Determination of carbohydrate structure recognized by prostate-specific F77 monoclonal antibody through expression analysis of glycosyltransferase genes

Journal of Biological Chemistry

Volumn 289, Issue 23, 2014, Pages 16478-16486

  Nonaka, Motohiro ^a   Fukuda, Michiko N ^a,e   Gao, Chao ^b   Li, Zhen ^b   Zhang, Hongtao ^c   Greene, Mark I ^c   Peehl, Donna M ^d   Feizi, Ten ^b   Fukuda, Minoru ^a  

^a BURNHAM INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d IMPERIAL COLLEGE LONDON   (United Kingdom)

^e NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATES; CELL CULTURE; CELLS; DISEASES; ENCODING (SYMBOLS); ENZYMES; MAMMALS; MONOCLONAL ANTIBODIES; UROLOGY;

CARBOHYDRATE EPITOPES; EXPRESSION ANALYSIS; EXPRESSION VECTORS; GLYCOSYL TRANSFERASE; GLYCOSYLTRANSFERASES; HUMAN PROSTATE CANCER; PROSTATE CANCER CELLS; QUANTITATIVE RT-PCR;

EPITOPES;

CARBOHYDRATE; EPITOPE; FUCOSYLTRANSFERASE; GLYCOSYLTRANSFERASE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY F77; N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEIN GCNT1; PROTEIN GCNT2; PROTEIN GCNT3; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

ANTIGEN EXPRESSION; ANTIGEN RECOGNITION; ARTICLE; BLOOD GROUP ABO SYSTEM; CARBOHYDRATE ANALYSIS; CELL HYPOXIA; CONTROLLED STUDY; GENE EXPRESSION; GENETIC CODE; GLYCOSYLTRANSFERASE GENE; PRIORITY JOURNAL; PROSTATE CANCER CELL LINE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TRANSCRIPTION REGULATION; UPREGULATION;

ANTIGEN; BIOMARKER OF EPITHELIAL CANCER CELL; CANCER-ASSOCIATED CARBOHYDRATE ANTIGEN; CARBOHYDRATE BIOSYNTHESIS; CARBOHYDRATE STRUCTURE; GLYCOBIOLOGY; GLYCOSYLTRANSFERASE;

ABO BLOOD-GROUP SYSTEM; ANTIBODIES, MONOCLONAL; BASE SEQUENCE; CARBOHYDRATE SEQUENCE; CELL LINE, TUMOR; DNA PRIMERS; GLYCOSYLTRANSFERASES; HUMANS; PROSTATE-SPECIFIC ANTIGEN;

EID: 84902188865     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.559047     Document Type: Article

References (43)

1. Hakomori, S. (2002) Glycosylation defining cancer malignancy: new wine in an old bottle. Proc. Natl. Acad. Sci. U. S. A. 99, 10231-10233
2. Adamczyk, B., Tharmalingam, T., and Rudd, P. M. (2012) Glycans as cancer biomarkers. Biochim. Biophys. Acta 1820, 1347-1353
3. Baković, M. P., Selman, M. H., Hoffmann, M., Rudan, I., Campbell, H., Deelder, A. M., Lauc, G., and Wuhrer, M. (2013) High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides. J. Proteome Res. 12, 821-831
4. Carrington, S. D., Irwin, J. A., Liu, L., Rudd, P. M., Matthews, E., and Corfield, A. P. (2012) Analysing mucin degradation. Methods Mol. Biol. 842, 191-215
5. Gornik, O., Pavić, T., and Lauc, G. (2012) Alternative glycosylation modulates function of IgG and other proteins-implications on evolution and disease. Biochim. Biophys. Acta 1820, 1318-1326
6. Lauc, G., Rudan, I., Campbell, H., and Rudd, P. M. (2010) Complex genetic regulation of protein glycosylation. Mol. Biosyst. 6, 329-335
7. Lauc, G., Vojta, A., and Zoldoš, V. (2014) Epigenetic regulation of glycosylation is the quantum mechanics of biology. Biochim. Biophys. Acta 1840, 65-70
8. Liu, L., Tharmalingam, T., Maischberger, E., Albrecht, S., Gallagher, M. E., Miranda-Casoluengo, R., Meijer, W. G., Rudd, P. M., and Irwin, J. A. (2013) A HPLC-based glycoanalytical protocol allows the use of natural O-glycans derived from glycoproteinsas substrates for glycosidase discovery from microbial culture. Glycoconj. J. 30, 791-800
9. Wada, Y., Dell, A., Haslam, S. M., Tissot, B., Canis, K., Azadi, P., Bäckström, M., Costello, C. E., Hansson, G. C., Hiki, Y., Ishihara, M., Ito, H., Kakehi, K., Karlsson, N., Hayes, C. E., Kato, K., Kawasaki, N., Khoo, K. H., Kobayashi, K., Kolarich, D., Kondo, A., Lebrilla, C., Nakano, M., Narimatsu, H., Novak, J., Novotny, M. V., Ohno, E., Packer, N. H., Palaima, E., Renfrow, M. B., Tajiri, M., Thomsson, K. A., Yagi, H., Yu, S. Y., and Taniguchi, N. (2010) Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1. Mol. Cell Proteomics 9, 719-727
10. Zitzmann, N., Block, T., Methta, A., Rudd, P., Burton, D., Wilson, I., Platt, F., Butters, T., and Dwek, R. A. (2005) Glycosylation: disease targets and therapy. Adv. Exp. Med. Biol. 564, 1-2
11. Zivkovic, A. M., German, J. B., Lebrilla, C. B., and Mills, D. A. (2011) Human milk glycobiome and its impact on the infant gastrointestinal microbiota. Proc. Natl. Acad. Sci. U. S. A. 108, 4653-4658
12. Kannagi, R. (2000) Monoclonal anti-glycosphingolipid antibodies. Methods Enzymol. 312, 160-179
13. Feizi, T. (2013) Carbohydrate recognition in the immune system: contributions of neoglycolipid-based microarrays to carbohydrate ligand discovery. Ann. N. Y. Acad. Sci. 1292, 33-44
14. Miyake, M., Taki, T., Hitomi, S., and Hakomori, S. (1992) Correlation of expression of H/Le (y)/Le (b) antigens with survival in patients with carcinoma of the lung. N. Engl. J. Med. 327, 14-18
15. Nakamori, S., Furukawa, H., Hiratsuka, M., Iwanaga, T., Imaoka, S., Ishikawa, O., Kabuto, T., Sasaki, Y., Kameyama, M., Ishiguro, S., and Irimura, T. (1997) Expression of carbohydrate antigen sialyl Le (a): a new functional prognostic factor in gastric cancer. J. Clin. Oncol. 15, 816-825
16. Feizi, T. (2000) Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium. Glycoconj. J. 17, 553-565
17. Alvarez-Rueda, N., Leprieur, S., Clémenceau, B., Supiot, S., Sébille-Rivain, V., Faivre-Chauvet, A., Davodeau, F., Paris, F., Barbet, J., Aubry, J., and Birklé, S. (2007) Binding activities and antitumor properties of a new mouse/human chimeric antibody specific for GD2 ganglioside antigen. Clin. Cancer Res. 13, 5613s-5620s
18. Hellström, I., Garrigues, H. J., Garrigues, U., and Hellström, K. E. (1990) Highly tumor-reactive, internalizing, mouse monoclonal antibodies to Le (y)-related cell surface antigens. Cancer Res. 50, 2183-2190
19. Nozawa, S., Aoki, D., Tsukazaki, K., Susumu, N., Sakayori, M., Suzuki, N., Suzuki, A., Wakita, R., Mukai, M., Egami, Y., Kojima-Aikawa, K., Ishida, I., Belot, F., Hindsgaul, O., Fukuda, M., and Fukuda, M. N. (2004) HMMC-1: a humanized monoclonal antibody with therapeutic potential against Mullerian duct-related carcinomas. Clin. Cancer Res. 10, 7071-7078
20. Zhang, G., Zhang, H., Wang, Q., Lal, P., Carroll, A. M., de la Llera-Moya, M., Xu, X., and Greene, M. I. (2010) Suppression of human prostate tumor growth by a unique prostate-specific monoclonal antibody F77 targeting a glycolipid marker. Proc. Natl. Acad. Sci. U. S. A. 107, 732-737
21. Shibata, T. K., Matsumura, F., Wang, P., Yu, S., Chou, C. C, Khoo, K. H., Kitayama, K., Akama, T. O., Sugihara, K., Kanayama, N., Kojima-Aikawa, K., Seeberger, P. H., Fukuda, M., Suzuki, A., Aoki, D., and Fukuda, M. N. (2012) Identification of mono- and disulfated N-acetyl-lactosaminyl oligosaccharide structures as epitopes specifically recognized by humanized monoclonal antibody HMOCC-1 raised against ovarian cancer. J. Biol. Chem. 287, 6592-6602
22. Carroll, A. M., Zalutsky, M., Schatten, S., Bhan, A., Perry, L. L., Sobotka, C, Benacerraf, B., and Greene, M. I. (1984) Monoclonal antibodies to tissuespecific cell surface antigens. I. Characterization of an antibody to a prostate tissue antigen. Clin. Immunol. Immunopathol. 33, 268-281
23. Abe, K., McKibbin, J. M., and Hakomori, S. (1983) The monoclonal antibody directed to difucosylated type 2 chain (Fucα1 leads to 2Galβ1 leads to 4[Fu α1 leads to 3]GlcNAc; Y determinant). J. Biol. Chem. 258, 11793-11797
24. Bierhuizen, M. F., Mattei, M. G., and Fukuda, M. (1993) Expression of the developmental I antigen by a cloned human cDNA encoding a member of a β-1, 6-N-acetylglucosaminyltransferase gene family. Genes Dev. 7, 468-478
25. Yeh, J. C, Ong, E., and Fukuda, M. (1999) Molecular cloning and expression of a novel β-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274, 3215-3221
26. Yamamoto, F., Clausen, H., White, T., Marken, J., and Hakomori, S. (1990) Molecular genetic basis of the histo-blood group ABO system. Nature 345, 229-233
27. Yamamoto, F., and Hakomori, S. (1990) Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions. J. Biol. Chem. 265, 19257-19262
28. Stanley, P., Raju, T. S., and Bhaumik, M. (1996) CHO cells provide access to novel N-glycans and developmentally regulated glycosyltransferases. Glycobiology 6, 695-699
29. Howard, D. R., Fukuda, M., Fukuda, M. N., and Stanley, P. (1987) The GDP-fucose: N-acetylglucosaminide 3-α-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates. J. Biol. Chem. 262, 16830-16837
30. Bierhuizen, M. F., and Fukuda, M. (1992) Expression cloning of a cDNA encoding UDP-GlcNAc: Galβ1-3-GalNAc-R (GlcNAc to GalNAc) β1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen. Proc. Natl. Acad. Sci. U. S. A. 89, 9326-9330
31. Wattenberg, B. W. (1990) Glycolipid and glycoprotein transport through the Golgi complex are similar biochemically and kinetically. Reconstitution of glycolipid transport in a cell free system. J. Cell Biol. 111, 421-428
32. Vaupel, P., and Mayer, A. (2007) Hypoxia in cancer: significance and impact on clinical outcome. Cancer Metastasis Rev. 26, 225-239
33. Koike, T., Kimura, N., Miyazaki, K., Yabuta, T., Kumamoto, K., Takenoshita, S., Chen, J., Kobayashi, M., Hosokawa, M., Taniguchi, A., Kojima, T., Ishida, N., Kawakita, M., Yamamoto, H., Takematsu, H., Suzuki, A., Kozutsumi, Y., and Kannagi, R. (2004) Hypoxia induces adhesion molecules on cancer cells: A missing link between Warburg effect and induction of selectin-ligand carbohydrates. Proc. Natl. Acad. Sci. U. S. A. 101, 8132-8137
34. Harris, A. L. (2002) Hypoxia-a key regulatory factor in tumour growth. Nat. Rev. Cancer 2, 38-47
35. Shimodaira, K., Nakayama, J., Nakamura, N., Hasebe, O., Katsuyama, T., and Fukuda, M. (1997) Carcinoma-associated expression of core 2 β-1, 6-N-acetylglucosaminyltransferase gene in human colorectal cancer: role of O-glycans in tumor progression. Cancer Res. 57, 5201-5206
36. Zhang, H, Meng, F., Wu, S., Kreike, B., Sethi, S., Chen, W., Miller, F. R., and Wu, G. (2011) Engagement of I-branching β-1, 6-N- acetylglucosaminyltransferase 2 in breast cancer metastasis and TGF-β signaling. Cancer Res. 71, 4846-4856
37. Siegel, R., DeSantis, C, Virgo, K., Stein, K., Mariotto, A., Smith, T., Cooper, D., Gansler, T., Lerro, C, Fedewa, S., Lin, C, Leach, C, Cannady, R. S., Cho, H., Scoppa, S., Hachey, M., Kirch, R., Jemal, A., and Ward, E. (2012) Cancer treatment and survivorship statistics, 2012. CA. Cancer J. Clin. 62, 220-241
38. Prensner, J. R., Rubin, M. A., Wei, J. T., and Chinnaiyan, A. M. (2012) Beyond PSA: the next generation of prostate cancer biomarkers. Sci. Transl. Med. 4, 127rv123
39. Maeda, T., Yamada, Y., Tawara, M., Yamasaki, R., Yakata, Y., Tsutsumi, C, Onimaru, Y., Kamihira, S., and Tomonaga, M. (2001) Successful treatment with a chimeric anti-CD20 monoclonal antibody (IDEC-C2B8, rituximab) for a patient with relapsed mantle cell lymphoma who developed a human anti-chimeric antibody. Int. J. Hematol. 74, 70-75
40. Tobinai, K. (2001) Clinical trials of a mouse-human chimeric anti-CD20 monoclonal antibody (rituximab) for B cell non-Hodgkin's lymphoma in Japan. Cancer Chemother. Pharmacol. 48, S85-S90
41. Talwar, G. P., Gupta, R., Gupta, S. K., Malhotra, R., Khanna, R., Mitra, D. K., Sehgal, S., Minz, R., and Kumar, A. (2001) A monoclonal antibody cytolytic to androgen independent DU145 and PC-3 human prostatic carcinoma cells. Prostate 46, 207-213
42. Huang, X., Bennett, M., and Thorpe, P. E. (2004) Anti-tumor effects and lack of side effects in mice of an immunotoxin directed against human and mouse prostate-specific membrane antigen. Prostate 61, 1-11
43. Gao, C, Liu, Y., Zhang, H, Zhang, Y., Fukuda, M. N., Palma, A. S., Kozak, R. P., Childs, R. A., Nonaka, M., Li, Z., Siegel, D. L., Hanfland. P., Peehl, D. M., Chai, W., Greene, M. I., and Feizi, T. (April 21, 2014) Carbohydrate sequence of the prostate cancer-associated antigen F77 assigned by a mucin O-glycome designer array. J. Biol. Chem. 10.1074/jbc. M114.558932