Identification of rat α1 macroglobulin as an inhibitor of rat Galβ1-4GlcNAc α2-6 sialyltransferase

Glycobiology

Volumn 7, Issue 6, 1997, Pages 791-801

  Harder, P Gwen ^a   Jamieson, James C ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

Author keywords

1 macroglobulin; Acute phase response; Glycosyltransferase inhibitor; Molecular trapping; Sialyltransferase

Indexed keywords

ENZYME INHIBITOR; GLYCOSYLTRANSFERASE; MACROGLOBULIN; SIALYLTRANSFERASE; ALPHA 2 MACROGLOBULIN; BETA D GALACTOSIDE ALPHA 2 6 SIALYLTRANSFERASE; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE;

ACUTE PHASE RESPONSE; ARTICLE; ENZYME INHIBITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; RAT; SERUM; AMINO ACID SEQUENCE; ANIMAL; BLOOD; DRUG ANTAGONISM; ENZYME SPECIFICITY; HYDROLYSIS; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; KINETICS; MALE; METABOLISM; MOLECULAR GENETICS;

ALPHA-MACROGLOBULINS; AMINO ACID SEQUENCE; ANIMALS; CHROMATOGRAPHY, DEAE-CELLULOSE; ENZYME INHIBITORS; HYDROLYSIS; KINETICS; MALE; MOLECULAR SEQUENCE DATA; RATS; SIALYLTRANSFERASES; SUBSTRATE SPECIFICITY;

EID: 0030612556     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.6.791     Document Type: Article

References (102)

1. Albarracin, I., Lassaga, F.E. and Caputto, R. (1988) Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate:lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biohem. J., 254, 559-565.
2. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. and Lipman, D.J. (1990) Basic local alignment search tool. J. Mol. Biol., 215, 403-410.
3. Andrews, P. (1965) The gel-filtration behavior of proteins related to their molecular weights over a wide range. Biochem. J., 96, 595-606.
4. Ashton, F.E., Jamieson, J.C. and Friesen, A.D. (1970) Studies on the effect of inflammation on rat serum proteins. Can. J. Biochem., 48, 841-850.
5. 2-macroglobulin with proteinases. Characteristics and specificty of the reaction, and a hypothesis concerning its molecular mechanism. Biochem. J., 133, 709-724.
6. Bernacki, R.J. and Kim, U. (1977) Concomitant elevations in serum sialyltransferase activity and sialic acid content in rats with metastasizing mammary tumors. Science, 195, 577-580.
7. Bonner, J.C., Hoffman, M. and Brody, A.R. (1989) Alpha-macroglobulin secreted by alveolar macrophages serves as a binding protein for a macrophage-derived homologue of platelet-derived growth factor. Am. J. Respir. Cell Mol. Biol., 1, 171-179.
8. 2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J., 6, 3345-3353.
9. Borth, W., Scheer, B., Urbansky, A., Luger, T.A. and Sottup-Jensen, L. (1990) Binding of IL-1β to α-macroglobulins and release by thioredoxin. J. Immunol., 145, 3747-3754.
10. 1-inhibitor III messenger RNA. J. Biol. Chem., 263, 3999-4012.
11. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
12. Broquet, P., Baubichon-Cortay, H., George, P. and Louisot, P. (1991) Glycoprotein sialyltransferases in eucaryotic cells. Int. J. Biochem., 23, 385-389.
13. Collard, J.G., Schijven, J.F., Bikker, A., La Riviere, G., Bolscher, J.G.M. and Roos, E. (1986) Cell surface sialic acid and the invasive and metastatic potential of T-cell hybridomas. Canc. Res., 46, 3521-3527.
14. Constantino-Ceccarini, E. and Suzuki, K. (1978) Isolation and partial characterization of an endogenous inhibitor of ceramide glycosyltransferases from rat brain. J. Biol. Chem., 253, 340-342.
15. Corfield, A.P. and Schauer, R. (1982) Metabolism of sialic acids. In Schauer, R., (ed.), Sialic Acids. Chemistry, Metabolism and Function. Cell Biology Monographs, Vol. 10, Springer-Verlag Wien, New York, pp. 195-261.
16. 2-macroglobulin. Biochem. Biophys. Res. Commun., 200, 1578-1585.
17. 2-macroglobulin-trypsin complex in the rat is mainly accounted for by uptake into hepatocytes. Biochim. Biophys. Acta, 846, 85-92.
18. Debanne, M.T., Bell, R. and Dolovich, J. (1975) Uptake of proteinase-α-macroglobulin complexes by macrophages. Biochim. Biophys. Acta, 411, 295-304.
19. De Beer, F.C., Baltz, M.L., Munn, E.A., Feinstein, A., Taylor, J., Bruton, C., Clamp, J.R. and Pepys, M.B. (1982) Isolation and characterization of C-reactive protein and serum amyloid P component in the rat. Immunology, 45, 55-70.
20. 2-macroglobulin by activated human polymorphonuclear leukocytes. Mediat. Inflamm., 3, 117-123.
21. Delannoy, P., Pelczar, H., Van Damme, V. and Verbert, A. (1993) Sialyltransferase activity in FR3T3 cells transformed with ras oncogene: decreased CMP-Neu5Ac:Galβ1-3GalNAc α-2,3-sialyltransferase. Glycoconj. J., 10, 91-98.
22. 2-Macroglobulin is a binding protein for basic fibroblast growth factor. J Biol. Chem. 264, 7210-7216.
23. Duffard, R.O., and Caputto, R. (1972) A natural inhibitor of sialyl transferase and its possible influence on this enzyme activity during brain development. Biochemistry, 11, 1396-1400.
24. 1-macroglobulin, a broad-range proteinase inhibitor from the α-macroglobulin-complement family. Mol. Biol. Med., 8, 287-302.
25. Elbein, A.D. (1987a) Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem., 56, 497-534.
26. Elbein, A.D. (1987b) Glycosylation inhibitors for N-linked glycoproteins. Methods Enzymol., 138, 661-709.
27. Elbein, A.D. (1991) Inhibitors of the addition, modification or procesing of the oligosaccharide chains of the N-linked glycoproteins. In Ginsburg, V. and Robbins, P.W. (eds.), Biology of Carbohydrates, Vol. 3. JAI Press, London, pp. 119-177.
28. 2-macroglobulin as trypsin-protein esterase. Clin. Chim. Acta, 14, 493-501.
29. 1-macroglobulin. Identification of an intracellular precursor. J. Biol. Chem., 262, 4973-4977.
30. Gordon, A.H. (1976) The α-macroglobulins of rat serum. Biochem. J., 159, 643-650.
31. Goss, P.E., Baker, M.A., Carver, J.P. and Dennis, J.W. (1995) Inhibitors of carbohydrate processing: a new class of anticancer agents. Clin. Canc. Res., 1, 935-944.
32. Hall, M. and Söderhäll, K. (1994) Crayfish α-macroglobulin as a substrate for transglutaminases. Comp. Biochem. Physiol., 108B, 65-72.
33. Harder, P.G., Jamieson, J.C. and Woloski, B.M.R.N.J. (1990) Stimulation of release of Galβ1-4GlcNAcα2-6 sialyltransferase from the Faza hepatoma cell line by dexamethasone and phorbol ester. Int. J. Biochem., 22, 11-14.
34. Hendrickson, T.L., Spencer, J.R., Kato, M. and Imperiali, B. (1996) Design and evaluation of potent inhibitors of asparagine-linked protein glycosylation. J. Am. Chem. Soc., 118, 7636-7637.
35. Huang, J.S. (1989) Alpha-2-macroglobulin - a modulator for growth factors? Am. J. Respir. Cell Mol. Biol., 1, 169-170.
36. 2 macroglobulin and its possible importance in immune systems. Trends Biochem. Sci., 5, 43-47.
37. 2-macroglobulin. Immunol. Today, 11, 163-166.
38. 2-macroglobulin. Can. J. Biochem., 50, 856-870.
39. Jamieson, J.C., Kaplan, H.A., Woloski, B.M.R.N.J., Hellman, M. and Ham, K. (1983) Glycoprotein biosynthesis during the acute phase response to inflammation. Can. J. Biochem. Cell Biol., 61, 1041-1048.
40. Jamieson, J.C. McCaffrey, G. and Harder, P.G. (1993) Sialyltransferase - a novel acute-phase reactant. Comp. Biochem. Physiol. 105B, 29-33.
41. 2-macroglobulin receptor. Eur. J. Biochem., 220, 819-826.
42. Kaplan, H.A., Woloski, B.M.R.N.J., Hellman, M. and Jamieson, J.C. (1983) Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of Galβ1→4GlcNAc α2→6 sialyltransferase from liver. J. Biol. Chem., 258, 11505-11509.
43. Kolb-Bachofen, V. (1991) A membrane-bound form of the acute phase protein C-reactive protein is the galactose-specific particle receptor on rat liver macrophages. Pathobiology, 59, 272-275.
44. 2-macroglobulin as a growth hormone-binding protein in human blood. J. Clin. Endocrinol. Metab., 80, 585-590.
45. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
46. 2-macroglobulins. Lab. Invest., 65, 3-14.
47. Lammers, G. and Jamieson, J.C. (1986) Studies on the effect of experimental inflammation on sialyltransferase in the mouse and guinea pig. Comp. Biochem. Physiol., 84B, 181-187.
48. Lammers, G. and Jamieson, J.C. (1988) The role of a cathepsin D-like activity in the release of Galβ1-4GlcNAc α2-6-sialyltransferase from rat liver golgi membranes during the acute-phase response. Biochem. J., 256, 623-631.
49. Lammers, G. and Jamieson, J.C. (1989) Studies on the effect of lysosomotropic agents on the release of Galβ1-4GlcNAc α-2,6-sialyltransferase from rat liver slices during the acute-phase response. Biochem. J., 261, 389-393.
50. Lammers, G. and Jamieson, J.C. (1990) Cathepsin D-like activity in the release of Galβ1-4GlcNAcα2-6sialyltransferase from mouse and guinea pig liver golgi membranes during the acute phase response. Comp. Biochem. Physiol., 95B, 327-334.
51. LeGendre, N. and Matsudaira, P. (1988) Direct protein microsequencing from Immobilon-P transfer membrane. BioTechniques, 6, 154-159.
52. 2-macroglobulin. J. Biol. Chem., 270, 8381-8384.
53. Le Marer, N. and Stehelin, D. (1995) High alpha-2,6-sialylation of N-acetyllactosamine sequences in ras-transformed rat fibroblasts correlates with high invasive potential. Glycobiology, 5, 219-226.
54. Le Marer, N., Laudet, V., Svensson, E.C., Cazlaris, H., Van Hille, B., Lagrou, C., Stehelin, D., Montreuil, J., Verbert, A. and Delannoy, P. (1992) The c-Ha-ras oncogene induces increased expression of β-galactoside α-2,6-sialyltransferase in rat fibroblast (FR3T3) cells. Glycobiology, 2, 49-56.
55. 2-macroglobulin inhibits choline acetyltransferase of embryonic basal forebrain neurons and reversal of the inhibition by NGF and BDNF but not NT-3. J. Neurosci. Res., 38, 407-414.
56. Lonberg-Holm, K., Reed, D.L., Roberts, R.C, Hebert, R.R., Hillman, M.C. and Kulney, R.M. (1987) Three high molecular weight protease inhibitors of rat plasma. Isolation, characterization, and acute phase changes. J. Biol. Chem., 262, 438-445.
57. Martin, A., Ruggiero-Lopez, D., Biol, M.C. and Louisot, P. (1990) Evidence for the presence of an endogenous cytosolic protein inhibitor of intestinal fucosyltransferase activities. Biochem. Biophys. Res. Commun., 166, 1024-1031.
58. McCaffrey, G. and Jamieson, J.C. (1993) Evidence for the role of a cathepsin D-like activity in the release of Galβ1-4GlcNAcα2-6sialyltransferase from rat and mouse liver in whole-cell systems. Comp. Biochem. Physiol., 104B, 91-94.
59. 2-macroglobulin signaling receptor on macrophages induces synthesis of platelet activating factor. J. Cell Biochem., 61, 39-47.
60. 2-macroglobulin signaling receptor induces second messengers. J. Cell. Biochem., 61, 61-71.
61. Nelles, L.P. and Schnebli, H.P. (1982) Subunit structure of the rat α-macroglobulin proteinase inhibitors. Hoppe-Seyler's Z. Physiol. Chem., 363, 677-682.
62. 2-macroglobulin gene. Biochemistry, 27, 9194-9203.
63. 2-macroglobulin. J. Biol. Chem., 262, 14090-14099.
64. 2-macroglobulin interaction. Eur. J. Biochem., 221, 687-693.
65. Pilatte, Y., Bignon, J. and Lambré, C.R. (1993) Sialic acids as important molecules in the regulation of the immune system: pathophysiological implications of sialidases in immunity. Glycobiology, 3, 201-218.
66. Pizzo, S.V., and Gonias, S.L. (1984) Receptor-mediated protease regulation. In Conn, P.M. (ed.), The Receptors, Vol. 1. Academic Press, New York, pp. 177-221.
67. 2-macroglobulin. J. Biol. Chem., 264, 9850-9858.
68. Qiao, L., Murray, B.W., Shimazaki, M., Schultz, J. and Wong, C.-H. (1996) Synergistic inhibition of human α-1,3-fucosyltransferase V. J. Am. Chem. Soc., 118, 7653-7662.
69. Quiroga, S. and Caputto, R. (1988) An inhibitor of the UDP-N-acetylgalactosamine:GM3, N-acetylgalactosaminyltransferase: purification and properties, and preparation of an antibody to this inhibitor. J. Neurochem., 50, 1695-1700.
70. Quiroga, S., Caputto, B.L. and Caputto, R. (1984) Inhibition of the chicken retinal UDP-GalNAc:GM3, N-acetylgalatosaminyltransferase by blood serum and by pineal gland extracts. J. Neurosci. Res., 12, 269-276.
71. Quiroga, S., Panzetta, P. and Caputto, R. (1990) An endogenous inhibitor of N-acetylgalactosaminyltransferase inhibits retina neuron differentiation in culture. Brain Res., 508, 337-340.
72. Rassouli, M., Sambasivam, H., Azadi, P., Dell, A., Morris, H.R., Nagpurkar, A., Mookerjea, S. and Murray, R.K. (1992) Derivation of the amino acid sequence of rat C-reactive protein from cDNA cloning with additional studies on the nature of its dimeric component. J. Biol. Chem., 267, 2947-2954.
73. Reuter, G. and Gabius, H.-J. (1996) Sialic acids. Structure-analysis-metabolism-occurrence-recognition. Biol. Chem. Hoppe-Seyler, 377, 325-342.
74. Reutter, W., Kottgen, E., Bauer, C. and Gerok, W. (1982) Biological significance of sialic acids. In Schauer, R. (ed.), Sialic Acids. Chemistry, Metabolism and Function, Cell Biology Monographs, Vol. 10. Springer-Verlag Wien, New York, pp. 263-305.
75. Richardson, K. and Jamieson, J.C. (1995) Release of sialyltransferases from rat liver Golgi membranes by a cathepsin D-like proteinase: comparison of the release of Galβ1-4GlcNAcα2-6 sialyltransferase. Galβ1-3(4)GlcNAcα2-3 sialyltransferase and lactosylceramide α2-3 sialyltransferase (SAT-1). Comp. Biochem. Physiol., 110B, 445-450.
76. Roth, J. (1993) Cellular sialoglycoconjugates: a histochemical perspective. Histochem. J., 25, 687-710.
77. Salvesen, G. and Enghild, J.J. (1993) α-Macroglobulins: detection and charac-terization. Methods Enzymol., 223, 121-141.
78. Sambasivam, H., Rassouli, M. Murray, R.K., Nagpurkar, A., Mookerjea, S., Azadi, P., Dell, A. and Morris, H.R. (1993) Studies on the carbohydrate moiety and on the biosynthesis of rat C-reactive protein. J. Biol. Chem., 268, 10007-10016.
79. 2-macroglobulins. Biochem. Biophys. Res. Commun., 108, 1-7
80. Schauer, R. (1982) Chemistry, metabolism, and biological functions of sialic acids. Adv. Carbohydr. Chem. Biochem., 40, 131-234.
81. Schauer, R. (1985) Sialic acids and their role as biological masks. Trends Biochem. Sci., 10, 357-360.
82. 2-macroglobulin and the binding is inhibited by heparin. J. Biol. Chem., 268, 7685-7691.
83. 2-Macroglobulin and related thiol ester plasma proteins. In Putnam, F.W. (ed.), The Plasma Proteins, 2nd ed., Vol 5. Academic Press, Orlando, FL, pp 191-291.
84. Sottrup-Jensen, L. (1989) α-Macroglobulins: structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem., 264, 11539-11542.
85. 2-macroglobulin-proteinase complexes. Nature of the high molecular weight cross-linked products J. Biol. Chem., 265, 17727-17737.
86. Sottrup-Jensen, L., Sand, O., Kristensen, L. and Fey, G.H. (1989) The α-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian α-macroglobulins. J. Biol. Chem., 264, 15781-15789.
87. Sticher, U., Gross, H.J. and Brossmer, R. (1988) Purification of α2,6-sialyltransferase from rat liver by dye chromatography. Biochem. J., 253, 577-580.
88. Travis, J. and Salvesen, G.S. (1983) Human plasma proteinase inhibitors. Annu. Rev. Biochem., 52, 655-709.
89. 1-macroglobulin-proteinase complex endocytosed into rat liver lysosomes. Biochem. J., 298, 79-85.
90. Tsuji, S. (1996) Molecular cloning and functional anlaysis of sialyltransferases. J. Biochem., 120, 1-13.
91. Twining, S.S. (1984) Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal. Biochem., 143, 30-34.
92. Van den Eijnden, D.H. and Schiphorst, W.E.C.M. (1988) Specificity and inhibition of sialyltransferases. Sialic Acids 1988, Proc. Jpn.-Ger. Symp., 128-129.
93. 2-macroglobulin receptor in human fibroblasts, absent in tumor-derived cell lines. J. Biol. Chem., 254, 5155-5160.
94. Verdon, B. and Berger, E.G. (1983) Galactosyltransferase. In Bergmeyer, H.U., (ed.), Methods of Enzymatic Analysis, Vol. 3. Verlag Chemie, Weinheim, pp. 374-381.
95. 2-macroglobulin. Biochem. J., 300, 443-448.
96. 1-macroglobulin. Biochemistry, 31, 2346-2352.
97. Webb, D.J., Crookston, K.P., Figler, N.L., La Marre, J. and Gonias,S.L. (1995) Differences in the binding of transforming growth factor β1 to the acute-phase reactant and constitutively synthesized α-macroglobulins of rat. Biochem. J., 312, 579-586.
98. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982) Purification of a Galβ1→4GlcNAc α2→6 sialyltransferase and a Galβ1→3(4)GlcNAc α2→3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem., 257, 13835-13844.
99. 2-macroglobulin under apparent equilibrium conditions. Biochemistry, 33, 11270-11277.
100. 1-acid glycoprotein and β-N-acetylhexosaminidase. Biochem. Biophys. Res. Commun., 130, 30-36.
101. Woloski, B.M.R.N.J., Fuller, G.M., Jamieson, J.C. and Gospodarek, E. (1986) Studies on the effect of the hepatocyte-stimulating factor on galactose-β1→4-N-acetylglucosamine α2→6-sialyltransferase in cultured hepatocytes. Biochim. Biophys. Acta, 885, 185-191.
102. Yogeeswaran, G. and Salk, P.L. (1981) Metastatic potential is positively correlated with cell surface sialylation of cultured murine tumor cell lines. Science, 212, 1514-1516.