Abstract
β-Galactoside α2,6-sialyltransferase (ST6Gal.I) is the principal sialyltransferase responsible for the biosynthesis of the sialyl α2,6-galactosyl linkage. This enzyme and its cognate glycosidic structure are overexpressed in several malignancies and are related to cancer progression. The expression of the enzyme is regulated primarily through the expression of three principal mRNA species differing in the 5′-untranslated exons. The form known as YZ is considered associated with the basal expression of the gene, while forms H and X are specific to the liver and B-lymphocytes, respectively. The authors have studied the expression of ST6Gal.I activity by two different methods using a panel of human cancer cell lines: the expression of α2,6-sialylated sugar chains by the lectin from Sambucus nigra (SNA), and the expression of the different mRNA species by RT-PCR using oligonucleotide primers complementary to the isoform-specific regions. Very high levels of ST6Gal.I activity result in high levels of SNA reactivity and are associated with the expression of the H transcript in colon and liver cell lines, and of the X transcript in B cells.
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References
Tsuji, S., Datta, A. K., and Paulson, J. C. (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6, v–vii.
Weinstein, J., de Souza e Silva, U., and Paulson, J. C. (1982) Purification of a Gal β 1,4GlcNAc α 2,6 sialyltransferase and a Gal α 1,3(4)GlcNAc α 2,3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem. 257, 13,835–13,844.
Weinstein, J., Lee, E. U., McEntee, K., Lai, P. H., and Paulson, J. C. (1987) Primary structure of β-galactoside α 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. J. Biol. Chem. 262, 17,735–17,743.
Takashima, S., Tsuji, S., and Tsujimoto, M. (2002) Characterization of the second type of human β-galactoside α2,6-sialyltransferase (ST6Gal II), which sialylates Galβ1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes. J. Biol. Chem. 277, 45,719–45,728.
Dall’Olio, F. and Trere, D. (1993) Expression of α 2,6-sialylated sugar chains in normal and neoplastic colon tissues. detection by digoxigenin-conjugated Sambucus nigra agglutinin. Eur. J. Histochem. 37, 257–265.
Sata, T., Roth, J., Zuber, C., Stamm, B., and Heitz, P. U. (1991) Expression of α 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins. Am. J. Pathol. 139, 1435–1448.
Dall’Olio, F., Malagolini, N., Di Stefano, G., Minni, F., Marrano, D., and Serafini-Cessi, F. (1989) Increased CMP-NeuAc:Galβ1,4GlcNAc-R α 2,6 sialyltransferase activity in human colorectal cancer tissues. Int. J. Cancer 44, 434–439.
Dall’Olio, F., Chiricolo, M., and Lau, J. T. (1999) Differential expression of the hepatic transcript of β-galactoside α2,6-sialyltransferase in human colon cancer cell lines. Int. J. Cancer 81, 243–247.
Dall’Olio, F., Chiricolo, M., Ceccarelli, C., Minni, F., Marrano, D., and Santini, D. (2000) β-galactoside α2,6 sialyltransferase in human colon cancer: contribution of multiple transcripts to regulation of enzyme activity and reactivity with Sambucus nigra agglutinin. Int. J. Cancer 88, 58–65.
Dall’Olio, F., Chiricolo, M., D’Errico, A., et al. (2004) Expression of β-galactoside α2,6 sialyltransferase and of α2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis. Glycobiology 14, 39–49.
Dalziel, M., Dall’Olio, F., Mungul, A., Piller, V., and Piller, F. (2004) Ras oncogene induces β-galactoside α2,6-sialyltransferase (ST6Gal I) via a RalGEF-mediated signal to its housekeeping promoter. Eur. J. Biochem. 271, 3623–3634.
Gessner, P., Riedl, S., Quentmaier, A., and Kemmner, W. (1993) Enhanced activity of CMP-neuAc:Gal β 1-4GlcNAc:α 2,6-sialyltransferase in metastasizing human colorectal tumor tissue and serum of tumor patients. Cancer Lett. 75, 143–149.
Lise, M., Belluco, C., Perera, S. P., Patel, R., Thomas, P., and Ganguly, A. (2000) Clinical correlations of α2,6-sialyltransferase expression in colorectal cancer patients. Hybridoma 19, 281–286.
Petretti, T., Schulze, B., Schlag, P. M., and Kemmner, W. (1999) Altered mRNA expression of glycosyltransferases in human gastric carcinomas. Biochim. Biophys. Acta 1428, 209–218.
Recchi, M. A., Hebbar, M., Hornez, L., Harduin-Lepers, A., Peyrat, J. P., and Delannoy, P. (1998) Multiplex reverse transcription polymerase chain reaction assessment of sialyltransferase expression in human breast cancer. Cancer Res. 58, 4066–4070.
Dall’Olio, F. (2000) The sialyl-α2,6-lactosaminyl-structure: biosynthesis and functional role. Glycoconj. J. 17, 669–676.
Dall’Olio, F. and Chiricolo, M. (2001) Sialyltransferases in cancer. Glycoconj. J. 18, 841–850.
Dall’Olio, F., Malagolini, N., and Serafini-Cessi, F. (1992) Enhanced CMP-NeuAc: Gal β 1,4GlcNAc-R α 2,6 sialyltransferase activity of human colon cancer xenografts in athymic nude mice and of xenograft-derived cell lines. Int. J. Cancer 50, 325–330.
Vierbuchen, M. J., Fruechtnicht, W., Brackrock, S., Krause, K. T., and Zienkiewicz, T. J. (1995) Quantitative lectin-histochemical and immunohistochemical studies on the occurrence of α(2,3)-and α(2,6)-linked sialic acid residues in colorectal carcinomas. Relation to clinicopathologic features. Cancer 76, 727–735.
Wang, X., Vertino, A., Eddy, R. L., et al. (1993) Chromosome mapping and organization of the human β-galactoside α 2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells. J. Biol. Chem. 268, 4355–4361.
Grundmann, U., Nerlich, C., Rein, T., and Zettlmeissl, G. (1990) Complete cDNA sequence encoding human β-galactoside α-2,6-sialyltransferase. Nucleic Acids Res. 18, 667.
Stamenkovic, I., Asheim, H. C., Deggerdal, A., Blomhoff, H. K., Smeland, E. B., and Funderud, S. (1990) The B cell antigen CD75 is a cell surface sialytransferase. J. Exp. Med. 172, 641–643.
Aas-Eng, D. A., Asheim, H. C., Deggerdal, A., Smeland, E., and Funderud, S. (1995) Characterization of a promoter region supporting transcription of a novel human β-galactoside α-2,6-sialyltransferase transcript in HepG2 cells. Biochim. Biophys. Acta 1261, 166–169.
Shibuya, N., Goldstein, I. J., Broekaert, W. F., Nsimba-Lubaki, M., Peeters, B., and Peumans, W. J. (1987) The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(α 2-6)Gal/GalNAc sequence. J. Biol. Chem. 262, 1596–1601.
Dall’Olio, F., Malagolini, N., Di Stefano, G., Ciambella, M., and Serafini-Cessi, F. (1991) α 2,6 sialylation of N-acetyllactosaminic sequences in human colorectal cancer cell lines. Relationship with non-adherent growth. Int. J. Cancer 47, 291–297.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275.
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Dall’Olio, F., Malagolini, N., Chiricolo, M. (2006). β-Galactoside α2,6-Sialyltransferase and the Sialyl α2,6-Galactosyl-Linkage in Tissues and Cell Lines. In: Brockhausen, I. (eds) Glycobiology Protocols. Methods in Molecular Biology, vol 347. Humana Press. https://doi.org/10.1385/1-59745-167-3:157
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DOI: https://doi.org/10.1385/1-59745-167-3:157
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