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Gene Review

St6gal1  -  beta galactoside alpha 2,6...

Mus musculus

Synonyms: AW742324, Alpha 2,6-ST 1, Beta-galactoside alpha-2,6-sialyltransferase 1, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, ST6Gal I, ...
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Disease relevance of St6gal1


High impact information on St6gal1

  • Here we report that mice deficient in both CD22 and its ligand (Cd22-/- St6gal1-/- mice) showed restored B cell receptor (BCR) signaling, suggesting that the suppressed signaling of St6gal1-/- cells is mediated through CD22 [6].
  • Coincident with suppressed BCR signaling, B cells lacking ST6Gal I showed a net redistribution of the BCR to clathrin-rich microdomains containing most of the CD22, resulting in a twofold increase in the localization of CD22 together with the BCR [6].
  • Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands [7].
  • Deficiency of ST6Gal was further found to alter phosphotyrosine accumulation during signal transduction from the B lymphocyte antigen receptor [8].
  • When the levels of glycoprotein glycosyltransferases of the cells were examined, the level of sialyltransferase (CMP-N-acetylneuraminytransferase,EC of the cells grown at the restrictive temperature was low compared with that of cells grown at the permissive temperature [3].

Chemical compound and disease context of St6gal1


Biological context of St6gal1


Anatomical context of St6gal1


Associations of St6gal1 with chemical compounds

  • Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation [18].
  • We previously reported that BACE1 cleaved rat beta-galactoside alpha2,6-sialyltransferase (ST6Gal I) that was overexpressed in COS cells and that the NH(2) terminus of ST6Gal I secreted from the cells (E41 form) was Glu(41) [1].
  • This general increase in alpha2,6 sialylation on all glycoproteins is due to the increased activity of the galactoside:alpha2,6 sialyltransferase (ST6Gal I), which specifically transfers Neu5Ac residues in alpha2,6 linkage to Gal beta1,4GlcNAc units on N-glycans [19].
  • The identity of this enzyme was confirmed by construction of a recombinant sialyltransferase in which the NH2-terminal part including the cytoplasmic tail, signal-anchor domain and stem region was replaced with an immuno-globulin signal sequence [21].
  • Enzymatic assays indicate that the best acceptor substrate of ST6Gal II was the free disaccharide Galbeta1-4GlcNAc structure whereas ST6Gal I preferred Galbeta1-4GlcNAc-R disaccharide sequence linked to a protein [14].

Other interactions of St6gal1

  • Here we examine the cell type-specific expression of terminal glycans in tissues of normal mice in comparison with animals deficient in ST6Gal-I (transfers alpha2-6-linked sialic acid to Galbeta1-4GlcNAc) or ST3Gal-I (transfers alpha2-3-linked sialic acid to Galbeta1-3GalNAc) [18].
  • Recombinant ST6Gal II exhibited alpha2,6-sialyltransferase activity toward oligosaccharides that have the Galbeta1,4GlcNAc sequence at the nonreducing end of their carbohydrate groups, but it exhibited relatively low and no activity toward some glycoproteins and glycolipids, respectively [12].
  • Mouse gene knockout studies have provided unimpeachable evidence of immune-relevant functions for several sialyltransferase enzymes including ST6Gal I, ST3Gal I, and ST3Gal IV [22].
  • In particular, transfection of codon 12 point mutated H-Ras increases CMP-Neu5Ac: Galbeta1,4GlcNAc alpha2,6-sialyltransferase I (ST6Gal I) activity in rodent fibroblasts [15].
  • We have disrupted the gene encoding GD3 synthase (GD3S), a sialyltransferase expressed in the CNS that is responsible for the synthesis of b-series gangliosides [23].

Analytical, diagnostic and therapeutic context of St6gal1


  1. In vivo cleavage of alpha2,6-sialyltransferase by Alzheimer beta-secretase. Kitazume, S., Nakagawa, K., Oka, R., Tachida, Y., Ogawa, K., Luo, Y., Citron, M., Shitara, H., Taya, C., Yonekawa, H., Paulson, J.C., Miyoshi, E., Taniguchi, N., Hashimoto, Y. J. Biol. Chem. (2005) [Pubmed]
  2. Surfaces of murine lymphocyte subsets differ in sialylation states and antigen distribution of a major N-linked penultimate saccharide structure. Whiteheart, S.W., McLenithan, J.C., Hart, G.W. Cell. Immunol. (1990) [Pubmed]
  3. Alterations in surface glycoproteins and level of sialyltransferase of cells transformed by a temperature-sensitive mutant of simian virus 40. Onodera, K., Yamaguchi, N., Kuchino, T., Aoi, Y. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  4. A correlation between cell surface sialyltransferase, sialic acid, and glycosidase activities and the implantability of B16 murine melanoma. Dobrossy, L., Pavelic, Z.P., Bernacki, R.J. Cancer Res. (1981) [Pubmed]
  5. Inhibition of experimental pulmonary metastasis of mouse colon adenocarcinoma 26 sublines by a sialic acid:nucleoside conjugate having sialyltransferase inhibiting activity. Kijima-Suda, I., Miyamoto, Y., Toyoshima, S., Itoh, M., Osawa, T. Cancer Res. (1986) [Pubmed]
  6. Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling. Collins, B.E., Smith, B.A., Bengtson, P., Paulson, J.C. Nat. Immunol. (2006) [Pubmed]
  7. Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands. Ellies, L.G., Ditto, D., Levy, G.G., Wahrenbrock, M., Ginsburg, D., Varki, A., Le, D.T., Marth, J.D. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Immune regulation by the ST6Gal sialyltransferase. Hennet, T., Chui, D., Paulson, J.C., Marth, J.D. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  9. Correlation of retinoic acid-enhanced sialyltransferase activity and glycosylation of specific cell surface sialoglycoproteins with growth inhibition in a murine melanoma cell system. Lotan, R., Lotan, D., Meromsky, L. Cancer Res. (1984) [Pubmed]
  10. Alterations of cell surface carbohydrates and inhibition of metastatic property of murine melanomas by alpha 1,3 galactosyltransferase gene transfection. Gorelik, E., Duty, L., Anaraki, F., Galili, U. Cancer Res. (1995) [Pubmed]
  11. Stimulation of sialyltransferase activity of melanoma cells by retinoic acid. Deutsch, V., Lotan, R. Exp. Cell Res. (1983) [Pubmed]
  12. Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II. Takashima, S., Tsuji, S., Tsujimoto, M. J. Biochem. (2003) [Pubmed]
  13. Molecular cloning and genomic analysis of mouse Galbeta1, 3GalNAc-specific GalNAc alpha2,6-sialyltransferase. Kurosawa, N., Inoue, M., Yoshida, Y., Tsuji, S. J. Biol. Chem. (1996) [Pubmed]
  14. Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II. Krzewinski-Recchi, M.A., Julien, S., Juliant, S., Teintenier-Lelièvre, M., Samyn-Petit, B., Montiel, M.D., Mir, A.M., Cerutti, M., Harduin-Lepers, A., Delannoy, P. Eur. J. Biochem. (2003) [Pubmed]
  15. Ras oncogene induces beta-galactoside alpha2,6-sialyltransferase (ST6Gal I) via a RalGEF-mediated signal to its housekeeping promoter. Dalziel, M., Dall'Olio, F., Mungul, A., Piller, V., Piller, F. Eur. J. Biochem. (2004) [Pubmed]
  16. Differential expression of mRNAs for sialyltransferase isoenzymes induced in the hippocampus of mouse following kindled seizures. Okabe, A., Tawara, Y., Masa, T., Oka, T., Machida, A., Tanaka, T., Matsuhashi, H., Shiosaka, S., Kato, K. J. Neurochem. (2001) [Pubmed]
  17. Mouse beta-galactoside alpha 2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression. Kono, M., Ohyama, Y., Lee, Y.C., Hamamoto, T., Kojima, N., Tsuji, S. Glycobiology (1997) [Pubmed]
  18. Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation. Martin, L.T., Marth, J.D., Varki, A., Varki, N.M. J. Biol. Chem. (2002) [Pubmed]
  19. Increased alpha2,6 sialylation of N-glycans in a transgenic mouse model of hepatocellular carcinoma. Pousset, D., Piller, V., Bureaud, N., Monsigny, M., Piller, F. Cancer Res. (1997) [Pubmed]
  20. The sialyltransferase ST3Gal-I is not required for regulation of CD8-class I MHC binding during T cell development. Kao, C., Sandau, M.M., Daniels, M.A., Jameson, S.C. J. Immunol. (2006) [Pubmed]
  21. Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain. Lee, Y.C., Kurosawa, N., Hamamoto, T., Nakaoka, T., Tsuji, S. Eur. J. Biochem. (1993) [Pubmed]
  22. Sialyltransferase mRNA abundances in B cells are strictly controlled, correlated with cognate lectin binding, and differentially responsive to immune signaling in vitro. Marino, J.H., Hoffman, M., Meyer, M., Miller, K.S. Glycobiology (2004) [Pubmed]
  23. Mice expressing only monosialoganglioside GM3 exhibit lethal audiogenic seizures. Kawai, H., Allende, M.L., Wada, R., Kono, M., Sango, K., Deng, C., Miyakawa, T., Crawley, J.N., Werth, N., Bierfreund, U., Sandhoff, K., Proia, R.L. J. Biol. Chem. (2001) [Pubmed]
  24. Quantitative analysis of expression of mouse sialyltransferase genes by competitive PCR. Takashima, S., Tachida, Y., Nakagawa, T., Hamamoto, T., Tsuji, S. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
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