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ST8Sia-I (GD3 Synthase, SAT-II)

  • Yutaka Sanai

Abstract

GD3 synthase and its biosynthetic products, b-series gangliosides, have been suggested to have significant roles in development because of their unique expression patterns during neuronal differentiation. In extraneural tissues, GD3 is implicated in cell attachment, cell-to-cell interactions during embryogenesis, and signal transduction in the glycolipid-enriched microdomain. These observations suggest that GD3 may play an important role not only in brain development, but also in extraneural tissues. GD3 synthase (CMP-N-acetylneuraminate: GM3 α2,8-sialyltransferase) is a key enzyme of ganglioside synthesis that, in concert with GM2 synthase, regulates the ratio of a- and b-pathway gangliosides. The ganglioside composition of cells and tissues thus reflects the relative expression of these two biosynthetic glycosyltrans- ferases. GD3 synthase is characteristically expressed in the early developmental stage of brain tissues.

Keywords

Extraneural Tissue Ganglioside Composition Human Promyelocytic Leukemia Cell Line Embryonic Chicken Brain Ganglioside Synthesis 
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. Basu M, De T, Das KK, Kyle JW, Chon HC, Schaeper RJ, Basu S (1987) Glycolipids. Methods Enzymol 138:575–607PubMedCrossRefGoogle Scholar
  2. Daniotti JL, Martina JA, Giraudo CG, Zurita AR, Maccioni, HJ (2000) GM3 α2,8-sialyltransferase (GD3 synthase): protein characterization and sub-Golgi location in CHO-K1 cells. J Neurochem 74:1711–1720PubMedCrossRefGoogle Scholar
  3. Fukumoto S, Mutoh T, Hasegawa T, Miyazaki H, Okada M, Goto G, Furukawa K, Urano T (2000) GD3 synthase gene expression in PC12 cells results in the continuous activation of TrkA and ERK1/2 and enhanced proliferation. J Biol Chem 275:5832–5838PubMedCrossRefGoogle Scholar
  4. Gu XB, Gu TJ, Yu RK (1990) Purification to homogeneity of GD3 synthase and partial purification of GM3 synthase from rat brain. Biochem Biophys Res Commun 166:387–393PubMedCrossRefGoogle Scholar
  5. Klein D, Pohlentz G, Schwarzmann G, Sandhoff K (1987) Substrate specificity of GM2 and GD3 synthase of Golgi vesicles derived from rat liver. Eur J Biochem 167:417–424PubMedCrossRefGoogle Scholar
  6. Kojima N, Kurosawa N, Nishi T, Hanai N, Tsuji S (1994) Induction of cholinergic differentiation with neurite sprouting by de novo biosynthesis and expression of GD3 and b-series gangliosides in Neuro2a cells. J Biol Chem 269:30451–30456PubMedGoogle Scholar
  7. Lannert H, Gorgas K, Meissner I, Wieland FT, Jeckel D (1998) Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi. J Biol Chem 273:2939–2946PubMedCrossRefGoogle Scholar
  8. Maccioni HJ, Daniotti JL, Martina, JA (1999) Organization of ganglioside synthesis in the Golgi apparatus. Biochim Biophys Acta 1437:101–118PubMedCrossRefGoogle Scholar
  9. Martina JA, Daniotti JL, Maccioni, HJ (1998) Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase. J Biol Chem 273:3725–3731PubMedCrossRefGoogle Scholar
  10. Nakayama J, Fukuda MN, Hirabayashi Y, Kanamori A, Sasaki K, Nishi T, Fukuda M (1996) Expression cloning of a human GT3 synthase. GD3 and GT3 are synthesized by a single enzyme. J Biol Chem 271:3684–3691PubMedCrossRefGoogle Scholar
  11. Nara K, Watanabe Y, Kawashima I, Tai T, Nagai Y, Sanai Y (1996) Acceptor substrate specificity of a cloned GD3 synthase that catalyzes the biosynthesis of both GD3 and GD1c/GT1a/GQ1b. Eur J Biochem 238:647–652PubMedCrossRefGoogle Scholar
  12. Okada M, Furukawa K, Yamashiro S, Yamada Y, Haraguchi M, Horibe K, Kato K, Tsuji Y (1996) High expression of ganglioside α-2,8-sialyltransferase (GD3 synthase) gene in adult T-cell leukemia cells unrelated to the gene expression of human T-lymphotropic virus type ICancer Res 56:2844–2848Google Scholar
  13. Osanai T, Watanabe Y, Sanai Y (1997) Glycolipid sialyltransferases are enhanced during neural differentiation of mouse embryonic carcinoma cells, P19. Biochem Biophys Res Commun 241:327–333PubMedCrossRefGoogle Scholar
  14. Pohlentz G, Kaes C, Sandhoff K (2000) In vitro assays for enzymes of ganglioside synthesis. Methods Enzymol 311:82–94PubMedCrossRefGoogle Scholar
  15. Trinchera M, Pirovano B, Ghidoni R (1990) Sub-Golgi distribution in rat liver of CMP-NeuAc GM3-and CMP-NeuAc:GTlb α-2-8sialyltransferases and comparison with the distribution of the other glycosyltransferase activities involved in ganglioside biosynthesis. J Biol Chem 265:18242–18247PubMedGoogle Scholar
  16. Tsuji S, Datta AK, Paulson, JC (1996) Systematic nomenclature for sialyltransferases [letter]. Glycobiology 6:v–viiPubMedCrossRefGoogle Scholar
  17. Watanabe Y, Nara K, Takahashi H, Nagai Y, Sanai Y (1996) The molecular cloning and expression of α-2,8-sialyltransferase (GD3 synthase) in a rat brain. J Biochem (Tokyo) 120:1020–1027CrossRefGoogle Scholar
  18. Yamamoto A, Haraguchi M, Yamashiro S, Fukumoto S, Furukawa K, Takamiya K, Atsuta M, Shiku H (1996a) Heterogeneity in the expression pattern of two ganglioside synthase genes during mouse brain development. J Neurochem 66:26–34PubMedCrossRefGoogle Scholar
  19. Yamamoto A, Yamashiro S, Fukumoto S, Haraguchi M, Atsuta M, Shiku H, Furukawa K (1996b). Site-restricted and neuron-dominant expression of α-2,8-sialyltransferase gene in the adult mouse brain and retina. Glycoconj J 13:471–480PubMedCrossRefGoogle Scholar
  20. Yamashiro S, Okada M, Haraguchi M, Furukawa K, Lloyd KO, Shiku H (1995) Expression of α-2,8-sialyltransferase (GD3 synthase) gene in human cancer cell lines: high-level expression in melanomas and up-regulation in activated T lymphocytes. Glycoconj J 12:894–900PubMedCrossRefGoogle Scholar
  21. Yu RK, Macala LJ, Taki T, Weinfield HM, Yu FS (1988) Developmental changes in ganglio-side composition and synthesis in embryonic rat brain. J Neurochem 50:1825–1829PubMedCrossRefGoogle Scholar
  22. Zeng G, Ariga T, Gu XB, Yu RK (1995) Regulation of glycolipid synthesis in HL-60 cells by antisense oligodeoxynucleotides to glycosyltransferase sequences: effect on cellular differentiation. Proc Natl Acad Sci USA 92:8670–8674PubMedCrossRefGoogle Scholar
  23. Zeng G, Gao L, Yu RK (2000) Reduced cell migration, tumor growth and experimental metastasis of rat F-11 cells whose expression of GD3-synthase is suppressed. Int J Cancer 88:53–57PubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Yutaka Sanai
    • 1
  1. 1.Department of Biochemical Cell ResearchTokyo Metropolitan Institute of Medical ScienceTokyoJapan

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