Murine β1,4-Galactosyltransferase

Analysis of a Gene That Serves Both A Housekeeping and a Cell Specific Function
  • Joel H. Shaper
  • Anne Harduin-Lepers
  • Bhanu Rajput
  • Nancy L. Shaper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 376)


Glycoconjugates (glycolipids and glycoproteins) are a major class of biomolecules found on the cell surface of essentially all cells and tissues. A remarkable and somewhat bewildering number of different oligosaccharide structures (glycans) have been isolated and characterized from glycoconjugates. Because of this remarkable structural diversity, oligosaccharide structures have long been considered ideal candidates for information-containing molecules which can mediate intercellular communication and recognition or alternatively, communication between a cell and its environment. Indeed, ordered, sequential changes in the expression of specific glycan structures at the cell surface may provide an important mechanism for controlling cell-cell behavior and fate during development. During early murine embryogenesis, temporal changes in cell surface glycosylation patterns (stage specific antigens) have been documented using monoclonal antibodies that are specific for defined glycan structures (reviewed in 1).


Mammary Gland Start Site Transcriptional Start Site Somatic Tissue Male Germ Cell 
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  1. 1.
    Fenderson, B.A., Eddy, E.M., and Hakomori, S., 1990, Glycoconjugate expression during embryogenesis and its biological significance, BioEssays 12:173–179.PubMedCrossRefGoogle Scholar
  2. 2.
    Bleil, J.D., and Wassarman, P.M., 1988, Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein’s sperm receptor activity, Proc. Natl. Acad. Sci. USA 85:6778–6782.PubMedCrossRefGoogle Scholar
  3. 3.
    Cheng, A., Le, T., Palacios, M., Bookbinder, L.H., Wassarman, P.M., Suzuki, F., and Bleil, J.D., 1994, Sperm-egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3, J. Cell Biol. 125:867–878.PubMedCrossRefGoogle Scholar
  4. 4.
    Varki, A., 1993, Biological roles of disaccharides: all of the theories are correct, Glycobiology 3:97–130.PubMedCrossRefGoogle Scholar
  5. 5.
    Singhal, A., and Hakomori, S., 1990, Molecular changes in carbohydrate antigens associated with cancer, BioEssays 12:223–230.PubMedCrossRefGoogle Scholar
  6. 6.
    Axford, J.S., Lydyard, P.M., Isenberg, D.A., Mackenzie, L., Hay, F.C., and Roitt, I.V., 1987, Reduced B-cell galactosyltransferase activity in rheumatoid arthritis, Lancet (Dec. 26): 1486–1488.Google Scholar
  7. 7.
    Parekh, R.B., Dwek, R.A., Sutton, B.J., Fernandes, D.L., Leung, A., Stanworth, D., and Rademacher, T.W., 1985, Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG, Nature 316:452–457.PubMedCrossRefGoogle Scholar
  8. 8.
    Schachter, H., 1991, Enzymes associated with glycosylation, Curr. Opin. Struc. Biol. 1:755–765.CrossRefGoogle Scholar
  9. 9.
    Beyer, T.A., and Hill, R.L., 1982, Glycosylation pathway in the biosynthesis of nonreducing terminal sequences in oligosaccharides of glycoproteins, in Horowitz, M. (ed.), The Glycoconjugates Vol. III, Academic Press, New York, pp. 25–45.Google Scholar
  10. 10.
    Hollis, G.F., Douglas, J.G., Shaper, N.L., and Shaper, J.H., 1989, Genomic structure of murine β1,4-galactosyltransferase, Biochem. Biophys. Res. Comm. 162:1069–1075.PubMedCrossRefGoogle Scholar
  11. 11.
    Joziasse, D.H., Shaper, N.L., Kim, D., Van den Eijnden, D.H., and Shaper, J.H., 1992, Murine α1,3-galactosyltransferase: a single gene locus specifies four isoforms of the enzyme by alternative splicing, J. Biol. Chem. 267:5534–5541.PubMedGoogle Scholar
  12. 12.
    Joziasse, D.H., 1993, Mammalian glycosyltransferases: genomic organization and protein structure, Curr. Opin. Struct. Biol. 3:271–277.Google Scholar
  13. 13.
    Brodbeck, V., Denton, W.L., Tanahashi, N., and Ebner, K.E., 1967, The isolation and identification of the β protein of lactose synthetase as α-lactalbumin, J. Biol. Chem. 242:1391–1397.PubMedGoogle Scholar
  14. 14.
    Turkington, R.W., Brew, K., Vanaman, T.C., and Hill, R.L., 1968, The hormonal control of lactose synthetase in the developing mouse mammary gland, J. Biol. Chem. 243:3382–3387.PubMedGoogle Scholar
  15. 15.
    Brew, K., 1970, Lactose synthetase: evolutionary origins, structure and control, Essays in Biochem. 6:93–118.Google Scholar
  16. 16.
    Nitta, K., and Sugai, S., 1989, The evolution of lysozyme and α-lactalbumin, Eur. J. Biochem. 182:111–118.PubMedCrossRefGoogle Scholar
  17. 17.
    Shur, B.D., 1993, Glycosyltransferases as cell adhesion molecules, Curr. Opin. Cell Biol. 5:854–863.PubMedCrossRefGoogle Scholar
  18. 18.
    Taatjes, D.J., Roth, J., Weinstein, J., and Paulson, J.C., 1988, Post-golgi apparatus localization and regional expression of rat intestinal sialyltransferase detected by immunoelectron microscopy with polypeptide epitope-purified antibody, J. Biol. Chem. 263:6302–6309.PubMedGoogle Scholar
  19. 19.
    Taatjes, D.J., Roth, J., Shaper, N.L., and Shaper, J.H., 1992, Immunocytochemical localization of β1,4-galactosyltransferase in epithelial cells from bovine tissues using monoclonal antibodies, Glycobiology 2:579–589.PubMedCrossRefGoogle Scholar
  20. 20.
    Roseman, S., 1970, The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intracellular adhesion, Chem. Phys. Lipids 5:270–297.PubMedCrossRefGoogle Scholar
  21. 21.
    Powell, J.T., and Brew, K., 1976, Metal ion inactivation of galactosyltransferase, J. Biol. Chem. 251:3645–3652.PubMedGoogle Scholar
  22. 22.
    Shaper, N.L., Shaper, J.H., Peyser, M., and Kozak, C.A., 1990, Localization of the gene for β1,4-galactosyltransferase to a position in the centromeric region of mouse chromosome 4, Cytogenet Cell Genet. 54:172–174.PubMedCrossRefGoogle Scholar
  23. 23.
    Hollis, G.F., Douglas, J.G., Shaper, N.L., and Shaper, J.H., 1989, Genomic structure of murine β1,4-galactosyltransferase, Biochem. Biophys. Res. Comm. 162:1069–1075.PubMedCrossRefGoogle Scholar
  24. 24.
    Shaper, N.L., Hollis, G.F., Douglas, J.G., Kirsch, I.R., and Shaper, J.H., 1988, Characterization of the full-length cDNA for murine β1,4-galactosyltransferase: novel features at the 5’ end predict two translational start sites at two in-frame AUGs, J. Biol. Chem. 263:10420–10428.PubMedGoogle Scholar
  25. 25.
    Russo, R.N., Shaper, N.L., and Shaper, J.H., 1990, Bovine β1→4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino terminal domains-in vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins, J. Biol. Chem. 265:3324–3331.PubMedGoogle Scholar
  26. 26.
    Shaper, N.L., Wright, W.W., and Shaper, J.H., 1990, Murine β1,4-galactosyltransferase: both the amounts and structure of the mRNA are regulated during spermatogenesis, Proc. Natl. Acad. Sci. USA 87:791–795.PubMedCrossRefGoogle Scholar
  27. 27.
    Harduin-Lepers, A., Shaper, N.L., Mahoney, J.A., and Shaper, J.H., 1992, Murine β1,4-galactosyltransferase: round spermatid transcripts are characterized by an extended 5’-untranslated region, Glycobiology 2:361–368.PubMedCrossRefGoogle Scholar
  28. 28.
    Shaper, N.L., Harduin-Lepers, A., and Shaper, J.H., 1994, Male germ cell expression of murine β4-galactosyltransferase-A 796-base pair genomic region, containing two cAMP-responsive element (CRE)-like elements, mediates male germ cell-specific expression in transgenic mice, J. Biol. Chem. 269:25165–25171.PubMedGoogle Scholar
  29. 29.
    Harduin-Lepers, A., Shaper, J.H., and Shaper, N.L., 1993, Characterization of two cis-regulatory regions in the murine β1,4-galactosyltransferase gene: evidence for a negative regulatory element that controls initiation at the proximal site, J. Biol. Chem. 268:14348–14359.PubMedGoogle Scholar
  30. 30.
    Saffer, J.D., Jackson, S.P., and Annarella, M.B., 1991, Developmental expression of Sp1 in the mouse, Mol. Cell. Biol. 11:2189–2199.PubMedGoogle Scholar
  31. 31.
    Vilotte, J-L., and Soulier, S., 1992, Isolation and characterization of the mouse α-lactalbumin-encoding gene: interspecies comparison, tissue- and stage-specific expression, Gene 119:287–292.PubMedCrossRefGoogle Scholar
  32. 32.
    Kozak, M., 1992, Translational regulation, Ann. Rev. Cell Biol. 8:197–225.PubMedCrossRefGoogle Scholar
  33. 33.
    Bellve, A.R., Cavicchia, J.C., Millette, C.F., O’Brien, D.A., Bhatnagar, Y.M., and Dym, M., 1977, Spermatogenic cells of the prepuberal mouse-Isolation and morphological characterization, J. Cell Biol. 74:68–85.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Joel H. Shaper
    • 1
    • 2
  • Anne Harduin-Lepers
    • 1
  • Bhanu Rajput
    • 1
  • Nancy L. Shaper
    • 1
  1. 1.Department of Pharmacology and Molecular SciencesSchool of Medicine, The Johns Hopkins UniversityBaltimoreUSA
  2. 2.Cell Structure and Function Laboratory, The Oncology CenterSchool of Medicine, The Johns Hopkins UniversityBaltimoreUSA

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