• Nancy L. Shaper
  • Joel H. Shaper


The enzyme β4-galactosyltransferase-I (β4GalT-I; UDP-Gal:GlcNAc β4-galactosyltransferase; EC is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that is widely distributed in vertebrates. The protein domain structure established for β4GalT-I consists of: (1) a short NH2-terminal cytoplasmic domain of 11 or 24 amino acids depending on the protein isoform (Shaper et al. 1988; Russo et al. 1990); (2) a large COOH-terminal luminal domain containing the catalytic center (~270 amino acids) linked to a single transmembrane domain (19 amino acids) through a glycosylated peptide segment (~86 amino acids) termed the stem region. In essentially all vertebrate tissues, the primary function of β4GalT-I is to catalyze the transfer of Gal from UDP-Gal to GlcNAcβ-R, forming the N-acetyllactosamine (Galβ1-4GlcNAcβ1-R) or poly-N-acetyllactosamine structures assembled on glycoconjugates.


Mammary Gland Round Spermatid Stem Region Acceptor Substrate Golgi Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Asano M, Furukawa K, Kido M, Matsumoto S, Umesaki Y (1997) Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. EMBO J 16:1850–1855PubMedCrossRefGoogle Scholar
  2. Andrews P (1970) Purification of lactose synthetase A protein from human milk and demonstration of its interaction with α-lactalbumin. FEBS Lett 9:297–300PubMedCrossRefGoogle Scholar
  3. Barker R, Olsen KW, Shaper JH, Hill RL (1972) Agarose derivatives of uridine diphosphate and N-acetylglucosamine for the purification of a galactosyltransferase. J Biol Chem 247:7135–7147PubMedGoogle Scholar
  4. Bendiak B, Ward LD, Simpson RJ (1993) Proteins of the Golgi apparatus: purification to homogeneity, N-terminal sequence, and unusually large Stokes radius of the membrane-bound form of UDP-galactose:N-acetylglucosamine β1-4galactosyltrans-ferase from rat liver. Eur J Biochem 216:405–417PubMedCrossRefGoogle Scholar
  5. Brew K, Vanaman TC, Hill RL (1968) The role of α-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Proc Natl Acad Sci USA 59:491–497PubMedCrossRefGoogle Scholar
  6. Brodbeck U, Ebner KE (1966) Resolution of a soluble lactose synthetase into two protein components and solubilization of microsomal lactose synthetase. J Biol Chem 241:1391–1397Google Scholar
  7. Charron M, Shaper JH, Shaper NL (1998) The increased level of β1,4-galactosyltransferase required for lactose biosynthesis is achieved in part by translational control. Proc Natl Acad Sci USA 95:14805–14810PubMedCrossRefGoogle Scholar
  8. Charron M, Shaper NL, Rajput B, Shaper JH (1999) A novel 14-base-pair regulatory element is essential for in vivo expression of murine β4-galactosyltransferase-l in late pachytene spermatocytes and round spermatids. Mol Cell Biol 19:5823–5832PubMedGoogle Scholar
  9. Chung SJ, Takayama S, Wong C-H (1998) Acceptor substrate-based selective inhibition of galactosyltransferases. Bioorg Med Chem Lett 8:3359–3364PubMedCrossRefGoogle Scholar
  10. Ebner KE, Mawal R, Fitzgerald DK, Colvin B (1972) Lactose synthetase (UDP-D-galactose:acceptor β-4-galactosyltransferase) from bovine milk. Methods Enzymol 28:500–510CrossRefGoogle Scholar
  11. Fleischer B, Mclntyre JO, Kempner ES (1993) Target sizes of galactosyltransferase, sialyltransferase, and uridine diphosphatase in Golgi apparatus of rat liver. Biochemistry 32:2076–2081PubMedCrossRefGoogle Scholar
  12. Gastinel LN, Cambillau C, Bourne Y (1999) Crystal structures of the bovine β4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J 18:3546–3557PubMedCrossRefGoogle Scholar
  13. Grobler JA, Rao KR, Pervaiz S, Brew K (1994) Protein sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme α-lactalbumin superfamily. Arch Biochem Biophys 313:360–366PubMedCrossRefGoogle Scholar
  14. Harduin-Lepers A, Shaper NL, Mahoney JA, Shaper JH (1992) Murine β1,4 galactosyltransferase: round spermatid transcripts are characterized by an extended 5′-untranslated region. Glycobiology 2:361–368PubMedCrossRefGoogle Scholar
  15. Hashimoto H, Endo T, Kajihara Y (1997) Synthesis of the first tricomponent bisubstrate analog that exhibits potent inhibition against GlcNAc: β-1,4-galactosyltransferase. J Org Chem 62:1914–1915PubMedCrossRefGoogle Scholar
  16. Lo N-W, Shaper JH, Pevsner J, Shaper NL (1998) The expanding β4-galactosyltransferase gene family: messages from the databanks. Glycobiology 8:517–526PubMedCrossRefGoogle Scholar
  17. Lu Q-X, Hasty P, Shur BD (1997) Targeted mutation in β1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. Dev Biol 181:257–267PubMedCrossRefGoogle Scholar
  18. McGuire EJ, Jourdian GW, Carlson DM, Roseman S (1965) Incorporation of D-galactose into glycoproteins. J Biol Chem 240:PC4112–4115PubMedGoogle Scholar
  19. Nixon B, Lu Q, Wassler MJ, Foote CI, Ensslin MA, Shur BD (2001) Galactosyltransferase function during mammalian fertilization. Cells Tissues Organs 168:46–57PubMedCrossRefGoogle Scholar
  20. Rajput B, Shaper NL, Shaper JH (1996) Transcriptional regulation of murine β1,4 galactosyltransferase in somatic cells: analysis of a gene that serves both a housekeeping and a mammary gland-specific function. J Biol Chem 271:5131–5142PubMedCrossRefGoogle Scholar
  21. Russo RN, Shaper NL, Shaper JH (1990) Bovine β1,4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. J Biol Chem 265:3324–3331PubMedGoogle Scholar
  22. Shaper NL, Hollis GF, Douglas JG, Kirsch IR, Shaper JH (1988) Characterization of the full length cDNA for murine β-1,4-galactosyltransferase: novel features at the 5′-end predict two translational start sites at two in-frame AUG’s. J Biol Chem 263:10420–10428PubMedGoogle Scholar
  23. Shaper NL, Meurer JA, Joziasse DH, Chou TD, Smith EJ, Schnaar RL, Shaper JH (1997) The chicken genome contains two functional nonallelic β1,4-galactosyltransferase genes: chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome. J Biol Chem 272:31389–31399PubMedCrossRefGoogle Scholar
  24. Smith CA, Brew K (1977) Isolation and characteristics of galactosyltransferase from Golgi membranes of lactating sheep mammary glands. J Biol Chem 252:7294–7299PubMedGoogle Scholar
  25. Snow DM, Shaper JH, Shaper NL, Hart GW (1999) Determination of β1,4-galactosyltransferase enzymatic activity by capillary electrophoresis and laserinduced fluorescence detection. Anal Biochem 271:36–42PubMedCrossRefGoogle Scholar
  26. Spiro RG (1962) Studies on the monosaccharide sequence of the serum glycoprotein fetuin. J Biol Chem 237:646–652PubMedGoogle Scholar
  27. Strous GJ, van Kerkhof P, Fallon RJ, Schwartz AL (1987) Golgi galactosyltransferase contains serine-linked phosphate. Eur J Biochem 169:307–311PubMedCrossRefGoogle Scholar
  28. Takayama S, Chung SJ, Igarashi Y, Ichikawa Y, Sepp A, Lechler RI, Wu J, Hayashi T, Siuzdak G, Wong C-H (1999) Selective inhibition of β-1,4-and α-1,3-galactosyltransferases: donor sugar-nucleotide based approach. Bioorg Med Chem 7:401–409PubMedCrossRefGoogle Scholar
  29. Trayer IP, Hill RL (1971) The purification and properties of the A protein of lactose synthetase. J Biol Chem 246:6666–6675PubMedGoogle Scholar
  30. Watkins W, Hassid WZ (1962) The synthesis of lactose by particulate enzyme preparations from guinea pig and bovine mammary glands. J Biol Chem 237:1432–1440PubMedGoogle Scholar
  31. Zhou D, Malissard M, Berger EG, Hennet T (2000) Secretion and purification of recombinant galactosyltransferase from insect cells using pFmel-protA, a novel transponsition-based baculovirus transfer vector. Arch Biochem Biophys 373:3–7CrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Nancy L. Shaper
    • 1
  • Joel H. Shaper
    • 1
    • 2
  1. 1.Cell Structure and Function Laboratory, Johns Hopkins Oncology Center CRB-345The Johns Hopkins University School of MedicineBaltimoreUSA
  2. 2.Department of Pharmacology and Molecular SciencesThe Johns Hopkins University School of MedicineBaltimoreUSA

Personalised recommendations