites on plasma derived ADAMTS13. One of the N-linked glycosylation sites (N1354) is close to one of the previously identified peptides preferentially presented on

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10

Pennarubia, Florian, Emilie Pinault, Bilal Al Jaam, et al. "Mouse WIF1 Is Only Modified with O-Fucose in Its EGF-like Domain III Despite Two Evolutionarily Conserved Consensus Sites." Biomolecules 10, no. 9 (2020): 1250. http://dx.doi.org/10.3390/biom10091250.

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The Wnt Inhibitory Factor 1 (Wif1), known to inhibit Wnt signaling pathways, is composed of a WIF domain and five EGF-like domains (EGF-LDs) involved in protein interactions. Despite the presence of a potential O-fucosylation site in its EGF-LDs III and V, the O-fucose sites occupancy has never been demonstrated for WIF1. In this study, a phylogenetic analysis on the distribution, conservation and evolution of Wif1 proteins was performed, as well as biochemical approaches focusing on O-fucosylation sites occupancy of recombinant mouse WIF1. In the monophyletic group of gnathostomes, we showed

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11

Mormann, Michael, Boris Maček, Anne Gonzalez de Peredo, Jan Hofsteenge, and Jasna Peter-Katalinić. "Structural studies on protein O-fucosylation by electron capture dissociation." International Journal of Mass Spectrometry 234, no. 1-3 (2004): 11–21. http://dx.doi.org/10.1016/j.ijms.2003.12.005.

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12

Lira-Navarrete, Erandi, and Ramon Hurtado-Guerrero. "A perspective on structural and mechanistic aspects of protein O-fucosylation." Acta Crystallographica Section F Structural Biology Communications 74, no. 8 (2018): 443–50. http://dx.doi.org/10.1107/s2053230x18004788.

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Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs), respectively. Within the past six years, crystal structures of both enzymes have been reported, revealing important information on how they recognize protein substrates and achieve catalysis. Here, the structural information available today is su

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13

Serth, Katrin, Karin Schuster-Gossler, Elisabeth Kremmer, Birte Hansen, Britta Marohn-Köhn, and Achim Gossler. "O-Fucosylation of DLL3 Is Required for Its Function during Somitogenesis." PLOS ONE 10, no. 4 (2015): e0123776. http://dx.doi.org/10.1371/journal.pone.0123776.

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14

Smith, D. K., J. F. Harper, and I. S. Wallace. "A potential role for protein O-fucosylation during pollen-pistil interactions." Plant Signaling & Behavior 13, no. 5 (2018): e1467687. http://dx.doi.org/10.1080/15592324.2018.1467687.

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15

Yang, Yu, Dandan Zhang, Huamin Qin, Shuai Liu, and Qiu Yan. "poFUT1 promotes endometrial decidualization by enhancing the O-fucosylation of Notch1." EBioMedicine 44 (June 2019): 563–73. http://dx.doi.org/10.1016/j.ebiom.2019.05.027.

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16

Zhou, Lan, Quanjian Yan, David Yao, Lebing W. Li, Stanton L. Gerson, and John B. Lowe. "Notch-Dependent Control of Blood Lineage Development is Modified by Fucosylation." Blood 112, no. 11 (2008): 2448. http://dx.doi.org/10.1182/blood.v112.11.2448.2448.

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Abstract Notch receptors are conserved cell surface molecules essential for hematopoietic cell fate determination. Activated Notch enhances self-renewal of hematopoietic stem cells and promotes T lymphopoiesis. O-linked fucose moieties attached to the EGF domains of Notch receptors and its modification by Fringe can strongly modulate Notch signaling. Our recently published results indicate that Notch-dependent signaling controls myelopoiesis both in vitro and in vivo, and identify a requirement for Notch fucosylation in the expression of Notch ligand binding activity and Notch signaling effici

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17

Kim, Mi-Lyang, Kumaran Chandrasekharan, Matthew Glass, et al. "O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors." Molecular and Cellular Neuroscience 39, no. 3 (2008): 452–64. http://dx.doi.org/10.1016/j.mcn.2008.07.026.

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18

Pennarubia, Florian, Emilie Pinault, Abderrahman Maftah, and Sébastien Legardinier. "In vitro acellular method to reveal O-fucosylation on EGF-like domains." Glycobiology 29, no. 3 (2018): 192–98. http://dx.doi.org/10.1093/glycob/cwy106.

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19

Bandini, Giulia, John R. Haserick, Edwin Motari, et al. "O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii." Proceedings of the National Academy of Sciences 113, no. 41 (2016): 11567–72. http://dx.doi.org/10.1073/pnas.1613653113.

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Toxoplasma gondii is an intracellular parasite that causes disseminated infections in fetuses and immunocompromised individuals. Although gene regulation is important for parasite differentiation and pathogenesis, little is known about protein organization in the nucleus. Here we show that the fucose-binding Aleuria aurantia lectin (AAL) binds to numerous punctate structures in the nuclei of tachyzoites, bradyzoites, and sporozoites but not oocysts. AAL also binds to Hammondia and Neospora nuclei but not to more distantly related apicomplexans. Analyses of the AAL-enriched fraction indicate th

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20

Mutanwad, Krishna Vasant, Isabella Zangl, and Doris Lucyshyn. "The Arabidopsis O-fucosyltransferase SPINDLY regulates root hair patterning independently of gibberellin signaling." Development 147, no. 19 (2020): dev192039. http://dx.doi.org/10.1242/dev.192039.

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ABSTRACTRoot hairs are able to sense soil composition and play an important role in water and nutrient uptake. In Arabidopsis thaliana, root hairs are distributed in the epidermis in a specific pattern, regularly alternating with non-root hair cells in continuous cell files. This patterning is regulated by internal factors such as a number of hormones, as well as by external factors like nutrient availability. Thus, root hair patterning is an excellent model for studying the plasticity of cell fate determination in response to environmental changes. Here, we report that loss-of-function mutant

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21

Sun, Tai-ping. "Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants." Current Opinion in Structural Biology 68 (June 2021): 113–21. http://dx.doi.org/10.1016/j.sbi.2020.12.013.

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22

Der Vartanian, Audrey, Aymeric Audfray, Bilal Al Jaam, et al. "ProteinO-Fucosyltransferase 1 Expression Impacts Myogenic C2C12 Cell Commitment via the Notch Signaling Pathway." Molecular and Cellular Biology 35, no. 2 (2014): 391–405. http://dx.doi.org/10.1128/mcb.00890-14.

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The Notch signaling pathway plays a crucial role in skeletal muscle regeneration in mammals by controlling the transition of satellite cells from quiescence to an activated state, their proliferation, and their commitment toward myotubes or self-renewal. O-fucosylation on Notch receptor epidermal growth factor (EGF)-like repeats is catalyzed by the proteinO-fucosyltransferase 1 (Pofut1) and primarily controls Notch interaction with its ligands. To approach the role of O-fucosylation in myogenesis, we analyzed a murine myoblastic C2C12 cell line downregulated forPofut1expression by short hairpi

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23

Kałuża, Anna, Justyna Szczykutowicz, and Mirosława Ferens-Sieczkowska. "Glycosylation: Rising Potential for Prostate Cancer Evaluation." Cancers 13, no. 15 (2021): 3726. http://dx.doi.org/10.3390/cancers13153726.

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Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adh

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24

Müller, Julia, Nadia A. Rana, Katrin Serth, Shinako Kakuda, Robert S. Haltiwanger, and Achim Gossler. "O-fucosylation of the Notch Ligand mDLL1 by POFUT1 Is Dispensable for Ligand Function." PLoS ONE 9, no. 2 (2014): e88571. http://dx.doi.org/10.1371/journal.pone.0088571.

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25

Nifant'ev, Nikolay E., Vera Y. Amochaeva, Alexander S. Shashkov та Nikolay K. Kochetkov. "α-Fucosylation by 2,3,4-tri-O-benzoyl-α-l-fucopyranosyl bromide under Helferich conditions". Carbohydrate Research 242 (квітень 1993): 77–89. http://dx.doi.org/10.1016/0008-6215(93)80023-8.

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26

THOMSSON, Kristina A., Marina HINOJOSA-KURTZBERG, Karin A. AXELSSON та ін. "Intestinal mucins from cystic fibrosis mice show increased fucosylation due to an induced Fucα1-2 glycosyltransferase". Biochemical Journal 367, № 3 (2002): 609–16. http://dx.doi.org/10.1042/bj20020371.

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In gene-targeted mouse models for cystic fibrosis (CF), the disease is mainly manifested by mucus obstruction in the intestine. To explore the mucus composition, mucins insoluble and soluble in 6M guanidinium chloride were purified by three rounds of isopycnic ultracentrifugation from the small and large intestines of CF mice (Cftrm1UNC/Cftrm1UNC) and compared with wild-type mice. The amino acid composition was typical of that for mucins and showed increased amounts of the insoluble (2.5-fold increase) and soluble (7-fold increase) mucins in the small intestine of the CF mice compared with wil

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27

Al Jaam, Bilal, Katy Heu, Florian Pennarubia, et al. "Reduced Notch signalling leads to postnatal skeletal muscle hypertrophy in Pofut1 cax/cax mice." Open Biology 6, no. 9 (2016): 160211. http://dx.doi.org/10.1098/rsob.160211.

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Postnatal skeletal muscle growth results from the activation of satellite cells and/or an increase in protein synthesis. The Notch signalling pathway maintains satellite cells in a quiescent state, and once activated, sustains their proliferation and commitment towards differentiation. In mammals, POFUT1-mediated O -fucosylation regulates the interactions between NOTCH receptors and ligands of the DELTA/JAGGED family, thus initiating the activation of canonical Notch signalling. Here, we analysed the consequences of downregulated expression of the Pofut1 gene on postnatal muscle growth in muta

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28

Wang, Lauren W., Malgosia Dlugosz, Robert P. T. Somerville, Mona Raed, Robert S. Haltiwanger, and Suneel S. Apte. "O-Fucosylation of Thrombospondin Type 1 Repeats in ADAMTS-like-1/Punctin-1 Regulates Secretion." Journal of Biological Chemistry 282, no. 23 (2007): 17024–31. http://dx.doi.org/10.1074/jbc.m701065200.

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29

Ayukawa, Tomonori, Kenjiroo Matsumoto, Hiroyuki O. Ishikawa, et al. "Rescue of Notch signaling in cells incapable of GDP-l-fucose synthesis by gap junction transfer of GDP-l-fucose in Drosophila." Proceedings of the National Academy of Sciences 109, no. 38 (2012): 15318–23. http://dx.doi.org/10.1073/pnas.1202369109.

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Notch (N) is a transmembrane receptor that mediates cell–cell interactions to determine many cell-fate decisions. N contains EGF-like repeats, many of which have an O-fucose glycan modification that regulates N-ligand binding. This modification requires GDP-l-fucose as a donor of fucose. The GDP-l-fucose biosynthetic pathways are well understood, including the de novo pathway, which depends on GDP-mannose 4,6 dehydratase (Gmd) and GDP-4-keto-6-deoxy-d-mannose 3,5-epimerase/4-reductase (Gmer). However, the potential for intercellularly supplied GDP-l-fucose and the molecular basis of such trans

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30

Hinneburg, Hannes, Jessica L. Pedersen, Nilesh J. Bokil, et al. "High-resolution longitudinal N- and O-glycoprofiling of human monocyte-to-macrophage transition." Glycobiology 30, no. 9 (2020): 679–94. http://dx.doi.org/10.1093/glycob/cwaa020.

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Abstract Protein glycosylation impacts the development and function of innate immune cells. The glycophenotypes and the glycan remodelling associated with the maturation of macrophages from monocytic precursor populations remain incompletely described. Herein, label-free porous graphitised carbon–liquid chromatography–tandem mass spectrometry (PGC-LC-MS/MS) was employed to profile with high resolution the N- and O-glycome associated with human monocyte-to-macrophage transition. Primary blood-derived CD14+ monocytes were differentiated ex vivo in the absence of strong anti- and proinflammatory

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31

Valliere-Douglass, J. F., L. J. Brady, C. Farnsworth, et al. "O-Fucosylation of an antibody light chain: Characterization of a modification occurring on an IgG1 molecule." Glycobiology 19, no. 2 (2008): 144–52. http://dx.doi.org/10.1093/glycob/cwn116.

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32

Sorvillo, N., P. H. Kaijen, M. Matsumoto, et al. "Identification of N-linked glycosylation and putative O-fucosylation, C-mannosylation sites in plasma derived ADAMTS13." Journal of Thrombosis and Haemostasis 12, no. 5 (2014): 670–79. http://dx.doi.org/10.1111/jth.12535.

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33

Uchiyama, Taketo, та Ole Hindsgaul. "Per-O-Trimethylsilyl-α-L-Fucopyranosyl Iodide: A Novel Glycosylating Agent for Terminal α-L-Fucosylation". Synlett 1996, № 06 (1996): 499–501. http://dx.doi.org/10.1055/s-1996-5491.

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34

Kao, Yung-Hsiang, Geoffrey F. Lee, Yang Wang, et al. "The Effect of O-Fucosylation on the First EGF-like Domain from Human Blood Coagulation Factor VII†." Biochemistry 38, no. 22 (1999): 7097–110. http://dx.doi.org/10.1021/bi990234z.

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35

Yuan, Youxi, and Robert S. Haltiwanger. "How does GDP‐fucose get into the Endoplasmic Reticulum for O‐fucosylation of EGF Repeats and TSRs?" FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04235.

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36

Naumenko, Olesya I., Han Zheng, Yanwen Xiong, et al. "Studies on the O-polysaccharide of Escherichia albertii O2 characterized by non-stoichiometric O-acetylation and non-stoichiometric side-chain l-fucosylation." Carbohydrate Research 461 (May 2018): 80–84. http://dx.doi.org/10.1016/j.carres.2018.02.013.

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37

Ząbczyńska, Marta, Kamila Kozłowska, and Ewa Pocheć. "Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders." International Journal of Molecular Sciences 19, no. 9 (2018): 2792. http://dx.doi.org/10.3390/ijms19092792.

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The key proteins responsible for hormone synthesis in the thyroid are glycosylated. Oligosaccharides strongly affect the function of glycosylated proteins. Both thyroid-stimulating hormone (TSH) secreted by the pituitary gland and TSH receptors on the surface of thyrocytes contain N-glycans, which are crucial to their proper activity. Thyroglobulin (Tg), the protein backbone for synthesis of thyroid hormones, is a heavily N-glycosylated protein, containing 20 putative N-glycosylated sites. N-oligosaccharides play a role in Tg transport into the follicular lumen, where thyroid hormones are prod

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38

UCHIYAMA, T., та O. HINDSGAUL. "ChemInform Abstract: per-O-Trimethylsilyl-α-L-fucopyranosyl Iodide: A Novel Glycosylating Agent for Terminal α-L-Fucosylation." ChemInform 27, № 42 (2010): no. http://dx.doi.org/10.1002/chin.199642226.

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39

Bandini, Giulia, Andreia Albuquerque-Wendt, Jan Hegermann, John Samuelson, and Françoise H. Routier. "Protein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparum." Parasitology 146, no. 14 (2019): 1755–66. http://dx.doi.org/10.1017/s0031182019000040.

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AbstractApicomplexan parasites are amongst the most prevalent and morbidity-causing pathogens worldwide. They are responsible for severe diseases in humans and livestock and are thus of great public health and economic importance. Until the sequencing of apicomplexan genomes at the beginning of this century, the occurrence of N- and O-glycoproteins in these parasites was much debated. The synthesis of rudimentary and divergent N-glycans due to lineage-specific gene loss is now well established and has been recently reviewed. Here, we will focus on recent studies that clarified classical O-glyc

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40

Kim, Jihye, Changsoo Ryu, Jongkwan Ha, et al. "Structural and Quantitative Characterization of Mucin-Type O-Glycans and the Identification of O-Glycosylation Sites in Bovine Submaxillary Mucin." Biomolecules 10, no. 4 (2020): 636. http://dx.doi.org/10.3390/biom10040636.

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Bovine submaxillary mucin (BSM) is a gel-forming glycoprotein polymer, and Ser/Thr-linked glycans (O-glycans) are important in regulating BSM’s viscoelasticity and polymerization. However, details of O-glycosylation have not been reported. This study investigates the structural and quantitative characteristics of O-glycans and identifies O-glycosylation sites in BSM using liquid chromatography–tandem mass spectrometry. The O-glycans (consisting of di- to octa-saccharides) and their quantities (%) relative to total O-glycans (100%; 1.1 pmol per 1 μg of BSM) were identified with 14 major (>1.

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Du, Jianguang, Hideyuki Takeuchi, Christina Leonhard-Melief, et al. "O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation." Developmental Biology 346, no. 1 (2010): 25–38. http://dx.doi.org/10.1016/j.ydbio.2010.07.008.

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42

Gebauer, Jan M., Stefan Müller, Franz-Georg Hanisch, Mats Paulsson, and Raimund Wagener. "O-Glucosylation andO-Fucosylation Occur Together in Close Proximity on the First Epidermal Growth Factor Repeat of AMACO (VWA2 Protein)." Journal of Biological Chemistry 283, no. 26 (2008): 17846–54. http://dx.doi.org/10.1074/jbc.m704820200.

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43

Yao, David, Yuanshuai Huang, Xiaoran Huang, et al. "Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of Notch receptor ligand interactions." Blood 117, no. 21 (2011): 5652–62. http://dx.doi.org/10.1182/blood-2010-12-326074.

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Abstract Notch signaling is essential for lymphocyte development and is also implicated in myelopoiesis. Notch receptors are modified by O-fucosylation catalyzed by protein O-fucosyltransferase 1 (Pofut1). Fringe enzymes add N-acetylglucosamine to O-fucose and modify Notch signaling by altering the sensitivity of Notch receptors to Notch ligands. To address physiologic functions in hematopoiesis of Notch modified by O-fucose glycans, we examined mice with inducible inactivation of Pofut1 using Mx-Cre. These mice exhibited a reduction in T lymphopoiesis and in the production of marginal-zone B

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44

Deschuyter, Marlène, Florian Pennarubia, Emilie Pinault, Sébastien Legardinier, and Abderrahman Maftah. "Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer." Cancers 12, no. 6 (2020): 1430. http://dx.doi.org/10.3390/cancers12061430.

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Background: Protein O-fucosyltransferase 1 (POFUT1) overexpression, which is observed in many cancers such as colorectal cancer (CRC), leads to a NOTCH signaling dysregulation associated with the tumoral process. In rare CRC cases, with no POFUT1 overexpression, seven missense mutations were found in human POFUT1. Methods: Recombinant secreted forms of human WT POFUT1 and its seven mutated counterparts were produced and purified. Their O-fucosyltransferase activities were assayed in vitro using a chemo-enzymatic approach with azido-labeled GDP-fucose as a donor substrate and NOTCH1 EGF-LD26, p

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45

Whitfield, Dennis M., Caroline J. Ruzicka, Jeremy P. Carver та Jiri J. Krepinsky. "Syntheses of model oligosaccharides of biological significance. 9. Syntheses of trideuteriomethyl di-3,6-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-β-D-galactopyranoside: the I antigen branch-point trisaccharide and related disaccharides". Canadian Journal of Chemistry 65, № 4 (1987): 693–703. http://dx.doi.org/10.1139/v87-118.

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The title trisaccharide, 13c, was synthesized, as well as its two component disaccharides, 10c and 11c. Four disaccharides, 3c, 4c, 5c, and 7c, were also prepared to serve as model compounds for the investigation of the 3-dimensional structure of more complex oligosaccharides. The β-1,3 linkage was formed in 75% yield by coupling 3,4,6-tri-O-acetyl-2-deoxy-2-phthalimido-β-D-glucopyranosyl bromide (9) with trideuteriomethyl 2-O-benzoyl-4,6-benzylidene-β-D-galactopyranoside (2a), using silver trifluoromethanesulphonate as a promoter in the presence of the base 2,6-di-tert-butyl-4-methylpyridine.

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Li, Cui-yun, Guang-jian Liu, Wei Du, Yuan Zhang, and Guo-wen Xing. "A novel O -fucosylation strategy preactivated by ( p -Tol) 2 SO/Tf 2 O and its application for the synthesis of Lewis blood group antigen Lewis a." Tetrahedron Letters 58, no. 22 (2017): 2109–12. http://dx.doi.org/10.1016/j.tetlet.2017.04.056.

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Nanno, Yoshihide, Asif Shajahan, Roberto N. Sonon, Parastoo Azadi, Bernhard J. Hering, and Christopher Burlak. "High-mannose type N-glycans with core fucosylation and complex-type N-glycans with terminal neuraminic acid residues are unique to porcine islets." PLOS ONE 15, no. 11 (2020): e0241249. http://dx.doi.org/10.1371/journal.pone.0241249.

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Abstract:

Objectives Islet transplantation is an emerging treatment option for type 1 diabetes but its application is limited by the shortage of human pancreas donors. Characterization of the N- and O-glycan surface antigens that vary between human and genetically engineered porcine islet donors could shed light on targets of antibody mediated rejection. Methods N- and O-glycans were isolated from human and adult porcine islets and analyzed using matrix-assisted laser-desorption time-of-flight mass spectrometry (MALDI-TOF-MS) and electrospray ionization mass spectrometry (ESI-MS/MS). Results A total of

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Al-Shareffi, E., J. L. Chaubard, C. Leonhard-Melief, S. K. Wang, C. H. Wong, and R. S. Haltiwanger. "6-Alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin Type-1 repeats by protein O-fucosyltransferases 1 and 2." Glycobiology 23, no. 2 (2012): 188–98. http://dx.doi.org/10.1093/glycob/cws140.

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MARTI, Thomas, Johann SCHALLER, Egon E. RICKLI, et al. "The N-and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns." European Journal of Biochemistry 173, no. 1 (1988): 57–63. http://dx.doi.org/10.1111/j.1432-1033.1988.tb13966.x.

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Krushkal, Julia, Yingdong Zhao, Curtis Hose, Anne Monks, James H. Doroshow, and Richard Simon. "Longitudinal Transcriptional Response of Glycosylation-Related Genes, Regulators, and Targets in Cancer Cell Lines Treated With 11 Antitumor Agents." Cancer Informatics 16 (January 1, 2017): 117693511774725. http://dx.doi.org/10.1177/1176935117747259.

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Cellular glycosylation processes are vital to cell functioning. In malignant cells, they are profoundly altered. We used time-course gene expression data from the NCI-60 cancer cell lines treated with 11 antitumor agents to analyze expression changes of genes involved in glycosylation pathways, genes encoding glycosylation targets or regulators, and members of cancer pathways affected by glycosylation. We also identified glycosylation genes for which pretreatment expression levels or changes after treatment were correlated with drug sensitivity. Their products are involved in N-glycosylation a

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