Uptake and incorporation of an epitope-tagged sialic acid donor into intact rat liver Golgi compartments. Functional localization of sialyltransferase overlaps with β-galactosyltransferase but not with sialic acid O-acetyltransferase

Molecular Biology of the Cell

Volumn 7, Issue 11, 1996, Pages 1691-1707

  Chammas, Roger ^d   McCaffery, J Michael ^d   Klein, André ^a   Ito, Yumi ^b   Saucan, Lucian ^d   Palade, George ^d   Farquhar, Marilyn G ^d   Varki, Ajit ^c  

^a INSERM   (France)

^b KANAGAWA DENTAL COLLEGE   (Japan)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d NONE

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; FLUORESCEIN ISOTHIOCYANATE; GALACTOSE; GALACTOSYLTRANSFERASE; GLYCOCONJUGATE; GLYCOPROTEIN; SIALIC ACID; SIALYLTRANSFERASE; URIDINE DIPHOSPHATE GALACTOSE;

ACETYLATION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; GOLGI COMPLEX; IMMUNOELECTRON MICROSCOPY; INTRAHEPATIC BILE DUCT; LIVER CELL; LIVER SINUSOID; NONHUMAN; PRIORITY JOURNAL; RAT;

ANIMALIA; SIA;

EID: 0029906774     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.11.1691     Document Type: Article

References (59)

1. Abeijon, C., and Hirschberg, C.B. (1990). Topography of initiation of N-glycosylation reactions. J. Biol. Chem. 265, 14691-14695.
2. Balch, W.E., Elliott, M.M., and Keller, D.S. (1986). ATP-coupled transport of vesicular stomatitis virus G protein between the endoplasmic reticulum and the Golgi. J. Biol. Chem. 267, 14681-14689.
3. Bergeron, J.J., Rachubinski, R.A., Sikstrom, R.A., Posner, B.I., and Paiement, J. (1982). Galactose transfer to endogenous acceptors within Golgi fractions of rat liver. J. Cell Biol. 92, 139-146.
4. Blouin, A., Bolender, R.P., and Weibel, E.R. (1977). Distribution of organelles and membranes between hepatocytes and nonhepatocytes in the rat liver parenchyma. A stereological study. J. Cell Biol. 72, 441-455.
5. Blum, A.S., and Barnstable, C.J. (1987). O-acetylation of a cell-surface carbohydrate creates discrete molecular patterns during neural development. Proc. Natl. Acad. Sci. USA 84, 8716-8720.
6. Burke, J., Pettitt, J.M., Humphris, D., and Gleeson, P.A. (1994). Medial-Golgi retention of N-acetylglucosaminyltransferase I. Contribution from all domains of the enzyme. J. Biol. Chem. 269, 12049-12059.
7. Butor, C., Diaz, S., and Varki, A. (1993). High level O-acetylation of sialic acids on N-linked oligosaccharides of rat liver membranes. Differential subcellular distribution of 7- and 9-O-acetyl groups and of enzymes involved in their regulation. J. Biol. Chem. 268, 10197-10206.
8. Carver, J.P., Michnick, S.W., Imberty, A., and Cumming, D.A. (1989). Oligosaccharide-protein interactions: a three-dimensional view. CIBA Found. Symp. 145, 6-18.
9. Chege, N.W., and Pfeffer, S.R. (1990). Compartmentation of the Golgi complex: brefeldin - A distinguishes trans-Golgi cisternae from the trans-Golgi network. J. Cell Biol. 111, 893-899.
10. D3 by human melanoma cells creates a unique antigenic determinant. Science 225, 844-846.
11. Diaz, S., Higa, H.H., Hayes, B.K., and Varki, A. (1989). O-Acetylation and de-O-acetylation of sialic acids: 7- and 9-O-acetylation of α2,6-linked sialic acids on endogenous N-linked glycans in rat liver Golgi vesicles. J. Biol. Chem. 264, 19416-19426.
12. Dunphy, W.G., Brands, R., and Rothman, J.E. (1985). Attachment of terminal N-acerylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the Golgi stack. Cell 40, 463-472.
13. Dunphy, W.G., and Rothman, J.E. (1985). Compartmental organization of the Golgi stack. Cell 42, 13-21.
14. Etchison, J.R., Srikrishna, G., and Freeze, H.H. (1995). A novel method to co-localize glycosaminoglycan-core oligosaccharide glycosyltransferases in rat liver Golgi. Co-localization of galactosyltransferase I with a sialyltransferase. J. Biol. Chem. 270, 756-764.
15. Freeze, H.H., Sampath, D., and Varki, A. (1993). α- and β-Xylosides alter glycolipid synthesis in human melanoma and Chinese hamster ovary cells. J. Biol. Chem. 268, 1618-1627.
16. Goldberg, D.E., and Kornfeld, S. (1983). Evidence for extensive subcellular organization of asparagine-linked oligosaccharide processing and lysosomal enzyme phosphorylation. J. Biol. Chem. 258, 3159-3165.
17. Griffiths, G., and Simons, K. (1986). The trans-Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438-443.
18. Gross, H.J. (1992). Fluorescent CMP-sialic acids as a tool to study the specificity of the CMP-sialic acid carrier and the glycoconjugate sialylation in permeabilized cells. Eur. J. Biochem. 203, 269-275.
19. Gross, H.J., and Brossmer, R. (1988). Enzymatic introduction of a fluorescent sialic acid into oligosaccharide chains of glycoproteins. Eur. J. Biochem. 177, 583-589.
20. 3H]N-acetylglucosamine. J. Biol. Chem. 268, 16139-16154.
21. 3H]N-acetylgalactosamine. J. Biol. Chem. 268, 16170-16178.
22. 3H]acetyl-coenzyme A. J. Biol. Chem. 268, 16155-16169.
23. Herrler, G., Rott, R., Klenk, H.D., Muller, H.P., Shukla, A.K., and Schauer, R. (1985). The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J. 4, 1503-1506.
24. Higa, H.H., Butor, C., Diaz, S., and Varki, A. (1989). O-Acetylation and de-O-acetylation of sialic acids. O-Acetylation of sialic acids in the rat liver Golgi apparatus involves an acetyl intermediate and essential histidine and lysine residues - a transmembrane reaction? J. Biol. Chem. 264, 19427-19434.
25. Higa, H.H., and Paulson, J.C. (1985). Sialylation of glycoprotein oligosaccharides with N-acetyl-, N-glycolyl-, and N-O-diacetyl-neuraminic acids. J. Biol. Chem. 260, 8838-8849.
26. Hirschberg, C.B., and Snider, M.D. (1987). Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 56, 63-87.
27. Kagiwada, S., Murata, M., Hishida, R., Tagaya, M., Yamashina, S., and Ohnishi, S. (1993). In vitro fusion of rabbit liver Golgi membranes with liposomes. J. Biol. Chem. 268, 1430-1435.
28. Klein, A., Krishna, M., Varki, N.M., and Varki, A. (1994). 9-O-acetylated sialic acids have widespread but selective expression: analysis using a chimeric dual-function probe derived from influenza C hemagglutinin-esterase. Proc. Natl. Acad. Sci. USA 91, 7782-7786.
29. Kornfeld, R., and Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
30. Leelavathi, D.E., Estes, L.W., Feingold, D.S., and Lombardi, B. (1970). Isolation of a Golgi-rich fraction from rat liver. Biochim. Biophys. Acta 211, 124-138.
31. Lugemwa, F.N., and Esko, J.D. (1991). Estradiol β-D-xyloside, an efficient primer for heparan sulfate biosynthesis. J. Biol. Chem. 266, 6674-6677.
32. Manzi, A.E., Diaz, S., and Varki, A. (1990a). High-pressure liquid chromatography of sialic acids on a pellicular resin anion-exchange column with pulsed amperometric detection: a comparison with six other systems. Anal. Biochem. 188, 20-32.
33. Manzi, A.E., Sjoberg, E.R., Diaz, S., and Varki, A. (1990b). Biosynthesis and turnover of O-acetyl and N-acetyl groups in the gangliosides of human melanoma cells. J. Biol. Chem. 265, 13091-13103.
34. Martina, J.A., Daniotti, J.L., and Maccioni, H.J.F. (1995). A UDP-sugar pyrophosphatase is developmentally regulated in the rat retina. J. Neurochem. 64, 1274-1280.
35. Maxzúd, M.K., Daniotti, J.L., and Maccioni, H.J.F. (1995). Functional coupling of glycosyl transfer steps for synthesis of gangliosides in Golgi membranes from neural retina cells. J. Biol. Chem. 270, 20207-20214.
36. Mellman, I., and Simons, K. (1992). The Golgi complex: in vitro veritas? Cell 68, 829-840.
37. Milla, M.E., and Hirschberg, C.B. (1989). Reconstitution of Golgi vesicle CMP-sialic acid and adenosine 3′-phosphate 5′-phosphosulfate transport into proteoliposomes. Proc. Natl. Acad. Sci. USA 86, 1786-1790.
38. Muchmore, E., and Varki, A. (1987). Inactivation of influenza C esterase decreases infectivity without loss of binding: a probe for 9-O-acetylated sialic acids. Science 236, 1293-1295.
39. Nilsson, T., Hoe, M.H., Slusarewicz, P., Rabouille, C., Watson, R., Hunte, F., Watzele, G., Berger, E.G., and Warren, G. (1994). Kin recognition between medial Golgi enzymes in HeLa cells. EMBO J. 23, 562-574.
40. Nilsson, T., Pypaert, M., Hoe, M.H., Slusarewicz, P., Berger, E.G., and Warren, G. (1993). Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol. 220, 5-13.
41. Powell, L.D., and Varki, A. (1996). Sialidases. In: Current Protocols in Molecular Biology, ed. F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl, L.M. Albright, D.M. Coen, and A. Varki, New York: John Wiley & Sons, unit 17.12.
42. Quinn, P., Griffiths, G., and Warren, G. (1983). Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin. J. Cell Biol. 96, 851-856.
43. Rogers, G.N., Herrler, G., Paulson, J.C., and Klenk, H.D. (1986). Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J. Biol. Chem. 261, 5947-5951.
44. Roth, J. (1991). Localization of glycosylation sites in the Golgi apparatus using immunolabeling and cytochemistry. J. Electron Microsc. Technol. 17, 121-131.
45. Roth, J., Taatjes, D.J., Lucocq, J.M., Weinstein, J., and Paulson, J.C. (1985). Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43, 287-295.
46. Roth, J., Taatjes, D.J., Weinstein, J., Paulson, J.C., Greenwell, P., and Watkins, W.M. (1986). Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J. Biol. Chem. 261, 14307-14312.
47. Sarkar, A.K., Fritz, T.A., Taylor, W.H., and Esko, J.D. (1995). Disaccharide uptake and priming in animal cells: inhibition of sialyl Lewis X by acetylated Galβ1→4GlcNAcβ-O-naphthalenemethanol. Proc. Natl. Acad. Sci. USA 92, 3323-3327.
48. Saucan, L., and Palade, G.E. (1994). Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers. J. Cell Biol. 525, 733-741.
49. Schauer, R. (1987). Analysis of sialic acids. Methods Enzymol. 138, 132-161.
50. Schultze, B., and Herrler, G. (1994). Recognition of cellular receptors by bovine coronavirus. Arch. Virol. 336 (suppl 9), 451-459.
51. Shibuya, N., Tazaki, K., Song, Z.W., Tarr, G.E., Goldstein, I.J., and Peumans, W.J. (1989). A comparative study of bark lectins from three elderberry (Sambucus) species. J. Biochem. 706, 1098-1103.
52. Sjoberg, E.R., and Varki, A. (1993). Kinetic and spatial interrelationships between ganglioside glycosyltransferases and O-acetyltransferase(s) in human melanoma cells. J. Biol. Chem. 268, 10185-10196.
53. Tabas, I., and Kornfeld, S. (1979). Purification and characterization of a rat liver Golgi alpha-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem. 254, 11655-11663.
54. Varki, A. (1992). Diversity in the sialic acids. Glycobiology 2, 25-40.
55. Varki, A., Hooshmand, F., Diaz, S., Varki, N.M., and Hedrick, S.M. (1991). Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetylesterase. Cell 65, 65-74.
56. Varki, A., and Kornfeld, S. (1980). An autosomal dominant gene regulates the extent of 9-O-acetylation of murine erythrocyte sialic acids. A probable explanation for the variation in capacity to activate the human alternate complement pathway. J. Exp. Med. 152, 532-544.
57. Velasco, A., Hendricks, L., Moremen, K.W., Tulsiani, D.R.P., Touster, O., and Farquhar, M.G. (1993). Cell type-dependent variations in the subcellular distribution of α-mannosidase I and II. J. Cell Biol. 222, 39-51.
58. Zimmer, G., Klenk, H.-D., and Herrler, G. (1995). Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin-Darby canine kidney cell line. J. Biol. Chem. 270, 17815-17822.
59. Zimmer, G., Suguri, T., Reuter, G., Yu, R.K., Schauer, R., and Herrler, G. (1994). Modification of sialic acids by 9-O-acetylation is detected in human leucocytes using the lectin property of influenza C virus. Glycobiology 4, 343-350.