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ST3Gal-V (GM3 Synthase, SAT-I)

  • Masaki Saito
  • Atsushi Ishii

Abstract

ST3Gal-V (GM3 synthase) belongs to the sialyltransferase family, and is a unique enzyme among all sialyltransferases so far identified since it is specifically involved in ganglioside GM3 formation. Since GM3 is a common precursor of almost all gangliosides (especially ganglio-series gangliosides), GM3 synthase plays an important role in the biosynthesis of more complex gangliosides, and primarily regulates the amount of GM3. As is found in all members of the sialyltransferase family, the cloned ST3Gal-Vs from different animal origins encode type II membrane proteins with two conserved regions, i.e., sialylmotifs L and S, although an invariant aspartic acid residue in sialylmotif Ls of all other sialyltransferases is characteristically replaced by histidine residue (Ishii et al. 1998; Kono et al. 1998; Fukumoto et al. 1999).

Keywords

Complex Ganglioside National Cancer Center Research Institute Ganglioside Biosynthesis Acetylneuraminic Acid NFS60 Cell 
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.

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References

  1. Chou DKH, Jungalwala FB (1996) N-Acetylglucosaminyl transferase regulates the expression of the sulfoglucuronyl glycolipids in specific cell types in cerebellum during development. J Biol Chem 271:28868–28874PubMedCrossRefGoogle Scholar
  2. Duffard RO, Fishman PH, Bradley RM, Lauter CJ, Brady RO, Trams EG (1977) Ganglioside composition and biosynthesis in cultred cells derived from CNS. J Neurochem 28:1161–1166PubMedCrossRefGoogle Scholar
  3. Fleischer B (1977) Localization of some glycolipid glycosylating enzymes in the Golgi apparatus of rat kidney. J Supramol Struct 7:79–89PubMedCrossRefGoogle Scholar
  4. Fukumoto S, Miyazaki H, Goto G, Urano T, Furukawa K, Furukawa K (1999) Expression cloning of mouse cDNA of CMP-NeuAc:lactosylceramide α2,3-sialyltransferase, an enzyme that initiates the synthesis of gangliosides. J Biol Chem 274:9271–9276PubMedCrossRefGoogle Scholar
  5. Glickman RM, Bouhours JF (1976) Characterization, distribution and biosynthesis of the major ganglioside of rat intestinal mucosa. Biochim Biophys Acta 424:17–25PubMedCrossRefGoogle Scholar
  6. Holmes EH, Hakomori S, Ostrander GK (1987) Synthesis of type 1 and 2 lacto-series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1-3 N-acetylglucosaminyltransferase. J Biol Chem 262:15649–15658PubMedGoogle Scholar
  7. Iber H, van Echten G, Sandhoff K (1992) Fractionation of primary cultured cerebellar neurons: distribution of sialyltransferases involved in ganglioside biosynthesis. J Neuro chem 58:1533–1537Google Scholar
  8. Ishii A, Ohta M, Watanabe Y, Matsuda K, Ishiyama K, Sakoe K, Nakamura M, Inokuchi J, Sanai Y, Saito M (1998) Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase. J Biol Chem 273:31652–31655PubMedCrossRefGoogle Scholar
  9. Kaufman B, Basu S, Roseman S (1968) Enzymatic synthesis of disialogangliosides from monosialogangliosides by sialyltransferases from embryonic chicken brain. J Biol Chem 243:5804–5807PubMedGoogle Scholar
  10. Keenan TW, Morre DJ, Basu S (1974) Ganglioside biosynthesis. Concentration of glycosphingolipid glycosyltransferases in Golgi apparatus from rat liver. J Biol Chem 249:310–315PubMedGoogle Scholar
  11. Kono M, Takashima S, Liu H, Inoue M, Kojima N, Lee Y-S, Hamamoto T, Tsuji S (1998) Molecular cloning and functional expression of a fifth-type α2,3-sialyltransferase (mST3Gal-V: GM3 synthase). Biochem Biophys Res Commun 253:170–175PubMedCrossRefGoogle Scholar
  12. Lannert H, Gorgas K, Meibner I, Wieland FT, Jeckel D (1998) Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. J Biol Chem 273:2939–2946PubMedCrossRefGoogle Scholar
  13. Lee Y-C, Kojima N, Wada E, Kurosawa N, Nakaoka T, Hamamoto T, Tsuji S (1994) Cloning and expression of cDNA for a new type of Galβ1,3GalNAcα2,3-sialyltransferase. J Biol Chem 269:10028–10033PubMedGoogle Scholar
  14. Melkerson-Watson LJ, Sweeley CC (1991) Purification to apparent homogeneity by immunoaffinity chromatography and partial characterization of the GM3 ganglioside-forming enzyme, CMP-sialic acid:lactosylceramide α2,3-sialyltransferase (SN-I), from rat liver Golgi. J Biol Chem 267:23507–23514Google Scholar
  15. Nakamura M, Tsunoda A, Sakoe K, Gu J, Nishikawa A, Taniguchi N, Saito M (1992) Total metabolic flow of glycosphingolipid biosynthesis is regulated by UDP-GlcNAc:lacosylceramide β1-3 N-acetylglucosaminyltransferase and CMP-NeuAc:lactosylceramide α2-3 sialyltransferase in human hematopoietic cell line HL-60 during differentiation. J Biol Chem 267:23507–23514PubMedGoogle Scholar
  16. Pacuszka T, Duffard RO, Nishimura RN, Brady RO, Fishman PH (1978) Biosynthesis of bovine thyroid gangliosides. J Biol Chem 253:5839–5846PubMedGoogle Scholar
  17. Preti A, Fiorilli A, Lombardo A, Caimi L, Tettamanti G (1980) Occurrence of sialyltransferase activity in the synaptosomal membranes prepared from calf brain cortex. J Neurochem 35:281–296PubMedCrossRefGoogle Scholar
  18. Preuss U, Gu X, Gu T, Yu RK (1993) Purification and characterization of CMP-N-acetylneuraminic acid:lactosylceramide (α2-3) sialyltransferase (GM3-synthase) from rat brain. J Biol Chem 268:26273–26278PubMedGoogle Scholar
  19. Richardson CL, Keenan TW, Morre DJ (1977) Ganglioside biosynthesis—characterization of CMP-N-acetylneuraminic acid: lactosylceramide sialyltransferase in Golgi apparatus from rat liver. Biochim Biophys Acta 488:88–96PubMedCrossRefGoogle Scholar
  20. Stern AS, Braverman TR, Tiemeyer M (2000) Molecular identification, tissue distribution and subcellular localization of mST3Gal-V/GM3 synthase. Glycobiology 10:365–374PubMedCrossRefGoogle Scholar
  21. Trams EG (1977) J Neurochem 28:1161–1166PubMedCrossRefGoogle Scholar
  22. Trinchera M, Ghidoni R (1989) Two glycosphingolipid sialyltransferases are localized in different sub-Golgi compartments in rat liver. J Biol Chem 264:15766–15769PubMedGoogle Scholar
  23. Trinchera M, Fabbri M, Ghidoni R (1991) Topography of glycosyltransferases involved in the initial glycosylations of gangliosides. J Biol Chem 266:20907–20912PubMedGoogle Scholar
  24. Tsunoda A, Nakamura M, Kirito K, Hara K, Saito M (1995) Interleukin-3-associated expression of gangliosides in mouse myelogenous leukemia NFS60 cells introduced with interleukin-3 gene: expression of ganglioside GD1a and key involvement of CMP-NeuAclactosylceramide α-2-3-sialyltransferase in GD1a expression. Biochemistry 34:9356–9367PubMedCrossRefGoogle Scholar
  25. van Echten G, Iber H, Stotz H, Takatsuki A, Sandhoff (1990) Uncoupling of ganglioside biosynthesis by Brefeldin A. Eur J Cell Biol 51:135–139PubMedGoogle Scholar
  26. Young WW Jr, Lutz MS, Mills SE, Lechler-Osborn S (1990) Use of brefeldin A to define sites of glycosphingolipid synthesis: GA2/GM2/GD2 synthase is trans to the brefeldin A block. Proc Natl Acad Sci USA 87:6838–6842PubMedCrossRefGoogle Scholar
  27. Yu RK, Lee SH (1976) In vitro biosynthesis of sialylgalactosylceramide (G7) by mouse brain microsomes. J Biol Chem 251:198–203PubMedGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Masaki Saito
    • 1
    • 2
  • Atsushi Ishii
    • 2
  1. 1.Department of Oncology and PharmacodynamicsMeiji Pharmaceutical UniversityTokyoJapan
  2. 2.Virology and Glycobiology DivisionNational Cancer Center Research InstituteTokyoJapan

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