Browse > Article
http://dx.doi.org/10.5483/BMBRep.2011.44.12.765

Pros and cons of using aberrant glycosylation as companion biomarkers for therapeutics in cancer  

Kang, Jeong-Gu (Division of KRIBB Strategy Projects, KRIBB)
Ko, Jeong-Heon (Division of KRIBB Strategy Projects, KRIBB)
Kim, Yong-Sam (Division of KRIBB Strategy Projects, KRIBB)
Publication Information
BMB Reports / v.44, no.12, 2011 , pp. 765-771 More about this Journal
Abstract
Cancer treatment has been stratified by companion biomarker tests that serve to provide information on the genetic status of cancer patients and to identify patients who can be expected to respond to a given treatment. This stratification guarantees better efficiency and safety during treatment. Cancer patients, however, marginally benefit from the current companion biomarker-aided treatment regimens, presumably because companion biomarker tests are dependent solely on the mutation status of several genes status quo. In the true sense of the term, "personalized medicine", cancer patients are deemed to be identified individually by their molecular signatures, which are not necessarily confined to genetic mutations. Glycosylation is tremendously dynamic and shows alterations in cancer. Evidence is accumulating that aberrant glycosylation contributes to the development and progression of cancer, holding the promise for use of glycosylation status as a companion biomarker in cancer treatment. There are, however, several challenges derived from the lack of a reliable detection system for aberrant glycosylation, and a limited library of aberrant glycosylation. The challenges should be addressed if glycosylation status is to be used as a companion biomarker in cancer treatment and contribute to the fulfillment of personalized medicine.
Keywords
Aberrant glycosylation; Cancer diagnostics; Companion biomarker;
Citations & Related Records

Times Cited By Web Of Science : 2  (Related Records In Web of Science)
Times Cited By SCOPUS : 2
연도 인용수 순위
  • Reference
1 Duverger, E., Frison, N., Roche, A. C. and Monsigny, M. (2003) Carbohydrate-lectin interactions assessed by surface plasmon resonance. Biochimie 85, 167-179.   DOI   ScienceOn
2 Ahn, H. J., Kim, Y. S., Lee, C. H., Cho, E. W., Yoo, H. S., Kim, S. H. Ko, J. H. and Kim, S. J. (2011) Generation of antibodies recognizing an aberrant glycoform of human tissue inhibitor of metalloproteinase-1 (TIMP-1) using decoy immunization and phage display. J. Biotechnol. 151, 225-230.   DOI   ScienceOn
3 Yoshida-Moriguchi, T., Yu, L., Stalnaker, S. H., Davis, S., Kunz, S., Madson, M., Oldstone, M. B., Schachter, H., Wells, L. and Campbell, K. P. (2010) O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding. Science 327, 88-92.   DOI   ScienceOn
4 Shirure, V. S., Henson, K. A., Schnaar, R. L., Nimrichter, L. and Burdick, M. M. (2011) Gangliosides expressed on breast cancer cells are E-selectin ligands. Biochem. Biophys. Res. Commun. 406, 423-429.   DOI   ScienceOn
5 Chen, G., Howe, A. G., Xu, G., Frohlich, O., Klein, J. D. and Sands, J. M. (2011) Mature N-linked glycans facilitate UT-A1 urea transporter lipid raft compartmentalization. FASEB J. In press.
6 Hollenstein, K., Dawson, R. J. and Locher, K. P. (2007) Structure and mechanism of ABC transporter proteins. Curr. Opin. Struct. Biol. 17, 412-418.   DOI   ScienceOn
7 Beretta, G. L., Benedetti, V., Cossa, G., Assaraf, Y. G., Bram, E., Gatti, L., Corna, E., Carenini, N., Colangelo, D., Howell, S. B., Zunino, F. and Perego, P. (2010) Increased levels and defective glycosylation of MRPs in ovarian carcinoma cells resistant to oxaliplatin. Biochem. Pharmacol. 79, 1108-1117.   DOI   ScienceOn
8 Leffler, H., Carlsson, S., Hedlund, M., Qian, Y. and Poirier, F. (2004) Introduction to galectins. Glycoconj. J. 19, 433-440.
9 Fred Brewer, C. (2002) Binding and cross-linking properties of galectins. Biochim. Biophys. Acta. 1572, 255-262.   DOI   ScienceOn
10 Liu, F. T. and Rabinovich GA. (2005) Galectins as modulators of tumour progression. Nat. Rev. Cancer 5, 29-41.   DOI   ScienceOn
11 Camby, I., Le Mercier, M., Lefranc, F. and Kiss, R. (2006) Galectin-1: a small protein with major functions. Glycobiology 16, 137R-157.   DOI   ScienceOn
12 Garner, O. B. and Baum, L. G. (2008) Galectin-glycan lattices regulate cell-surface glycoprotein organization and signaling. Biochem. Soc. Trans. 36, 1472-1477.   DOI   ScienceOn
13 Wu, A. M., Lisowska, E., Duk, M. and Yang, Z. (2009) Lectins as tools in glycoconjugate research. Glycoconj. J. 26, 899-913.   DOI   ScienceOn
14 Ko, J. H., Miyoshi, E., Noda, K., Ekuni, A., Kang, R., Ikeda, Y. and Taniguchi, N. (1999) Regulation of the GnT-V promoter by transcription factor Ets-1 in various cancer cell lines. J. Biol. Chem. 274, 22941-22948.   DOI
15 Dall'Olio, F. and Chiricolo, M. (2001) Sialyltransferases in cancer. Glycoconj. J. 18, 841-850.   DOI   ScienceOn
16 Cazet, A., Julien, S., Bobowski, M., Krzewinski-Recchi, M. A., Harduin-Lepers, A., Groux-Degroote, S. and Delannoy, P. (2010) Consequences of the expression of sialylated antigens in breast cancer. Carbohydr. Res. 345, 1377-1383.   DOI   ScienceOn
17 Itzkowitz, S. H., Bloom, E. J., Kokal, W. A., Modin, G., Hakomori, S. and Kim, Y. S. (1990) Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients. Cancer 66, 1960-1966.   DOI   ScienceOn
18 Ma, X. C., Terata, N., Kodama, M., Jancic, S., Hosokawa, Y. and Hattori, T. (1993) Expression of sialyl-Tn antigen is correlated with survival time of patients with gastric carcinomas. Eur. J. Cancer 29A, 1820-1823.
19 Kim, Y. S., Hwang, S. Y., Kang, H. Y., Sohn, H., Oh, S., Kim, J. Y., Yoo, J. S., Kim, Y. H., Kim, C. H., Jeon, J. H., Lee, J. M., Kang, H. A., Miyoshi, E., Taniguchi, N., Yoo, H. S. and Ko, J. H. (2008) Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1. Mol. Cell. Proteomics. 7, 1-14.   DOI
20 Burchell, J. M., Mungul, A. and Taylor-Papadimitriou, J. (2001) O-linked glycosylation in the mammary gland: changes that occur during malignancy. J. Mammary Gland Biol. Neoplasia 6, 355-364.   DOI   ScienceOn
21 Ben-David, T., Sagi-Assif, O., Meshel, T., Lifshitz, V., Yron, I. and Witz, I. P. (2008) The involvement of the sLe-a selectin ligand in the extravasation of human colorectal carcinoma cells. Immunol. Lett. 116, 218-224.   DOI   ScienceOn
22 Eberhard, D. A., Johnson, B. E., Amler, L. C., Goddard, A. D., Heldens, S. L., Herbst, R. S., Ince, W. L., Janne, P. A., Januario, T., Johnson, D. H., Klein, P., Miller, V. A., Ostland, M. A., Ramies, D. A., Sebisanovic, D., Stinson, J. A., Zhang, Y. R., Seshagiri, S. and Hillan, K. J. (2005) Mutations in the epidermal growth factor receptor and in KRAS are predictive and prognostic indicators in patients with non-small-cell lung cancer treated with chemotherapy alone and in combination with erlotinib. J. Clin. Oncol. 23, 5900-5909.   DOI   ScienceOn
23 The Food and Drug Administration (2005) Drug-Diagnostic Co-Development Concept Paper (Draft-Not for Implementation).
24 Holt, G. D. and Hart, G. W. (1986) The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J. Biol. Chem. 261, 8049-8057.
25 Wang, Z., Gucek, M. and Hart, G. W. (2008) Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. U.S.A. 105, 13793-13798.   DOI   ScienceOn
26 Roth, J. (2002) Protein N-glycosylation along the secretory pathway: relationship to organelle topography and function, protein quality control, and cell interactions. Chem. Rev. 102, 285-303.   DOI   ScienceOn
27 Maeda, Y. and Kinoshita, T. (2011) Structural remodeling, trafficking and functions of glycosylphosphatidylinositol-anchored proteins. Prog. Lipid. Res. 50, 411-424.   DOI   ScienceOn
28 Yu, R. K., Tsai, Y. T., Ariga, T. and Yanagisawa, M. (2011) Structures, biosynthesis., functions of gangliosides-an overview. J. Oleo. Sci. 60, 537-544.   DOI
29 Helenius, A. and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science 291, 2364-2369.   DOI   ScienceOn
30 Swaroop, A., Chew, E. Y., Bowes, Rickman, C. and Abecasis, G. R. (2009) Unraveling a multifactorial late-onset disease: from genetic susceptibility to disease mechanisms for age-related macular degeneration. Annu. Rev. Genomics Hum. Genet. 10, 19-43.   DOI   ScienceOn
31 Johnson, A. D. and O'Donnell, C. J. (2009) An open access database of genome-wide association results. BMC Med. Genet. 10, 6.
32 Reddy, E. P., Reynold, R. K., Santos, E. and Barbacid, M. A. (1982) A point mutation is responsible for the acquisition of transforming properties of the T24 human bladder carcinoma oncogene. Nature 300, 149-152.   DOI   ScienceOn
33 Capon, D. J., Seeburg, P. H., McGrath, J. P., Hayflick, J. S., Edman, U., Levinson, A. D. and Goeddel, D. V. (1983) Activation of Ki-ras2 gene in human colon and lung carcinomas by two different point mutations. Nature 304, 507-513.   DOI   ScienceOn
34 Bos, J. L., Toksoz, D., Marshall, C. J., Verlaan-de Vries, M., Veeneman, G. H., van der Eb, A. J., van Boom, J. H., Janssen, J. W. and Steenvoorden, A. C. (1985) Amino-acid substitutions at codon 13 of the N-ras oncogene in human acute myeloid leukaemia. Nature 315, 726-730.   DOI   ScienceOn
35 Herbst. R. S., Fukuoka, M. and Baselga, J. (2004) Gefitinib-a novel targeted approach to treating cancer. Nat. Rev. Cancer 4, 956-965.   DOI   ScienceOn
36 Lievre, A., Bachet, J. B., Boige, V., Cayre, A., Le Corre, D., Buc, E., Ychou, M., Bouche, O., Landi, B., Louvet, C., Andre, T., Bibeau, F., Diebold, M. D., Rougier, P., Ducreux, M., Tomasic, G., Emile, J. F., Penault-Llorca, F. and Laurent-Puig, P. (2008) KRAS mutations as an independent prognostic factor in patients with advanced colorectal cancer treated with cetuximab. J. Clin. Oncol. 26, 374-379.   DOI   ScienceOn
37 Amado, R. G., Wolf, M., Peeters, M., Van Cutsem, E., Siena, S., Freeman, D. J., Juan, T., Sikorski, R., Suggs, S., Radinsky, R., Patterson, S. D. and Chang, D. D. (2008) Wild-type KRAS is required for panitumumab efficacy in patients with meta-static colorectal cancer. J. Clin. Oncol. 26, 1626-1634.   DOI   ScienceOn
38 Vogel, C. L., Cobleigh, M. A., Tripathy, D., Gutheil, J. C., Harris, L. N., Fehrenbacher, L., Slamon, D. J., Murphy, M., Novotny, W. F., Burchmore, M., Shak, S., Stewart, S. J. and Press, M. (2002) Efficacy and safety of trastuzumab as a single agent in first-line treatment of HER2-overexpressing meta-static breast cancer. J. Clin. Oncol. 20, 719-726.   DOI   ScienceOn
39 Ferrara, N. (2005) VEGF as a therapeutic target in cancer. Oncology 69 (Suppl. 3), 11-16.   DOI   ScienceOn
40 Soda, M., Choi, Y. L., Enomoto, M., Takada, S., Yamashita, Y., Ishikawa, S., Fujiwara, S., Watanabe, H., Kurashina, K., Hatanaka, H., Bando, M., Ohno, S., Ishikawa, Y., Aburatani, H., Niki, T., Sohara, Y., Sugiyama, Y. and Mano, H. (2007) Identification of the transforming EML4-ALK fusion gene in non-small-cell lung cancer. Nature 448, 561-566.   DOI   ScienceOn
41 Vo, T. T. and Letai, A. (2010) BH3-only proteins and their effects on cancer. Adv. Exp. Med. Biol. 687, 49-63.   DOI
42 Liu, P., Cheng, H., Roberts, T. M. and Zhao, J. J. (2009) Targeting the phosphoinositide 3-kinase pathway in cancer. Nat. Rev. Drug Discov. 8, 627-644.   DOI   ScienceOn
43 Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., Martin, N. M., Jackson, S. P., Smith, G. C. and Ashworth, A. (2005) Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434, 917-921.   DOI   ScienceOn
44 Masamura, S., Santner, S. J., Heitjan, D. F. and Santen, R. J. (1995) Estrogen deprivation causes estradiol hypersensitivity in human breast cancer cells. J. Clin. Endocrinol. Metab. 80, 2918-2925.   DOI
45 Baxter, E. J., Scott, L. M., Campbell, P. J., East, C., Fourouclas, N., Swanton, S., Vassiliou, G. S., Bench, A. J., Boyd, E. M., Curtin, N., Scott, M. A., Erber, W. N. and Green, A. R. ; Cancer Genome Project (2005) Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 365, 1054-1061.   DOI   ScienceOn
46 World Health Organization Report (2009) Global health risks: mortality and burden of disease attributable to selected major risks.
47 Ross, J. S. and Ginsburg, G. S. (2002) Integrating diagnostics and therapeutics: revolutionizing drug discovery and patient care. Drug. Discov. Today 7, 859-864.   DOI   ScienceOn
48 Nowell, P. and Hungerford, D. (1960) A minute chromosome in human chronic granulocytic leukemia. Science 132, 1497.
49 Druker, B. J., Tamura, S., Buchdunger, E., Ohno, S., Segal, G. M., Fanning, S., Zimmermann, J. and Lydon, N. B. (1996) Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat. Med. 2, 561-566.   DOI   ScienceOn
50 Lugo, T. G., Pendergast, A. M., Muller, A. J. and Witte, O. N. (1990) Tyrosine kinase activity and transformation potency of bcr-abl oncogene products. Science 247, 1079-1082.   DOI
51 Slamon, D. J., Clark, G. M., Wong, S. G., Levin, W. J., Ullrich, A. and McGuire W. L. (1987) Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177-182.   DOI
52 Slamon, D. J., Leyland-Jones, B., Shak, S., Fuchs, H., Paton, V., Bajamonde, A., Fleming, T., Eiermann, W., Wolter, J., Pegram, M., Baselga, J. and Norton, L. (2001) Use of chemotherapy plus a monoclonal antibody against HER2 for meta-static breast cancer that overexpresses HER2. N. Engl. J. Med. 344, 783-792.   DOI   ScienceOn