Advertisement

Polypeptide N-Acetylgalactosaminyltransferases

  • Fred K. Hagen
  • Kelly G. Ten Hagen
  • Lawrence A. Tabak

Abstract

The initiation of (mucin-type) O-glycosylation is catalyzed by a family of UDP- GalNAcpolypeptide N-acetylgalactosaminyltransferases (ppGaNTases). These enzymes catalyze the transfer of GalNAc from the nucleotide sugar UDP-GalNAc to the hydroxyl group of either serine or threonine.

Keywords

Bovine Colostrum Sublingual Gland Ascites Hepatoma Murine Lymphoma Hydroxyamino Acid 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Alfalah M, Jacob R, Preuss U, Zimmer K-P, Nairn H, Nairn HY (1999) O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Curr Biol 9:593–596PubMedCrossRefGoogle Scholar
  2. Bennett EP, Hassan H, Clausen H (1996) cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. J Biol Chem 271:17006–17012PubMedCrossRefGoogle Scholar
  3. Bennett EP, Hassan H, Mandel U, Hollingsworth MA, Akisawa N, Ikematsu Y, Merkx G, van Kessel AG, Olofsson S, Clausen H (1999) Cloning and characterization of a close homologue of human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. J Biol Chem 274:25362–25370PubMedCrossRefGoogle Scholar
  4. Campbell JA, Davies GJ, Bulone V, Henrissat B (1998) A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem J 329:719PubMedGoogle Scholar
  5. Elhammer A, Kornfeld S (1996) Purification and characterization of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells. J Biol Chem 261:5249–5255Google Scholar
  6. Elhammer AP, Kézdy FJ, Kurosaka A (1999) The acceptor specificity of UDP-GalNAc:polypeptideN-acetylgalactosaminyltransferases. Glyco J 16:171–180CrossRefGoogle Scholar
  7. Hagen FK, Nehrke K (1998) cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans. J Biol Chem 272:8268–8CrossRefGoogle Scholar
  8. Hagen FK, VanWuyckhuyse B, Tabak LA (1993) Purification, cloning, and expression of a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem 268:18960–18965PubMedGoogle Scholar
  9. Hagen FK, Ten Hagen KG, Beres T, Balys MM, VanWuyckhuyse BC, Tabak LA (1997) cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem 272:13843–13848PubMedCrossRefGoogle Scholar
  10. Hagen FK, Hazes B, Raffo R, deSa D, Tabak LA (1999) Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem 274:6797–6803PubMedCrossRefGoogle Scholar
  11. Hanisch F-G, Müller S, Hassan H, Clausen H, Zachara N, Gooley AA, Paulsen H, Alving K, Peter-Katalinic J (1999) Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-acetylgalactosamine: peptide N-acetylgalactosaminyltransferases. J Biol Chem 274:9946–9954PubMedCrossRefGoogle Scholar
  12. Hassan H, Reis CA, Bennett EP, Mirgorodskaya E, Roespstorff P, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H (2000) The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. J Biol Chem 275:38197–38205PubMedCrossRefGoogle Scholar
  13. Hennet T, Hagen FK, Tabak LA, Marth JD (1995) T-cell-specific deletion of a polypeptide N-acetylgalactosaminyltransferase gene by site-directed recombination. Proc Natl Acad Sci USA 92:12070–12074PubMedCrossRefGoogle Scholar
  14. Jentoft N (1990) Why are proteins O-glycosylated? Trends Biochem Sci 15:291–294PubMedCrossRefGoogle Scholar
  15. Kinarsky L, Nomoto M, Ikematsu Y, Hassan H, Bennett EP, Cerny RL, Clausen H, Hollingsworth MA, Sherman S (1998) Structural analysis of peptide substrates for mucin-type O-glycosylation. Biochemistry 37:12811–12817CrossRefGoogle Scholar
  16. Kingsley PD, Ten Hagen KG, Maltby KM, Zara J, Tabak LA (2000) Diverse spatial expretes-sion patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family member RNAs during mouse development. Glycobiology 10:1317–1323PubMedCrossRefGoogle Scholar
  17. Leppänen A, Mehta P, Ouyang Y-B, Ju T, Helin J, Moore KL, van Die I, Canfield WM, McEver RP, Cummings RD (1999) A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin. J Biol Chem 274:24838–24848PubMedCrossRefGoogle Scholar
  18. McGuire EJ, Roseman S (1967) Enzymatic synthesis of the protein-hexosamine linkage in sheep submaxillary mucin. J Biol Chem 242:3745–3755PubMedGoogle Scholar
  19. Nehrke K, Ten Hagen KG, Hagen FK, Tabak LA (1997) Charge distribution of flanking amino acids inhibits O-glycosylation of several single-site acceptors in vivo. Glycobiology 7:1053–1060PubMedCrossRefGoogle Scholar
  20. Nehrke K, Hagen FK, Tabak LA (1998) Isoform-specific O-glycosylation by murine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3, in vivo. Glycobiology 8:367–371PubMedCrossRefGoogle Scholar
  21. Röttger S, White J, Wandall HH, Olivo J-C, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T (1998) Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci 111:45–50PubMedGoogle Scholar
  22. Sugiura M, Kawasaki T, Yamashina I (1982) Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosamine transferase from an ascites hepatoma, AH 66. J Biol Chem 257:9501–9507PubMedGoogle Scholar
  23. Ten Hagen KG, Hagen FK, Balys MM, Beres TM, VanWuyckhuyse BC, Tabak LA (1998) Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide.N-acetylgalactosaminyltransferase family. J Biol Chem 273:27749–27754PubMedCrossRefGoogle Scholar
  24. Ten Hagen KG, Tetaert D, Hagen FK, Richet C, Beres TM, Gagnon J, Balys MM, VanWuyckhuyse B, Bedi GS, Degand P, Tabak LA (1999) Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase which displays glycopeptide N-acetylgalactosaminyltransferase activity. J Biol Chem 274:27867–27874PubMedCrossRefGoogle Scholar
  25. Ten Hagen KG, Bedi GS, Tetaert D, Kingsley PD, Hagen FK, Balys MM, Beres TM, Degand P, Tabak LA (2001) Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9. J Biol Chem 276:17395–17404PubMedCrossRefGoogle Scholar
  26. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H (1997) Substrate specificities of three members of the human UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1-T2, and-T3. J Biol Chem 272:23503–23514PubMedCrossRefGoogle Scholar
  27. Westerman EL, Ellies LG, Hagen FK, Marek KW, Sutton-Smith M, Dell A, Tabak LA, Marth JD (1999) Selective loss of O-glycans in mice lacking polypeptide GalNAc-Tl. Glyco-biology 9:1121 (abstract No. 80)Google Scholar
  28. White T, Bennett EP, Takio K, S0rensen T, Bonding N, Clausen H (1995) Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem 270:24156–24165PubMedCrossRefGoogle Scholar
  29. Wragg S, Hagen FK, Tabak LA (1995) Kinetic analysis of a recombinant UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem 270:16947–16954PubMedCrossRefGoogle Scholar
  30. Zara J, Hagen FK, Ten Hagen KG, VanWuyckhuyse BC, Tabak LA (1996) Cloning and expression of mouse UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase. Biochem Biophys Res Comm 228:38–44PubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Fred K. Hagen
    • 1
  • Kelly G. Ten Hagen
    • 1
  • Lawrence A. Tabak
    • 2
  1. 1.Center for Oral Biology, Aab Institute of Biomedical SciencesUniversity of RochesterRochesterUSA
  2. 2.National Institute of Dental and Craniofacial Research. NIHBethesdaUSA

Personalised recommendations