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Gene Review

B3GALTL  -  beta 1,3-galactosyltransferase-like

Homo sapiens

Synonyms: B3GLCT, B3GTL, B3Glc-T, Beta-1,3-glucosyltransferase, Beta-3-glycosyltransferase-like, ...
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Disease relevance of B3GALTL

  • Recombinant proteins expressed by UG86-1 in Escherichia coli also had antigenic epitopes recognized by the other MAbs against normal GalT [1].
  • A complementary DNA (cDNA) library was constructed from a human ovarian cancer cell line, RMG-I, which secreted an amount of GAT into the culture supernatant and screened with monoclonal antibodies (MAbs) against GAT and normal GalT [1].
  • Previously, we have reported that the expression of GalT V is increased in the process of glioma [2].
  • The elevated levels of beta1,4-galactosyltransferase I (GalT I; EC are detected in highly metastatic lung cancer PGBE1 cells compared with its less metastatic partner PGLH7 cells [3].
  • GalT is deficient in galactosemia [4].

High impact information on B3GALTL

  • To mark the Golgi in HeLa cells, we stably expressed the Golgi stack enzyme N-acetylgalactosaminyltransferase-2 (GalNAc-T2) fused to the green fluorescent protein (GFP) or to an 11-amino acid epitope, VSV-G (VSV), and the trans/TGN enzyme beta1,4-galactosyltransferase (GalT) fused to GFP [5].
  • GalT was found in the trans-cisterna and trans-Golgi network but, contrary to expectation, NAGT I was found both in the medial- and trans-cisternae, overlapping the distribution of GalT [6].
  • After detection of a microdeletion by array-based comparative genomic hybridization, we identified biallelic truncating mutations in the beta 1,3-galactosyltransferase-like gene (B3GALTL) in all 20 tested patients, showing that Peters Plus is a monogenic, primarily single-mutation syndrome [7].
  • Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins [8].
  • The galactosyltransferase associated with tumor (GAT) was the name given to the isoenzyme that tends to polymerize resulting in slower moving in a nondenaturing polyacrylamide gel electrophoresis than normal (beta 1-4)galactosyltransferase (normal GalT) [1].

Chemical compound and disease context of B3GALTL


Biological context of B3GALTL

  • The B3GTL gene lacks canonical TATA and CAAT boxes and contains three functional polyadenylation sites [10].
  • The 229-base pair nucleotide sequence encoded by UG86-1 was identical to the stem region sequence of HGT832 which encodes a full-length cDNA of human GalT [1].
  • Cotransfection of the GalT I promoter/luciferase reporter and the Ets family protein E1AF expression plasmid increased the luciferase reporter activity in a dose-dependent manner [3].
  • Decreasing the GalT I surface expression by small interfering RNA or interfering with the surface of GalT I function by mutation inhibited cell adhesion on laminin, the invasive potential in vitro, and tyrosine phosphorylation of focal adhesion kinase [3].
  • Furthermore, decreasing the expression of GalT V in glioma cells promoted apoptosis, inhibited the invasion and migration and the ability of tumor formation in vivo, and reduced the activation of AKT [2].

Anatomical context of B3GALTL

  • In this study, the ectopic expression of GalT V could promote the invasion and survival of glioma cells and transformed astrocytes [2].
  • Use of GalT knockout donors markedly extends the survival of vascularized thymus plus renal xenografts in baboons [11].
  • After 24 h of treatment with 10 nM TX14(A), a 14-mer prosaptide, the specific activity of UDP-galactose:ceramide galactosyltransferase (GalT) in primary Schwann cells was increased by 150% over controls [12].
  • The membrane preparation also incorporated [(14)C]Gal into beta-(1-->4)-galactan, indicating that the membranes contained different types of GalT isoform catalyzing the synthesis of different types of galactosidic linkage [13].
  • Soluble Gal-T, purified from human breast milk, was shown to be very heterogeneous by isoelectric focusing (IEF) [14].

Associations of B3GALTL with chemical compounds

  • Gal-T1 also transfers GalNAc from UDP-GalNAc to GlcNAc, but with only approximately 0.1% of Gal-T activity [15].
  • After a 1-h nocodazole treatment, Vero alpha-2,6-sialyltransferase and GalT were found in scattered cytoplasmic patches that increased in number over time [16].
  • Here we identify the putative glycosyltransferase, B3GTL, as the beta1,3-glucosyltransferase involved in the biosynthesis of this disaccharide [17].
  • The RG-I GalT had a temperature optimum of 30 degrees C. an apparent Km for UDP-Gal and exogenous RG-I substrate of 460 +/- 40 microM and 1.1 +/- 0.1 mg ml(-1) respectively, and a Vmax of 3.0 +/- 0.5 pkat mg(-1) protein [18].
  • Using two-step discontinuous sucrose step gradients, galactosyltransferase (GalT) activity that synthesized 70%-methanol-insoluble products from UDP-[(14)C]Gal was detected in both the 0.5 M sucrose fraction and the 0.25/1.1 M sucrose interface [19].

Other interactions of B3GALTL

  • On the other hand, the catalytic constant (k(cat)) in the Gal-T reaction is comparable with the wild type, whereas it is 3-5-fold higher in the GalNAc-T reaction [15].
  • cDNAs, encoding human beta1,4-galactosyltransferase (hGalT I, EC, human Galbeta1,3(4)-GlcNAc alpha2,3-sialyltransferase (hST3GalIII, EC 2.4.99), and human Galbeta1,4-GlcNAc alpha2,6-sialyltransferase (hST6Gal I, EC, were cloned from human cell lines [20].

Analytical, diagnostic and therapeutic context of B3GALTL


  1. Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. Uejima, T., Uemura, M., Nozawa, S., Narimatsu, H. Cancer Res. (1992) [Pubmed]
  2. Beta1,4-galactosyltransferase V functions as a positive growth regulator in glioma. Jiang, J., Chen, X., Shen, J., Wei, Y., Wu, T., Yang, Y., Wang, H., Zong, H., Yang, J., Zhang, S., Xie, J., Kong, X., Liu, W., Gu, J. J. Biol. Chem. (2006) [Pubmed]
  3. Elevated beta1,4-galactosyltransferase I in highly metastatic human lung cancer cells. Identification of E1AF as important transcription activator. Zhu, X., Jiang, J., Shen, H., Wang, H., Zong, H., Li, Z., Yang, Y., Niu, Z., Liu, W., Chen, X., Hu, Y., Gu, J. J. Biol. Chem. (2005) [Pubmed]
  4. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Brenner, C. Biochemistry (2002) [Pubmed]
  5. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. Storrie, B., White, J., Röttger, S., Stelzer, E.H., Suganuma, T., Nilsson, T. J. Cell Biol. (1998) [Pubmed]
  6. Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. Nilsson, T., Pypaert, M., Hoe, M.H., Slusarewicz, P., Berger, E.G., Warren, G. J. Cell Biol. (1993) [Pubmed]
  7. Peters Plus syndrome is caused by mutations in B3GALTL, a putative glycosyltransferase. Lesnik Oberstein, S.A., Kriek, M., White, S.J., Kalf, M.E., Szuhai, K., den Dunnen, J.T., Breuning, M.H., Hennekam, R.C. Am. J. Hum. Genet. (2006) [Pubmed]
  8. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Brenner, C., Garrison, P., Gilmour, J., Peisach, D., Ringe, D., Petsko, G.A., Lowenstein, J.M. Nat. Struct. Biol. (1997) [Pubmed]
  9. Down-regulation of the expression of beta1,4-galactosyltransferase V promotes integrin beta1 maturation. Chen, X., Jiang, J., Yang, J., Chen, C., Sun, M., Wei, Y., Guang, X., Gu, J. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  10. A novel human glycosyltransferase: primary structure and characterization of the gene and transcripts. Heinonen, T.Y., Pasternack, L., Lindfors, K., Breton, C., Gastinel, L.N., Mäki, M., Kainulainen, H. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  11. Life-supporting pig-to-baboon renal transplantation using GalT knockout donors: Benefit of cotransplanting a vascularized donor thymic graft. Yamada, K. Kidney Int. (2005) [Pubmed]
  12. Prosaposin: a myelinotrophic protein that promotes expression of myelin constituents and is secreted after nerve injury. Hiraiwa, M., Campana, W.M., Mizisin, A.P., Mohiuddin, L., O'Brien, J.S. Glia (1999) [Pubmed]
  13. In vitro biosynthesis of galactans by membrane-bound galactosyltransferase from radish ( Raphanus sativus L.) seedlings. Kato, H., Takeuchi, Y., Tsumuraya, Y., Hashimoto, Y., Nakano, H., Kovác, P. Planta (2003) [Pubmed]
  14. Recombinant soluble beta-1,4-galactosyltransferases expressed in Saccharomyces cerevisiae. Purification, characterization and comparison with human enzyme. Malissard, M., Borsig, L., Di Marco, S., Grütter, M.G., Kragl, U., Wandrey, C., Berger, E.G. Eur. J. Biochem. (1996) [Pubmed]
  15. Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity. Ramakrishnan, B., Qasba, P.K. J. Biol. Chem. (2002) [Pubmed]
  16. Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins. Yang, W., Storrie, B. Mol. Biol. Cell (1998) [Pubmed]
  17. Identification and Characterization of abeta1,3-Glucosyltransferase That Synthesizes the Glc-beta1,3-Fuc Disaccharide on Thrombospondin Type 1 Repeats. Kozma, K., Keusch, J.J., Hegemann, B., Luther, K.B., Klein, D., Hess, D., Haltiwanger, R.S., Hofsteenge, J. J. Biol. Chem. (2006) [Pubmed]
  18. Solubilization of rhamnogalacturonan I galactosyltransfrases from membranes of a flax cell suspension. Peugnet, I., Goubet, F., Bruyant-Vannier, M.P., Thoiron, B., Morvan, C., Schols, H.A., Voragen, A.G. Planta (2001) [Pubmed]
  19. Subcellular localization and topology of beta(1-->4)galactosyltransferase that elongates beta(1-->4)galactan side chains in rhamnogalacturonan I in potato. Geshi, N., Jørgensen, B., Ulvskov, P. Planta (2004) [Pubmed]
  20. High-level expression of human glycosyltransferases in insect cells as biochemically active form. Kim, H.G., Yang, S.M., Lee, Y.C., Do, S.I., Chung, I.S., Yang, J.M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  21. Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells. Mackenzie, J.M., Jones, M.K., Westaway, E.G. J. Virol. (1999) [Pubmed]
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