Antibodies that detect o-linked β-D-N-Acetylglucosamine on the extracellular domain of cell surface glycoproteins

Journal of Biological Chemistry

Volumn 289, Issue 16, 2014, Pages 11132-11142

  Tashima, Yuko ^a   Stanley, Pamela ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; GLYCOPROTEINS;

CELL SURFACES; CYTOSOLIC; EXTRACELLULAR DOMAINS; N-GLYCANS; O-LINKED;

ANTIBODIES;

BETA DEXTRO N ACETYLGLUCOSAMINE; CELL SURFACE PROTEIN; EPIDERMAL GROWTH FACTOR SPECIFIC O LINKED BETA DEXTRO N ACETYLGLUCOSAMINE TRANSFERASE; GLUCOSAMINE; GLYCAN DERIVATIVE; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 10D8; MONOCLONAL ANTIBODY 18B10.C7; MONOCLONAL ANTIBODY 9D1.E4; MONOCLONAL ANTIBODY CTD110.6; MONOCLONAL ANTIBODY HGAC85; MONOCLONAL ANTIBODY IF5.D6; MONOCLONAL ANTIBODY RL2; N ACETYLGLUCOSAMINE; N GLYCAN; NOTCH1 RECEPTOR; O LINKED BETA DEXTRO N ACETYLGLUCOSAMINE; TRANSFERASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIBODY SPECIFICITY; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CHO CELL; CONTROLLED STUDY; FEMALE; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; SIGNAL TRANSDUCTION;

ANTIBODIES; CHO; FLOW CYTOMETRY; GLCNAC-TERMINATING N-GLYCANS; LEC1; LEC8; MUTANT; O-GLCNAC; O-GLCNACYLATION;

ACETYLGLUCOSAMINE; ANIMALS; ANTIBODIES, MONOCLONAL, MURINE-DERIVED; CHO CELLS; CRICETINAE; CRICETULUS; GLYCOPROTEINS; HUMANS; N-ACETYLGLUCOSAMINYLTRANSFERASES; REPETITIVE SEQUENCES, AMINO ACID;

EID: 84899006820     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.492512     Document Type: Article

References (32)

1. Varki, A., Cummings, R. D., Esko, J. D., Freeze, H. H., Stanley, P., Bertozzi, C. R., Hart, G. W., and Etlzler, M. E. (2009) Essentials of Glycobiology, 2nd Edition, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
2. Matsuura, A., Ito, M., Sakaidani, Y., Kondo, T., Murakami, K., Furukawa, K., Nadano, D., Matsuda, T., and Okajima, T. (2008) O-Linked N-Acetylglucosamine is present on the extracellular domain of Notch receptors. J. Biol. Chem. 283, 35486-35495
3. Sakaidani, Y., Furukawa, K., and Okajima, T. (2010) O-GlcNAc modification of the extracellular domain of Notch receptors. Methods Enzymol. 480, 355-373
4. Sakaidani, Y., Ichiyanagi, N., Saito, C., Nomura, T., Ito, M., Nishio, Y., Nadano, D., Matsuda, T., Furukawa, K., and Okajima, T. (2012) O-Linked N-Acetylglucosamine modification of mammalian Notch receptors by an atypical O-GlcNAc transferase Eogt1. Biochem. Biophys. Res. Commun. 419, 14-19
5. Sakaidani, Y., Nomura, T., Matsuura, A., Ito, M., Suzuki, E., Murakami, K., Nadano, D., Matsuda, T., Furukawa, K., and Okajima, T. (2011) O-Linked-N-Acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions. Nat. Commun. 2, 583
6. Hoffmann, B. R., Liu, Y., and Mosher, D. F. (2012) Modification of EGFlike module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-Acetylglucosamine. PLoS One 7, e32762
7. Müller, R., Jenny, A., and Stanley, P. (2013) The EGF repeat-specific O-GlcNAc-Transferase Eogt interacts with Notch signaling and pyrimidine metabolism pathways in Drosophila. PLoS One 8, e62835
8. Alfaro, J. F., Gong, C. X., Monroe, M. E., Aldrich, J. T., Clauss, T. R., Purvine, S. O., Wang, Z., Camp, D. G., 2nd, Shabanowitz, J., Stanley, P., Hart, G. W., Hunt, D. F., Yang, F., and Smith, R. D. (2012) Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proc. Natl. Acad. Sci. U.S.A. 109, 7280-7285
9. Butkinaree, C., Park, K., and Hart, G. W. (2010) O-Linked-N- Acetylglucosamine (O-GlcNAc): extensive cross-Talk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim. Biophys. Acta 1800, 96-106
10. Comer, F. I., Vosseller, K., Wells, L., Accavitti, M. A., and Hart, G. W. (2001) Characterization of a mouse monoclonal antibody specific for Olinked N-Acetylglucosamine. Anal. Biochem. 293, 169-177
11. Turner, J. R., Tartakoff, A. M., and Greenspan, N. S. (1990) Cytologic assessment of nuclear and cytoplasmic O-linked N-Acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc. Natl. Acad. Sci. U.S.A. 87, 5608-5612
12. Snow, C. M., Senior, A., and Gerace, L. (1987) Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143-1156
13. Yoshida, N., Mortara, R. A., Araguth, M. F., Gonzalez, J. C., and Russo, M. (1989) Metacyclic neutralizing effect of monoclonal antibody 10D8 directed to the 35-And 50-kilodalton surface glycoconjugates of Trypanosoma cruzi. Infect. Immun. 57, 1663-1667
14. Teo, C. F., Ingale, S., Wolfert, M. A., Elsayed, G. A., Nöt, L. G., Chatham, J. C., Wells, L., and Boons, G. J. (2010) Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc. Nat. Chem. Biol. 6, 338-343
15. Isono, T. (2011) O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation. PLoS One 6, e18959
16. Ogawa, M., Nakamura, N., Nakayama, Y., Kurosaka, A., Manya, H., Kanagawa, M., Endo, T., Furukawa, K., and Okajima, T. (2013) GTDC2 modifies O-mannosylated-dystroglycan in the endoplasmic reticulum to generate N-Acetylglucosamine epitopes reactive with CTD110.6 antibody. Biochem. Biophys. Res. Commun. 440, 88-93
17. Joutel, A., Andreux, F., Gaulis, S., Domenga, V., Cecillon, M., Battail, N., Piga, N., Chapon, F., Godfrain, C., and Tournier-Lasserve, E. (2000) The ectodomain of the Notch3 receptor accumulates within the cerebrovasculature of CADASIL patients. J. Clin. Invest. 105, 597-605
18. Chen, W., and Stanley, P. (2003) Five Lec1CHOcell mutants have distinct Mgat1 gene mutations that encode truncated N-Acetylglucosaminyltransferase I. Glycobiology 13, 43-50
19. Eckhardt, M., Gotza, B., and Gerardy-Schahn, R. (1998) Mutants of the CMP-sialic acid transporter causing the Lec2 phenotype. J. Biol. Chem. 273, 20189-20195
20. Oelmann, S., Stanley, P., and Gerardy-Schahn, R. (2001) Point mutations identified in lec8 Chinese hamster ovary glycosylation mutants that inactivate both the UDP-galactose and CMP-sialic acid transporters. J. Biol. Chem. 276, 26291-26300
21. Chen, J., Moloney, D. J., and Stanley, P. (2001) Fringe modulation of Jagged1-induced Notch signaling requires the action of-4-galactosyltransferase- 1. Proc. Natl. Acad. Sci. U.S.A. 98, 13716-13721
22. Hou, X., Tashima, Y., and Stanley, P. (2012) Galactose differentially modulates lunatic and Manic Fringe effects on Delta1-induced NOTCH signaling. J. Biol. Chem. 287, 474-483
23. Sanjabi, S., Williams, K. J., Saccani, S., Zhou, L., Hoffmann, A., Ghosh, G., Gerondakis, S., Natoli, G., and Smale, S. T. (2005) A c-Rel subdomain responsible for enhanced DNA-binding affinity and selective gene activation. Genes Dev. 19, 2138-2151
24. Moloney, D. J., Panin, V. M., Johnston, S. H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K. D., Haltiwanger, R. S., and Vogt, T. F. (2000) Fringe is a glycosyltransferase that modifies Notch. Nature 406, 369-375
25. Brückner, K., Perez, L., Clausen, H., and Cohen, S. (2000) Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406, 411-415
26. Kawar, Z. S., Haslam, S. M., Morris, H. R., Dell, A., and Cummings, R. D. (2005) Novel poly-GalNAc-1-4GlcNAc (LacdiNAc) and fucosylated poly-LacdiNAc N-glycans from mammalian cells expressing-1,4-N-Acetylgalactosaminyltransferase and-1,3-fucosyltransferase. J. Biol. Chem. 280, 12810-12819
27. North, S. J., Huang, H. H., Sundaram, S., Jang-Lee, J., Etienne, A. T., Trollope, A., Chalabi, S., Dell, A., Stanley, P., and Haslam, S. M. (2010) Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J. Biol. Chem. 285, 5759-5775
28. Foddy, L., Feeney, J., and Hughes, R. C. (1986) Properties of baby hamster kidney (BHK) cells treated with swainsonine, an inhibitor of glycoprotein processing: comparison with ricin-resistant BHK cell mutants. Biochem. J. 233, 697-706
29. Foddy, L., and Hughes, R. C. (1986) Interactions of lectins with normal, swainsonine-Treated and ricin-resistant baby hamster kidney BHK cells. Carbohydr. Res. 151, 293-304
30. Aguilan, J. T., Sundaram, S., Nieves, E., and Stanley, P. (2009) Mutational and functional analysis of Large in a novel CHO glycosylation mutant. Glycobiology 19, 971-986
31. Haltiwanger, R. S., Grove, K., and Philipsberg, G. A. (1998) Modulation of O-linked N-Acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-N-Acetylglucosaminidase inhibitor O-(2-Acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate. J. Biol. Chem. 273, 3611-3617
32. Torres, C. R., and Hart, G. W. (1984) Topography and polypeptide distribution of terminal N-Acetylglucosamine residues on the surfaces of intact lymphocytes: evidence for O-linked GlcNAc. J. Biol. Chem. 259, 3308-3317