Organization of ganglioside synthesis in the Golgi apparatus

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1437, Issue 2, 1999, Pages 101-118

  Maccioni, Hugo J F ^a   Daniotti, José L ^a   Martina, José A ^a  

^a Centro de Investigaciones En Quimica Biologica de Cordoba   (Argentina)

Author keywords

Brefeldin A; Ganglioside glycosylation; Ganglioside synthesis topology; Glycolipid trafficking; Glycosyltransferase; Golgi complex; Monensin

Indexed keywords

BREFELDIN A; GANGLIOSIDE; GLYCOLIPID; GLYCOSYLTRANSFERASE; MEMBRANE ENZYME; MONENSIN;

ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME SPECIFICITY; GLYCOSYLATION; GOLGI COMPLEX; LIPOGENESIS; PRIORITY JOURNAL; REACTION ANALYSIS; REGULATORY MECHANISM; REVIEW; TRANSCRIPTION REGULATION;

ANIMALS; CELLS, CULTURED; ENZYME ACTIVATION; GANGLIOSIDES; GLYCOSPHINGOLIPIDS; GLYCOSYLTRANSFERASES; GOLGI APPARATUS; HUMANS; SUBCELLULAR FRACTIONS; TRANSCRIPTION, GENETIC;

EID: 0033602111     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00002-5     Document Type: Review

References (142)

1. Sandhoff K., van Echten G. Ganglioside metabolism - topology and regulation. Adv. Lipid Res. 26:1993;119-142.
2. Hirschberg K., Rodger J., Futerman A.H. The long-chain sphingoid base of sphingolipids is acylated at the cytosolic surface of the endoplasmic reticulum in rat liver. Biochem. J. 290:1993;751-757.
3. Mandon E.C., Ehses I., Rother J., van Echten G., Sandhoff K. Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver. J. Biol. Chem. 267:1992;11144-11148.
4. G. van Echten-Deckert, K. Sandhoff, Organisation and topology of sphingolipid metabolism, in: B.M. Pinto (Ed.), Comprehensive Natural Products Chemistry, vol. 3, Pergamon Elsevier Science, New York, 1998, Ch. 5.
5. Rother J., van Echten G., Schwarzmann G., Sandhoff K. Biosynthesis of sphingolipids: dihydroceramide and not sphinganine is desaturated by cultured cells. Biochem. Biophys. Res. Commun. 189:1992;14-20.
6. Michel C., van Echten-Deckert G. Conversion of dihydroceramide to ceramide occurs at the cytosolic face of the endoplasmic reticulum. FEBS Lett. 416:1997;153-155.
7. Burger K.N., Van der Bijl P., Van Meer G. Topology of sphingolipid galactosyltransferases in ER and Golgi: transbilayer movement of monohexosyl sphingolipids is required for higher glycosphingolipid biosynthesis. J. Cell Biol. 133:1996;15-28.
8. Kendler A., Dawson G. Hypoxic injury to oligodendrocytes: reversible inhibition of ATP-dependent transport of ceramide from the endoplasmic reticulum to the Golgi. J. Neurosci. Res. 31:1992;205-211.
9. Sprong H., Kruithof B., Leijendekker R., Slot J.W., van Meer G., van der Sluijs P. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. J. Biol. Chem. 273:1998;25880-25888.
10. Radin N.S., Metz R.J. Cerebroside transfer protein. Methods Enzymol. 98:1983;613-622.
11. Sasaki T., Abe A. Glycolipid transfer protein from pig brain. Methods Enzymol. 179:1989;559-566.
12. Warnock D.E., Lutz M.S., Blackburn W.A., Young W.W. Jr., Baenziger J.U. Transport of newly synthesized glucosylceramide to the plasma membrane by a non-Golgi pathway. Proc. Natl. Acad. Sci. USA. 91:1994;2708-2712.
13. van Helvoort A., Smith A.J., Sprong H., Fritzsche I., Schinkel A.H., Borst P., van Meer G. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell. 87:1996;507-517.
14. Roseman S. The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intracellular adhesion. Chem. Phys. Lipids. 5:1970;270-297.
15. Keenan T.W., Morre D.J., Basu S. Ganglioside biosynthesis. Concentration of glycosphingolipid glycosyltransferases in Golgi apparatus from rat liver. J. Biol. Chem. 249:1974;310-315.
16. Caputto R., Maccioni H.J.F., Arce A. Biosynthesis of brain gangliosides. Mol. Cell. Biochem. 4:1974;97-106.
17. van Echten G., Sandhoff K. Ganglioside metabolism. Enzymology, topology, and regulation. J. Biol. Chem. 268:1993;5341-5344.
18. Gillard B.K., Clement R.G., Marcus D.M. Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways. Glycobiology. 8:1998;885-890.
19. Riboni L., Viani P., Bassi R., Prinetti A., Tettamanti G. The role of sphingolipids in the process of signal transduction. Prog. Lipid Res. 36:1997;153-195.
20. Schulte S., Stoffel W. Ceramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. USA. 90:1993;10265-10269.
21. Spiess M. Heads or tails - what determines the orientation of proteins in the membrane. FEBS Lett. 369:1995;76-79.
22. Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I., Hirabayashi Y. Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc. Natl. Acad. Sci. USA. 93:1996;4638-4643.
23. Ichikawa S., Hirabayashi Y. Glucosylceramide synthase and glycosphingolipid synthesis. Trends Cell Biol. 8:1998;198-202.
24. Coste H., Martel M.B., Got R. Topology of glucosylceramide synthesis in Golgi membranes from porcine submaxillary glands. Biochim. Biophys. Acta. 858:1986;6-12.
25. Futerman A.H., Pagano R.E. Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver. Biochem. J. 280:1991;295-302.
26. Jeckel D., Karrenbauer A., Burger K.N., van Meer G., Wieland F. Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions. J. Cell Biol. 117:1992;259-267.
27. Trinchera M., Fabbri M., Ghidoni R. Topography of glycosyltransferases involved in the initial glycosylations of gangliosides. J. Biol. Chem. 266:1991;20907-20912.
28. Paulson C., Colley K.J. Glycosyltransferases. Structure, localization and control of cell type-specific glycosylation. J. Biol. Chem. 30:1989;17615-17618.
29. Field M.C., Wainwright L.J. Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a survey. Glycobiology. 5:1995;463-472.
30. Haraguchi M., Yamashiro S., Furukawa K., Takamiya K., Shiku H., Furukawa K. The effects of the site-directed removal of N-glycosylation sites from beta-1,4-N-acetylgalactosaminyltransferase on its function. Biochem. J. 312:1995;273-280.
31. A Martina J., Daniotti J.L., Maccioni H.J.F. Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase. J. Biol. Chem. 273:1998;3725-3731.
32. Trinchera M., Ghidoni R. Two glycosphingolipid sialyltransferases are localized in different sub-Golgi compartments in rat liver. J. Biol. Chem. 264:1989;15766-15769.
33. Trinchera M., Pirovano B., Ghidoni R. Sub-Golgi distribution in rat liver of CMP-NeuAc GM3 and CMP-NeuAc GT1b α 2→8 sialyltransferases and comparison with the distribution of the other glycosyltransferase activities involved in ganglioside biosynthesis. J. Biol. Chem. 265:1990;18242-18247.
34. Lannert H., Gorgas K., Meissner I., Wieland F.T., Jeckel D. Functional organisation of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi. J. Biol. Chem. 273:1998;2939-2946.
35. Iber H H., van Echten G., Sandhoff K. Fractionation of primary cultured cerebellar neurons: distribution of sialyltransferases involved in ganglioside biosynthesis. J. Neurochem. 58:1992;1533-1537.
36. Donaldson J.G., Klausner R.D. ARF: a key regulatory switch in membrane traffic and organelle structure. Curr. Opin. Cell Biol. 6:1994;527-532.
37. van Echten G., Iber H., Stotz H., Takatsuki A., Sandhoff K. Uncoupling of ganglioside biosynthesis by brefeldin A. Eur. J. Cell Biol. 51:1990;135-139.
38. Young W.W. Jr., Lutz M.S., Mills S.E., Lechler-Osborn S. 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. 87:1990;6838-6842.
39. Rosales Fritz V.M., Maccioni H.J.F. Effects of brefeldin A on synthesis and intracellular transport of ganglioside GT3 by chick embryo retina cells. J. Neurochem. 65:1995;1859-1864.
40. Sciaky N., Presley J., Smith C., Zaal K.J., Cole N., Moreira J.E., Terasaki M., Siggia E., Lippincott-Schwartz J. Golgi tubule traffic and the effects of brefeldin A visualized in living cells. J. Cell Biol. 139:1997;1137-1155.
41. Mollenhauer H.H., Morré D.J., Rowe L.D. Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity. Biochim. Biophys. Acta. 1031:1990;225-246.
42. Miller-Prodraza H., Fishman P.H. Effect of drugs and temperature on biosynthesis and transport of glycosphingolipids in cultured neurotumor cells. Biochim. Biophys. Acta. 804:1984;44-51.
43. Nores G.A., Caputto R. Regulation of ganglioside and sialoglycoprotein biosynthesis. Effect of drugs affecting membrane flow. Neurochem. Int. 8:1986;501-506.
44. van Echten G., Sandhoff K. Modulation of ganglioside biosynthesis in primary cultured neurons. J. Neurochem. 52:1989;207-214.
45. Rosales Fritz V.M., Maxzúd M.K., Maccioni H.J.F. GT3 synthesis in the proximal Golgi occurs in a compartment different from those for GD3 and GM3 synthesis. J. Neurochem. 67:1996;1393-1400.
46. Nakayama J., Fukuda M.N., Hirabayashi Y., Kanamori A., Sasaki K., Nishi T., Fukuda M. Expression cloning of a human GT3 synthase. GD3 and GT3 are synthesized by a single enzyme. J. Biol. Chem. 271:1996;3684-3691.
47. Iber H., Zacharias C., Sandhoff K. The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver Golgi by the same set of glycosyltransferases that catalyse the biosynthesis of asialo-, a- and b-series gangliosides. Glycobiology. 2:1992;137-142.
48. Zeng G., Gao L., Yu R.K. Cloning of the cDNA coding for rat brain CMP-NeuAc:GD3 alpha2-8 sialyltransferase. Gene. 187:1997;131-134.
49. Maxzúd M.K., Daniotti J.L., Maccioni H.J.F. Functional coupling of glycosyltransfer steps for synthesis of gangliosides in Golgi membranes from neural retina cells. J. Biol. Chem. 270:1995;20207-20214.
50. Maxzúd M.K., Maccioni H.J.F. Compartmental organization of the synthesis of GM3, GD3 and GM2 in Golgi membranes from neural retina cells. Neurochem. Res. 22:1997;455-461.
51. Rothman J.E. Mechanisms of intracellular protein transport. Nature. 372:1994;55-63.
52. Arce A., Maccioni H.J.F., Caputto R. The biosynthesis of gangliosides. The incorporation of galactose, N-acetylgalactosamine and N-acetylneuraminic acid into endogenous acceptors of subcellular particles from rat brain in vitro. Biochem. J. 121:1971;483-493.
53. Maccioni H.J.F., Arce A., Landa C.A., Caputto R. Rat brain microsomal gangliosides. Accessibility to a neuraminidase preparation and the possible existence of different pools in relation to their biosynthesis. Biochem. J. 138:1974;291-298.
54. Sjoberg E.R., Varki A. Kinetic and spatial interrelationships between ganglioside glycosyltransferases and O-acetyltransferase(s) in human melanoma cells. J. Biol. Chem. 268:1993;10185-10196.
55. Varki A. Factors controlling the glycosylation potential of the Golgi apparatus. Trends Cell Biol. 8:1998;34-40.
56. Pfeffer S.R., Rothman J.E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56:1987;829-852.
57. Monica T.J., Andersen D.C., Goochee C.F. A mathematical model of sialylation of N-linked oligosaccharides in the trans-Golgi network. Glycobiology. 7:1997;515-521.
58. Daniotti J.L., Rosales Fritz V.M., Martina J.A., Furukawa K., Maccioni H.J.F. Expression of beta 1-4-N-acetylgalactosaminyltransferase gene in the developing rat brain and retina: mRNA, protein immunoreactivity and enzyme activity. Neurochem. Int. 31:1997;11-19.
59. Jaskiewicz E., Zhu G., Taatjes D.J., Darling D.S., Zwanzig G.E. Jr., Young W.W. Jr. Cloned beta 1,4-N-acetylgalactosaminyltransferase: subcellular localization and formation of disulfide bonded species. Glycoconjugate J. 13:1996;213-223.
60. H.J.F. Maccioni, J.L. Daniotti, C. Giraudo, V.R. Fritz, J.A. Martina, M.K. Maxzud, SubGolgi location of ganglioside GD3- and GM2-synthases (Abstr.), The Golgi Complex, 100th Anniversary Conference, Pavia, Italy, 1998, p. 81.
61. Jaskiewicz E., Zhu G., Bassi R., Darling D.S., Young W.W. Jr. Beta1,4-N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase-sensitive, disulfide-bonded dimer by a cathepsin D-like protease. J. Biol. Chem. 271:1996;26395-26403.
62. Zhu G., Jaskiewicz E., Bassi R., Darling D.S., Young W.W. Jr. Beta 1,4-N-acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: a strategy to test for dimerization of Golgi membrane proteins. Glycobiology. 7:1997;987-996.
63. J.L. Daniotti, H.J.F. Maccioni, Sub Golgi location of GD3 synthase. An immunocytochemical study, J. Neurochem. 69 (1997) Suppl. S12A.
64. Goda Y., Pfeffer S.R. Selective recycling of the mannose 6-phosphate/IGF-II receptor to the trans Golgi network in vitro. Cell. 55:1988;309-320.
65. Griffiths G., Hoflack B., Simons K., Mellman I., Kornfeld S. The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell. 52:1988;329-341.
66. Miyazaki H., Fukumoto S., Okada M., Hasegawa T., Furukawa K. Expression cloning of rat cDNA encoding UDP-galactose:GD2 beta1,3-galactosyltransferase that determines the expression of GD1b/GM1/GA1. J. Biol. Chem. 272:1997;24794-24799.
67. Amado M., Almeida R., Carneiro F., Levery S.B., Holmes E.H., Nomoto M., Hollingsworth M.A., Hassan H., Schwientek T., Nielsen P.A., Bennett E.P., Clausen H. A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetylglucosamine/beta-N-acetylgalactosamine beta-1,3-galactosyltransferase family. J. Biol. Chem. 273:1998;12770-12778.
68. Tarentino A.L., Plummer T.H., Maley F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249:1974;818-824.
69. Munro S. Localization of proteins to the Golgi apparatus. Trends Cell Biol. 8:1998;11-15.
70. Zeng G., Gao L., Ariga T., Yu R.K. Molecular cloning of cDNA for rat brain GD3-synthase. Biochem. Biophys. Res. Commun. 226:1996;319-323.
71. Daniotti J.L., Rosales Fritz V.M., Kunda P., Nishi T., Maccioni H.J.F. Cloning, characterization and developmental expression of alpha2,8 sialyltransferase (GD3 synthase, ST8Sia I) gene in chick brain and retina. Int. J. Dev. Neurosci. 15:1997;767-776.
72. Nagata Y., Yamashiro S., Yodoi J., Lloyd K., Shiku H., Furukawa K. Expression cloning of β1,4-N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. J. Biol. Chem. 267:1992;12082-12089.
73. Ichikawa S., Ozawa K., Hirabayashi Y. Molecular cloning and expression of mouse ceramide glucosyltransferase. Biochem. Mol. Biol. Int. 44:1998;1193-1202.
74. Stahl N., Jurevics H., Morell P., Suzuki K., Popko B. Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose:ceramide galactosyltransferase. J. Neurosci. Res. 38:1994;234-242.
75. Nomura T., Takizawa M., Aoki J., Arai H., Inoue K., Wakisaka E., Yoshizuka N., Imokawa G., Dohmae N., Takio K., Hattori M., Matsuo N. Purification, cDNA cloning, and expression of UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273:1998;13570-13577.
76. Fullekrug J., Nilsson T. Protein sorting in the Golgi complex. Biochim. Biophys. Acta. 1404:1998;77-84.
77. Costa J., Grabenhorst E., Nimtz M., Conradt H.S. Stable expression of the Golgi form and secretory variants of human fucosyltransferase III from BHK-21 cells. Purification and characterization of an engineered truncated form from the culture medium. J. Biol. Chem. 272:1997;11613-11621.
78. Borsig L., Katopodis A.G., Bowen B.R., Berger E.G. Trafficking and localization studies of recombinant alpha1,3-fucosyltransferase VI stably expressed in CHO cells. Glycobiology. 8:1998;259-268.
79. Masri K.A., Appert H.E., Fukuda M.N. Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide:beta 1,4-galactosyltransferase). Biochem. Biophys. Res. Commun. 157:1988;657-663.
80. Homa F.L., Hollander T., Lehman D.J., Thomsen D.R., Elhammer A.P. Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem. 268:1993;12609-12616.
81. Weinstein J., Lee E.U., Mcentee K., Lai P.H., Paulson J.C. Primary structure of beta-galactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. J. Biol. Chem. 262:1987;17735-17743.
82. Nara K., Watanabe Y., Maruyama K., Kasahara K., Nagai Y., Sanai Y. Expression cloning of a CMP-NeuAc:NeuAc alpha 2-3Gal beta 1-4Glc beta 1-1′Cer alpha 2,8-sialyltransferase (GD3 synthase) from human melanoma cells. Proc. Natl. Acad. Sci. USA. 91:1994;7952-7956.
83. Allende M.L., Schwendiman R.M., Young W.W. Jr. Appearance of beta 1,4 N-acetylgalactosaminyltransferase (glycosphingolipids GA2/GM2/GD2 synthase) in embryonic chicken vitreous humor during development. Curr. Eye Res. 16:1997;1263-1269.
84. Panzetta P., Maccioni H.J.F., Caputto R. Synthesis of retinal gangliosides during chick embryonic development. J. Neurochem. 35:1980;100-108.
85. H.J.F. Maccioni, P. Panzetta, C.A. Landa, Biosynthesis and expression of gangliosides during neural differentiation, in: R.W. Ledeen, E.L. Hogan, G. Tettamanti, A.J. Yates, R.K. Yu (Eds.), New Trends in Ganglioside Research: Neurochemical and Neuroregenerative Aspects, Liviana Press, Padua, 1988, pp. 295-305.
86. Yu R.K., Macala L.J., Taki T., Weinfield H.M., Yu F.S. Developmental changes in ganglioside composition and synthesis in embryonic rat brain. J. Neurochem. 50:1988;1825-1829.
87. Daniotti J.L., Landa C.A., Rosner H., Maccioni H.J.F. GD3 prevalence in adult rat retina correlates with the maintenance of a high GD3-/GM2-synthase activity ratio throughout development. J. Neurochem. 57:1991;2054-2058.
88. Ruan S., Lloyd K.O. Glycosylation pathways in the biosynthesis of gangliosides in melanoma and neuroblastoma cells: relative glycosyltransferase levels determine ganglioside patterns. Cancer Res. 52:1992;5725-5731.
89. Zeng G., Ariga T., Gu X.B., Yu R.K. Regulation of glycolipid synthesis in HL-60 cells by antisense oligodeoxynucleotides to glycosyltransferase sequences: effect on cellular differentiation. Proc. Natl. Acad. Sci. USA. 92:1995;8670-8674.
90. Rosales Fritz V.M., Daniotti J.L., Maccioni H.J.F. Chinese hamster ovary cells lacking GM1 and GD1a synthesize gangliosides upon transfection with human GM2 synthase. Biochim. Biophys. Acta. 1354:1997;153-158.
91. Lloyd K.O., Furukawa K. Biosynthesis and functions of gangliosides: recent advances. Glycoconjugate J. 15:1998;627-636.
92. Martina J.A., Daniotti J.L., Maccioni H.J.F. A UDP-GalNAc pyrophosphatase activity is developmentally regulated in the rat retina. J. Neurochem. 64:1995;1274-1280.
93. Yamamoto A., Haraguchi M., Yamashiro S., Fukumoto S., Furukawa K., Takamiya K., Atsuta M., Shiku H., Furukawa K. Heterogeneity in the expression pattern of two ganglioside synthase genes during mouse brain development. J. Neurochem. 66:1996;26-34.
94. Watanabe R., Wu K., Paul P., Marks D.L., Kobayashi T., Pittelkow M.R., Pagano R.E. Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation. J. Biol. Chem. 273:1998;9651-9655.
95. Furukawa K., Soejima H., Niikawa N., Shiku H. Genomic organization and chromosomal assignment of the human beta1, 4-N-acetylgalactosaminyltransferase gene. Identification of multiple transcription units. J. Biol. Chem. 271:1996;20836-20844.
96. Zeng G., Gao L., Yu R.K. Isolation and functional analysis of the promoter of the rat CMP-NeuAc:GM3 alpha2,8 sialyltransferase gene 1. Biochim. Biophys. Acta. 1397:1998;126-130.
97. Matsuda Y., Nara K., Watanabe Y., Saito T., Sanai Y. Chromosome mapping of the GD3 synthase gene (SIAT8) in human and mouse. Genomics. 32:1996;137-139.
98. Sasaki K., Kurata K., Kojima N., Kurosawa N., Ohta S., Hanai N., Tsuji S., Nishi T. Expression cloning of a GM3-specific α-2,8-sialyltransferase (GD3 synthase). J. Biol. Chem. 269:1994;15950-15956.
99. Scheideler M.A., Dawson G. Direct demonstration of the activation of UDP-N-acetylgalactosamine:[GM3]N-acetylgalactosaminyltransferase by cyclic AMP. J. Neurochem. 46:1986;1639-1643.
100. Takamiya K., Yamamoto A., Yamashiro S., Furukawa K., Haraguchi M., Okada M., Ikeda T., Shiku H., Furukawa K. T cell receptor-mediated stimulation of mouse thymocytes induces up-regulation of the GM2/GD2 synthase gene. FEBS Lett. 358:1995;79-83.
101. Gu X., Preuss U., Gu T., Yu R.K. Regulation of sialyltransferase activities by phosphorylation and dephosphorylation. J. Neurochem. 64:1995;2295-22302.
102. Bieberich E., Freischutz B., Liour S.S., Yu R.K. Regulation of ganglioside metabolism by phosphorylation and dephosphorylation. J. Neurochem. 71:1998;972-979.
103. Abeijon C., Mandon E.C., Hirschberg C.B. Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus. Trends Biochem. Sci. 22:1997;203-207.
104. Abeijon C., Yanagisawa K., Mandon E.C., Hausler A., Moremen K., Hirschberg C.B., Robbins P.W. Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae. J. Cell Biol. 122:1993;307-323.
105. Toma L., Pinhal M.A., Dietrich C.P., Nader H.B., Hirschberg C.B. Transport of UDP-galactose into the Golgi lumen regulates the biosynthesis of proteoglycans. J. Biol. Chem. 271:1996;3897-38901.
106. Brandli A.W., Hansson G.C., Rodriguez-Boulan E., Simons K. A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex. J. Biol. Chem. 263:1988;16283-16290.
107. Martina J.A., Maccioni H.J.F. UDP sugar pyrophosphatase of rat retina. Subcellular localization and topography. J. Neurosci. Res. 46:1996;485-491.
108. Daniotti J.L., Landa C.A., Gravotta D., Maccioni H.J.F. GD3 ganglioside is prevalent in fully differentiated neurons from rat retina. J. Neurosci. Res. 26:1990;436-446.
109. Coetzee T., Fujita N., Dupree J., Shi R., Blight A., Suzuki K., Suzuki K., Popko B. Myelination in the absence of galactocerebroside and sulfatide: normal structure with abnormal function and regional instability. Cell. 86:1996;209-219.
110. Bosio A., Binczek E., Stoffel W. Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis. Proc. Natl. Acad. Sci. USA. 93:1996;13280-13285.
111. Takamiya K., Yamamoto A., Furukawa K., Yamashiro S., Shin M., Okada M., Fukumoto S., Haraguchi M., Takeda N., Fujimura K., Sakae M., Kishikawa M., Shiku H., Furukawa K., Aizawa S. Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system. Proc. Natl. Acad. Sci. USA. 93:1996;10662-10667.
112. Ichikawa S., Nakajo N., Sakiyama H., Hirabayashi Y. A mouse B16 melanoma mutant deficient in glycolipids. Proc. Natl. Acad. Sci. USA. 91:1994;2703-2707.
113. Hidari K.I.P.J., Ichikawa S., Fujita T., Sakiyama H., Hirabayashi Y. Complete removal of sphingolipids from the plasma membrane disrupts cell to substratum adhesion of mouse melanoma cells. J. Biol. Chem. 271:1996;14636-14641.
114. Zheng M., Fang H., Tsuruoka T., Tsuji T., Sasaki T., Hakomori S. Regulatory role of GM3 ganglioside in alpha 5 beta 1 integrin receptor for fibronectin-mediated adhesion of FUA169 cells. J. Biol. Chem. 268:1993;2217-2222.
115. van der Bijl P., Strous G.J., Lopes-Cardozo M., Thomas-Oates J., van Meer G. Synthesis of non hydroxy-galactosylceramides and galactosyldiglycerides by hydroxy-ceramide galactosyltransferase. Biochem. J. 317:1996;589-597.
116. Nores G.A., Caputto R. Inhibition of the UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyl transferase by gangliosides. J. Neurochem. 42:1984;1205-1211.
117. Bussolino D.F., Guido M.E., Caputto B.L. Light exposure stimulates the activity of ganglioside glycosyltransferases of retina ganglion cells. Neurochem. Int. 31:1997;105-111.
118. Yusuf H.K., Schwarzmann G., Pohlentz G., Sandhoff K. Oligosialogangliosides inhibit GM2- and GD3-synthesis in isolated Golgi vesicles from rat liver. Biol. Chem. Hoppe Seyler. 368:1987;455-462.
119. Iber H., van Echten G., Klein R.A., Sandhoff K. pH-dependent changes of ganglioside biosynthesis in neuronal cells in culture. Eur. J. Cell Biol. 52:1990;236-240.
120. Quiroga S., Caputto R. An inhibitor of the UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyltransferase: purification and properties, and preparation of an antibody to this inhibitor. J. Neurochem. 50:1988;1695-1700.
121. Quiroga S., Panzetta P., Caputto R. An endogenous inhibitor of N-acetylgalactosaminyltransferase inhibits retina neuron differentiation in culture. Brain Res. 508:1990;337-340.
122. Grabois V.R., Conde C.B., Caputto R. Effects of the N-acetylgalactosaminyl-transferase inhibitor on cultured cerebral cells. J. Neurosci. Res. 39:1994;330-338.
123. Kivatinitz S.C., Grabois V.R., Quiroga S. High-density lipoprotein inhibits UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyltransferase and differentiation of cultured cerebral cells: comparison with a formerly described inhibitor of this enzyme. J. Neurochem. 65:1995;775-781.
124. Conde C.B., Grabois V.R., Deza S.N., Caputto B.L. Identification of an endogenous inhibitor of the UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyl transferase as apolipoprotein A1. Neurochem. Res. 22:1997;483-490.
125. Cole N.B., Smith C.L., Sciaky N., Terasaki M., Edidin M., Lippincott-Schwartz J. Diffusional mobility of Golgi proteins in membranes of living cells. Science. 273:1996;797-801.
126. Lippincott-Schwartz J., Cole N., Presley J. Unravelling Golgi membrane traffic with green fluorescent protein chimeras. Trends Cell Biol. 8:1998;16-20.
127. Maggio B. The surface behavior of glycosphingolipids in biomembranes: a new frontier of molecular ecology. Prog. Biophys. Mol. Biol. 62:1994;55-117.
128. Brown R.E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111:1998;1-9.
129. Yu R.K., Ando S. Structures of some new complex gangliosides of fish brain. Adv. Exp. Med. Biol. 125:1980;33-45.
130. Maccioni H.J.F., Fritz V.R., Maxzud M.K., Daniotti J.L., Martina J.A. Compartmental organization of ganglioside synthesis in the Golgi complex. Biocell. 20:1996;279-286.
131. S. Ichikawa, H. Sakiyama, G. Suzuki, K.I. Hidari, Y. Hirabayashi, Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis, Proc. Natl. Acad. Sci. USA 93 (1996) 12654. Published erratum.
132. Sango K., Johnson O.N., Kozak C.A., Proia R.L. Beta-1,4-N-Acetylgalactosaminyl-transferase involved in ganglioside synthesis: cDNA sequence, expression, and chromosome mapping of the mouse gene. Genomics. 27:1995;362-365.
133. Hidari J.K., Ichikawa S., Furukawa K., Yamasaki M., Hirabayashi Y. Beta 1-4-N-acetylgalactosaminyltransferase can synthesize both asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo: isolation and characterization of a beta 1-4-N-acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell line AH7974F. Biochem. J. 303:1994;957-965.
134. Watanabe Y., Nara K., Takahashi H., Nagai Y., Sanai Y. The molecular cloning and expression of alpha 2,8-sialyltransferase (GD3 synthase) in a rat brain. J. Biochem. 120:1996;1020-1027.
135. Kono M., Yoshida Y., Kojima N., Tsuji S. Molecular cloning and expression of a fifth type of alpha2,8-sialyltransferase (ST8Sia V). Its substrate specificity is similar to that of SAT-V/III, which synthesize GD1c, GT1a, GQ1b and GT3. J. Biol. Chem. 271:1996;29366-29371.
136. Haraguchi M., Yamashiro S., Yamamoto A., Furukawa K., Takamiya K., Lloyd K.O., Shiku H., Furukawa K. Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2,8-sialyltransferase cDNA using anti-GD2 monoclonal antibody. Proc. Natl. Acad. Sci. USA. 91:1994;10455-10459.
137. Iber H., van Echten G., Sandhoff K. Substrate specificity of alpha 2-3-sialyltransferases in ganglioside biosynthesis of rat liver Golgi. Eur. J. Biochem. 195:1991;115-120.
138. Kitagawa H., Paulson J.C. Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J. Biol. Chem. 269:1994;1394-1401.
139. Kim Y.J., Kim K.S., Kim S.H., Kim C.H., Ko J.H., Choe I.S., Tsuji S., Lee Y.C. Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-sialyltransferase (hST3Gal II). Biochem. Biophys. Res. Commun. 228:1996;324-327.
140. van Meer G. Lipids of the Golgi membrane. Trends Cell Biol. 8:1998;29-33.
141. Svennerholm L. Chromatographic separation of human brain gangliosides. J. Neurochem. 10:1963;613-623.
142. Ishii A., Ohta M., Watanabe Y., Matsuda K., Ishiyama K., Sakoe K., Nakamura M., Inokuchi J., Sanai Y., Saito M. Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase. J. Biol. Chem. 273:1998;31652-31655.