Differential recognition of glycoprotein acceptors by terminal glycosyltransferases

Glycobiology

Volumn 7, Issue 2, 1997, Pages 241-251

  Yeh, Jiunn Chern ^a   Cummings, Richard D ^a  

^a UNIVERSITY OF OKLAHOMA HEALTH SCIENCES CENTER   (United States)

Author keywords

Galactosyltransferases; Glycoproteins; Glycosyltransferases; Sialyltransferases

Indexed keywords

GALACTOSYLTRANSFERASE; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; SIALYLTRANSFERASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOHYDRATE ANALYSIS; CHO CELL; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; IN VITRO STUDY; LIVER; MUTANT; NONHUMAN; PRIORITY JOURNAL; RAT; REACTION ANALYSIS;

AMINO SUGARS; ANIMALS; CHO CELLS; CHROMATOGRAPHY, AFFINITY; CRICETINAE; GALACTOSE; GALACTOSYLTRANSFERASES; GLYCOPEPTIDES; GLYCOPROTEINS; GLYCOSYLATION; LECTINS; LIVER; MICE; POLYSACCHARIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; RATS; SIALYLTRANSFERASES; SUBSTRATE SPECIFICITY;

EID: 0030963571     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.2.241     Document Type: Article

References (82)

1. Aruffo, A., Kanner, S.B., Sgroi, D., Ledbetter, J.A. and Stamenkovic, I. (1992) CD22-mediated stimulation of T cells regulates T-cell receptor/CD3-induced signaling. Proc. Natl. Acad. Sci. USA, 89, 10242-10246.
2. Baenziger, J.U. (1994) Protein-specific glycosyltransferases: how and why they do it! FASEB J., 8, 1019-1025.
3. Baenziger, J.U. and Fiete, D. (1979) Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. J Biol. Chem., 254, 9795-9799.
4. Baranski, T.J., Koelsch, G., Harsuck, J.A., and Kornfeld, S. (1991) Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting. J. Biol. Chem., 266, 23365-23372.
5. Baranski, T.J., Cantor, A.B. and Kornfeld, S. (1992) Lysosomal enzyme phosphorylation. I. Protein recognition determinants in both lobes of procathepsin D mediate its interaction with UDP-GlcNAc: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. J. Biol. Chem., 267, 23342-23348.
6. Beyer, T.A., Rearick, J.I., Paulson, J.C, Prieels J.P., Sadler, J.E. and Hill, R.L. (1979) Biosynthesis of mammalian glycoproteins. Glycosylation pathways in the synthesis of the nonreducing terminal sequences. J. Biol. Chem., 254, 12531-12534.
7. Beyer, T.A., Sadler, J.C., Rearick, J.I., Paulson, J.C., and Hill, R.L. (1981) Glycosyltransferases and their use in assessing oligosaccharide structure and structure-function relationships. Adv. Enzymol., 52, 23-175.
8. Cantor, A.B., Baranski, T.J. and Kornfeld, S. (1992) Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides. J. Biol. Chem., 267, 23349-23356.
9. Cantor, A.B. and Kornfeld, S. (1992) Phosphorylation of Asn-linked oligosaccharides located at novel sites on the lysosomal enzyme cathepsin D. J. Biol. Chem., 267, 23357-23363.
10. Cho, S.K., Yeh, J.-C., Cho, M. and Cummings, R.D. (1996) Transcriptional regulation of α1,3-Galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis x antigens by α-galactosylation. J. Biol. Chem., 271, 3238-3246.
11. Cummings, R.D. (1992) Synthesis of asparagine-linked oligosaccharides: pathways, genetics and metabolic regulation. In Allen, J.J. and Kisailus, E.C. (eds.), Glycoconjugates: Composition, Structure and Function. Marcel Dekker, New York, pp. 333-360.
12. Cummings, R.D. and Kornfeld, S. (1982) Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography. J. Biol. Chem., 257, 11235-11240.
13. R 2.1: binding of oligosaccharides containing these sequences to immobilized Datura stramonium agglutinin. J. Biol. Chem., 259, 6253-6260.
14. Cummings, R.D. and Mattox, S.A. (1988) Retinoic acid-induced differentiation of the mouse teratocarcinoma cell line F9 is accompanied by an increase in the activity of UDP-galactose:β-g-Galactosyl-α1,3-galactosyltransferase. J. Biol. Chem., 263, 511-519.
15. Demetriou, M., Nabi, I.R., Coppolino, M., Dedhar, S. and Dennis, J.W. (1995) Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J. Cell Biol., 130, 383-392.
16. Deutscher, S.L., Nuwayhid, N., Stanley, P., Briles, E.I. and Hirschberg, C.B. (1984) Translocation across Golgi vesicle membranes: a CHO glycosylation mutant deficient in CMP-sialic acid transport. Cell, 39, 295-299.
17. Do, K.-Y., Smith, D.F., and Cummings, R.D. (1990) LAMP-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin. Biochem. Biophys. Res. Commun., 173, 1123-1128.
18. Do, K.-Y., Fregien, N., Pierce, M. and Cummings, R.D. (1994) Modification of glycoproteins by N-acetylglucosaminyltransferase V is greatly influenced by accessibility of the enzyme to oligosaccharide acceptors. J. Biol. Chem., 269, 23456-23464.
19. Elices, M.J. and Goldstein, I.J. (1989) Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing α-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell α(1,3)-galactosyltransferase. J. Biol. Chem., 264, 1375-1380.
20. Fukuda, M. and Fukuda, M.N. (1992) Cell surface carbohydrates in hematopoietic cell differentiation and malignancy. In Fukuda, M. (ed.), Cell Surface Carbohydrates and Cell Development. CRC Press, London, pp. 127-160.
21. Fukuda, M.N., Watanabe, K. and Hakomori, S. (1978) Release of oligosaccharides from various glycosphingolipids by endo-β-galactosidase. J. Biol. Chem., 253, 6814-6819.
22. Ginsburg, V. (1972) Enzymatic basis for blood groups in man. Adv. Enzymol. Rel. Areas Mol. Biol. 36, 131-149.
23. Granovsky, M., Bielfeldt, T., Peter, S., Paulsen, H., Meldal, M., Brockhausen, J. and Brockhausen, J. (1994) UDP-Galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates. Eur. J. Biochem., 221, 1039-1046.
24. 1H NMR spectroscopy. J. Biol. Chem., 263, 18253-18268.
25. Harduin-Lepers, A., Recchi, M.-A. and Delannoy, P. (1995) 1994, The year of sialyltransferases. Glycobiology, 5, 741-758.
26. Joziasse, D.H., Schiphorst, W.E., van den Eijnden, D., van Kuik, J.A., van Halbeek, H. and Vliegenthart, J.F. (1985) Branch specificity of bovine colostrum CMPsialic acid: N-acetyllactosaminide α2-6-sialyltransferase. Interaction with biantennary oligosaccharides and glycopeptides of N-glycosylproteins. J. Biol. Chem. 260, 714-719.
27. Joziasse, D.H., Schiphorst, W.E., van den Eijnden, D.H., van Kuik, J.A., van Halbeek, H. and Vliegenthart, J.F. (1987) Branch specificity of bovine colostrum CMP-sialic acid: Galβ1,4GlcNAc-R α2,6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type. J. Biol. Chem., 262, 2025-33.
28. Kitagawa, H. and Paulson, J.C. (1994) Differential expression of five sialyltransferase genes in human tissues. J. Biol. Chem., 269, 17872-17878.
29. Kobata, A. and Takasaki, S. (1992) Structure and biosynthesis of cell surface carbohydrates. In Fukuda, M. (ed.), Cell Surface Carbohydrates and Cell Developmen. CRC Press, London, pp. 1-24.
30. Kornfeld, S. (1986) Trafficking of lysosomal enzymes in normal and disease states. J. Clin. Invest., 77, 1-6.
31. Kornfeld, K., Reitman, M.L. and Kornfeld, R. (1981) The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. J. Biol. Chem., 256, 6633-6640.
32. Kornfeld, R. and Ferris, C. (1975) Interaction of immunoglobulin glycopeptides with concanavalin A. J. Biol. Chem., 250, 2614-2619.
33. Krusius, T., Finne, J. and Rauvala, H. (1976) The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin A-sepharose. FEBS Lett., 72, 117-120.
34. Larsen, R.D., Rajan, V.P., Ruff, M.M., Kukowaska-Latallo, J., Cummings, R.D. and Lowe, J.B. (1989) Isolation of a cDNA encoding a murine UDP-galactose:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide α1,3-galactosyltransferase: expression cloning by gene transfer. Proc. Natl. Acad. Sci. USA, 86, 8227-8231.
35. Lee., E.U., Roth., J. and Paulson., J.C. (1989) Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase. J. Biol. Chem., 264, 13848-13855.
36. Li, E., Gibson, R. and Kornfeld, S. (1980) Structure of an unusual complex-type oligosaccharide isolated from Chinese hamster ovary cells. Arch. Biochem. Biophys. 199, 393-399.
37. Li, F., Wilkins, P.P., Crawley, S., Weinstein, J., Cummings, R.D. and McEver, R.P. (1996) Post-translational modification of recombinant P-selectin glycoprotein ligand-1 required for binding to P-and E-selectin. J. Biol. Chem., 271, 3255-3264.
38. Lowe, J.B. (1991) Molecular cloning, expression, and uses of mammalian glycosyltransferases. Semin. Cell Biol., 2, 289-307.
39. Manzella, S.M., Hooper, L.V. and Baenziger, J.U. (1996) Oligosaccharides containing 1,4-linked N-acetylgalactosamine, a paradigm for protein-specific glycosylation. J. Biol. Chem., 271, 12117-12120.
40. Mattox, S., Walrath, K., Ceiler, D., Smith, D.F. and Cummings, R.D. (1992) A solid-phase assay for the activity of CMPNeuAc:Galβ1-4GlcNAc-R α2,6 sialyltransferase. Anal. Biochem., 206, 430-436.
41. McEver, R.P., Moore, K.L. and Cummings, R.D. (1995) Leukocyte trafficking mediated by selectin-carbohydrate interactions. J. Biol. Chem., 270, 11025-11028.
42. Merkle, R.K. and Cummings, R.D. (1988) Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin. J. Biol. Chem., 263, 16143-16149.
43. Montreuil, J. (1984) Spatial conformation of glycans and glycoproteins. Biol. Cell. 51, 115-132.
44. Nemansky, M. and van den Eijnden, D.H. (1993) Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta. Glycoconj. J., 10, 99-108.
45. Nemansky, M., Edzes, H.T., Wijnands, R.A. and van den Eijnden, D.H. (1992) The polypeptide part of human chorionic gonadotrophin affects the kinetics of α6-sialylation of its N-linked glycans but does not alter the branch specificity of CMP-NeuAc:Gal β1-4GlcNAc-R α2-6-sialyltransferase. Glycobiology, 2, 109-117.
46. Nemansky, M., DeLeeuw, R., Wijnands, R.A. and van den Eijnden, D.H (1995) Enzymic remodeling of the N-and O-linked carbohydrate chains of human chorionic gonadotropin. Effects on biological activity and receptor binding. Eur. J. Biochem., 227, 880-888.
47. Ogata, S., Muramatsu, T. and Kobata, A. (1975) Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose. J. Biochem. (Tokyo), 78, 687-696.
48. Orberger, G., Gessner, R., Fuchs, H., Volz, B., Kottgen, E. and Tauber, R. (1993) Enzymatic modeling of the oligosaccharide chains of glycoproteins immobilized onto polystyrene surfaces. Anal. Biochem., 214, 195-204.
49. Passaniti, A. and Hart, G.W. (1988) Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures. J. Biol. Chem., 263, 7591-7603.
50. 1-acid glycoprotein. J. Biol. Chem., 257, 12734-12738.
51. Paulson, J.C. and Colley, K.J. (1989) Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem., 264, 17615-17618.
52. Powell, L.D. and Varki, A. (1994) The oligosaccharide binding specificities of CD22β, a sialic acid-specific lectin of B cells. J. Biol. Chem., 269, 10628-10636.
53. Powell, L.D. and Varki, A. (1995) I-Type lectins. J. Biol. Chem., 270, 14243-14246.
54. Powell, L.D., Sgroi, D., Sjoberg, E.R., Stamenkovic, I. and Varki, A. (1993) Natural ligands of the B cell adhesion molecule CD22 β carry N-linked oligosaccharides with α-2,6 -linked sialic acids that are required for recognition. J. Biol. Chem., 268, 7019-7027.
55. Rademacher, T.W., Parekh, R.B. and Dwek, R.A. (1988) Glycobiology. Annu. Rev. Biochem., 57, 785-838.
56. Sato, T., Furukawa, K., Autero, M., Gahmberg, C.G. and Kobata, A. (1993) Structural study of the sugar chains of human leukocyte common antigen CD45. Biochemistry, 32, 12694-12704.
57. Schachter, H. (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell Biol. 64, 163-181.
58. Seppo, A., Penttila, L., Leppanen, A., Maaheimo, H., Niemela, R., Helin, J., Wieruszeski, J.M. and Renkonen, O. (1994) Bi-antennary oligo-(N-acetyllactosamino) glycans of I-type are galactosylated preferentially at the GlcNAc β1-6Gal linked arms by α 1,3-galactosyltransferase of bovine thymus. Glycoconj. J., 11, 217-225.
59. Sgroi, D., Koretzky, G.A. and Stamenkovic, I. (1995) Regulation of CD45 engagement by the B-cell receptor CD22. Proc. Natl. Acad. Sci. USA, 92, 4026-4030.
60. Shao, M.C. and Wold, F. (1995) The effect of the protein matrix proximity on glycan reactivity in a glycoprotein model. Eur. J. Biochem., 228, 79-85.
61. Shao, M.C., Sokolik, C.W. and Wold, F. (1994) Specificity studies of the GDP-L-fucose: 2-acetamido-2-deoxy-β-D-glucoside (FucvAsn-linked GlcNAc) 6-α-L-fucosyltransferase from rat-liver Golgi membranes. Carbohydrate Res., 251, 163-173.
62. Shibuya, N., Goldstein, I.J., Broekaert, W.F., Nsimba-Lubaki, M., Peeters, B. and Peumans, W.J. (1987) The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(α2-6)Gal/GalNAc sequence. J. Biol. Chem., 262, 1596-1601.
63. Smith, P.L. and Baenziger, J.U. (1992) Molecular basis of recognition by the glycoprotein hormone-specific N-acetylgalactosamine-transferase. Proc. Natl. Acad. Sci. USA, 89, 329-333.
64. Smith., D.F., Larsen., R.D., Mattox., S., Lowe., J.B. and Cummings., R.D. (1990) Transfer and expression of a murine UDP-Gal:β-D-Gal-α 1,3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the α 1,3-galactosyltransferase and the endogenous α 2,3-sialyltransferase. J. Biol. Chem., 265, 6225-6234.
65. Sousa, M.C., Ferrero-Garcia, M.A. and Parodi, A.J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry, 31, 97-105.
66. Spik, G., Bayard, B., Fourner, B., Strecker, G., Bouquelet, S. and Montreuil, J. (1975) Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin. FEBS Lett., 50, 296-299.
67. Spik, G., Coddeville, B., Mazurier, J., Bourne, Y., Cambillaut, C. and Montreuil, J. (1994) Primary and three-dimensional structure of lactotransferrin (lactoferrin) glycans. Adv. Exp. Med. Biol., 357, 21-32.
68. Thilo, L. (1983) Labeling of plasma membrane glycoconjugates by terminal glycosylation (galactosyltransferase and glycosidase). Methods Enzymol., 98, 415-421.
69. 1H-NMR to characterize glycosidase-treated glycopeptides. J. Biol. Chem., 257, 9704-9710.
70. Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130.
71. Vliegenthart, J.F.G., van Halbeek, H. and Dorland, L. (1981) Pure Appl. Chem., 53, 45-77.
72. Von Figura, K. and Hasilik, A. (1986) Lysosomal enzymes and their receptors. Annu. Rev. Biochem., 55, 167-193.
73. Wang, W.-C. and Cummings, R.D. (1988) The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing sialic acid-linked α2,3 to penultimate galactose residues. J. Biol. Chem., 263, 4576-4585.
74. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982a) Purification of a Galβ1-4GlcNAc α2-6 sialyltransferase and a Galβ1-3(4)GlcNAc α2-3sialyltransferase to homogeneity from rat liver. J. Biol. Chem., 257, 13835-13844.
75. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982b) Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Galβ1-3(4)GlcNAc α2-3sialyltransferase and a Galβ1-4GlcNAc α2-6 sialyltransferase from rat liver. J. Biol. Chem., 257, 13845-13853.
76. Whiteheart, S.W. and Hart, G.W. (1987) Sialyltransferases as specific cell surface probes of terminal and penultimate saccharide structures on living cells. Anal. Biochem., 163, 123-135.
77. Whiteheart, S.W., Passaniti, A., Reichner, J.S., Holt, G.D., Haltiwanger, R.S. and Hart, G.W. (1989) Glycosyltransferase probes. Methods Enzymol., 98, 82-95.
78. Whiteheart, S.W., McLenithan, J.C., and Hart, G.W. (1990) Surface of murine lymphocyte subsets differ in sialylation states and antigen distribution of a major N-linked penultimate saccharide structure. Cell Immunol., 125, 337-353.
79. Wilkins, P., McEver, R.P. and Cummings, R.D. (1996) Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J. Biol. Chem., 271, 18732-18742.
80. Yeh, J.-C. and Cummings, R.D. (1996) Absorbance-and light-based solid-phase assays for CMPNueAc:Galβ1-4GlcNAc-R α-2,3-sialyltransferase. Anal. Biochem., 236, 126-133.
81. Yeh, J.-C., Seals, J.R., Murphy, C.I., van Halbeek, H., and Cummings, R.D. (1993) Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry 32, 11087-11099.
82. 1-acid glycoproteins. J. Biol. Chem., 256, 8476-8484.