Substrate specificities of recombinant murine Golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing α1,2-mannosidases

Glycobiology

Volumn 8, Issue 10, 1998, Pages 981-995

  Lal, Anita ^a   Pang, Peng ^b   Kalelkar, Sandeep ^a   Romero, Pedro A ^b   Herscovics, Annette ^b   Moremen, Kelley W ^a  

^a University of Georgia ^*  (United States)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

ER; Golgi; High mannose oligosaccharides; Mannosidase; N glycan processing; Recombinant expression

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; ALPHA MANNOSIDASE; ENZYME ANTIBODY; KIFUNENSINE; MANNOSE; RECOMBINANT ENZYME;

ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GOLGI COMPLEX; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOMER; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTON NUCLEAR MAGNETIC RESONANCE;

ANIMALS; CARBOHYDRATE SEQUENCE; ENDOPLASMIC RETICULUM; GOLGI APPARATUS; HYDROLYSIS; ISOENZYMES; LIVER; MANNOSIDASES; MICE; MOLECULAR SEQUENCE DATA; PICHIA; PRECIPITIN TESTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

MURINAE;

EID: 0031712231     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/8.10.981     Document Type: Article

References (57)

1. Al Daher, S., De Gasperi, R., Daniel, P., Hall, N., Warren, C.D. and Winchester, B. (1991) The substrate-specificity of human lysosomal α-D-mannosidase in relation to genetic α-mannosidosis. Biochem. J., 277, 743-751.
2. Al Daher, S., De Gasperi, R., Daniel, P., Hirani, S., Warren, C. and Winchester, B. (1992) Substrate specificity of human liver neutral α-mannosidase. Biochem. J., 286, 47-53.
3. Bause, E., Breuer, W., Schweden, J., Roeser, R. and Geyer, R. (1992) Effect of substrate structure on the activity of Man9-mannosidase from pig liver involved in N-linked oligosaccharide processing. Eur. J. Biochem., 208, 451-457.
4. Bischoff, J. and Kornfeld, R. (1983) Evidence for an α-mannosidase in endoplasmic reticulum of rat liver. J. Biol. Chem., 258, 7907-7910.
5. Bischoff, J. and Kornfeld, R. (1984) The effect of 1-deoxymannojirimycin on rat liver α-mannosidases. Biochem. Biophys. Res. Commun., 125, 324-331.
6. Bischoff, J., Liscum, L. and Kornfeld, R. (1986) The use of 1-deoxymannojirimycin to evaluate the role of various α-mannosidases in oligosaccharide processing in intact cells. J. Biol. Chem., 261, 4766-4774.
7. Briles, E.B., Li, E. and Kornfeld, S. (1977) Isolation of wheat germ agglutinin-resistant clones of Chinese hamster ovary cells deficient in membrane sialic acid and galactose. J. Biol. Chem., 252, 1107-1116.
8. Burke, J., Lipari, F. Igdoura, S. and Herscovics, A. (1996) The Saccharomyces cerevisiae processing α1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur. J. Cell Biol., 70, 298-305.
9. Byrd, J.C., Tarentino, A.L., Maley, F., Atkinson, P.H. and Trimble, R.B. (1982) Glycoprotein synthesis in yeast. Identification of Man8GlcNAc2 as an essential intermediate in oligosaccharide processing. J. Biol. Chem., 257, 14657-14666.
10. Chapman, A. and Kornfeld, R. (1979) Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides. J. Biol. Chem., 254, 816-23.
11. Chen, P.S., Toribara, T.Y. and Warner, H. (1956) Microdetermination of phosphorus. Anal. Chem., 28, 1756-1758.
12. Chui, D., Oh-Eda, M., Liao, Y., Panneerselvam, K., Lal, A., Marek, K., Freeze, H., Moremen, K., Fukuda, M. and Marth, J. (1997) Alpha-mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis. Cell, 90, 157-67.
13. Cohen, R. and Ballou, C. (1980) Linkage and sequence analysis of mannose-rich glycoprotein core oligosaccharides by proton nuclear magnetic resonance spectroscopy. Biochemistry, 19, 4345-58.
14. Cregg, J.M., Vedvick, T.S. and Raschke, W.C. (1993) Recent advances in the expression of foreign genes in Pichia pastoris. Bio/technology, 11, 905-910.
15. De Gasperi, R., Al Daher, S., Winchester, B. and Warren, C. (1992) Substrate specificity of the bovine and feline neutral α-mannosidases. Biochem. J., 286, 55-63.
16. Depierre, J., and Dallner, G. (1976) Isolation, subfractionation and characterization of the endoplasmic reticulum. In Maddy, A.H. (ed.), Biochemical Analysis of Membranes. John Wiley and Sons, New York, pp. 79-131.
17. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. and Smith, F. (1956) Colorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350-356.
18. Esmon, B., Esmon, P.C. and Schekman, R. (1984) Early steps in processing of yeast glycoproteins. J. Biol. Chem., 259, 10322-10327.
19. Forsee, W.T., Palmer, C.F. and Schutzbach, J.S. (1989) Purification and characterization of an α1,2-mannosidase involved in processing asparagine-linked oligosaccharides. J. Biol. Chem., 264, 3869-3876.
20. Gebler, J., Gilkes, N.R., Claeyssens, M., Wilson, D.B., Beguin, P., Wakarchuk, W.W., Kilburn, D.G., Miller, R.C., Jr., Warren, R.A.J. and Withers, S.J. (1992) Stereoselective hydrolysis catalyzed by related β1,4-glucanases and β1,4-xylanases. J. Biol. Chem., 267, 12559-12561.
21. Haeuw, J., Strecker, G. Wieruszeski, J. Montreuil, J. and Michalski, J. (1991) Substrate specificity of rat liver cytosolic α-D-mannosidase. Novel degradative pathway for oligomannosidic type glycans. Eur. J. Biochem., 202, 1257-68.
22. Hamagashira, N., Oku, H., Mega, T. and Hase, S. (1996) Purification and characterization of hen oviduct α1,2-mannosidase. J. Biochem., 119, 998-1003.
23. Hase, S. (1994) High-performance liquid chromatography of pyridylaminated saccharides. Methods Enzymol., 230, 225-237.
24. Hase, S., Kikuchi, N., Ikenaka, T. and Inoue, K. (1985) Structures of sugar chains of the third component of human complement. J. Biochem., 98, 863-874.
25. Herscovics, A. (1998) Glycosidases of the asparagine-linked oligosaccharide processing pathway. In Pinto, B.M. (ed.), Comprehensive Natural Products Chemistry. Elsevier, Amsterdam, in press.
26. Herscovics, A., Schneikert, J., Athanassiadis, A. and Moremen, K.W. (1994) Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. J. Biol. Chem., 269, 9864-9871.
27. Jelinek Kelly, S. and Herscovics, A. (1988) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from Man9G1cNAc. J. Biol. Chem., 263, 14757-14763.
28. Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664.
29. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
30. Lal, A., Schutzbach, J.S., Forsee, W.T., Neame, P.J. and Moremen, K.W. (1994) Isolation and expression of murine and rabbit cDNAs encoding an α1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides. J. Biol. Chem., 269, 9872-9881.
31. 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.
32. Li, E. and Kornfeld, S. (1979) Structural studies of the major high mannose oligosaccharide units from Chinese hamster ovary cell glycoproteins. J. Biol. Chem., 254, 1600-1605.
33. Liao, Y.-F., Lal, A. and Moremen, K.W. (1996) Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid α-mannosidase. J. Biol. Chem., 271, 28348-28358.
34. Lipari, F. and Herscovics, A. (1994) Production, purification and characterization of recombinant yeast processing α1,2-mannosidase. Glycobiology, 4, 697-702.
35. Lipari, F., Gour Salin, B.J. and Herscovics, A. (1995) The Saccharomyces cerevisiae processing α1,2-mannosidase is an inverting glycosidase. Biochem. Biophys. Res. Commun., 209, 322-326.
36. Lis, H., Sharon, N. and Katchalski, E. (1966) Soybean hemagglutinin, a plant glycoprotein I. Isolation of a glycopeptide. J. Biol. Chem., 241, 684-689.
37. Lubas, W.A. and Spiro, R.G. (1987) Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem., 262, 3775-3781.
38. Lubas, W.A. and Spiro, R.G. (1988) Evaluation of the role of rat liver Golgi endo-α-d-mannosidase in processing N-linked oligosaccharides. J. Biol. Chem., 263, 3990-3998.
39. Merkle, R.K., Zhang, Y., Ruest, P.J., Lal, A., Liao, Y.-F. and Moremen, K.W. (1997) Cloning, expression, purification and characterization of the murine lysosomal acid α-mannosidase. Biochim. Biophvs. Acta, 1336, 132-146.
40. Moremen, K.W., Touster, O. and Robbins, P.W. (1991) Novel purification of the catalytic domain of Golgi α-mannosidase II. Characterization and comparison with the intact enzyme. J. Biol. Chem., 266, 16876-16885.
41. Moremen, K.W., Trimble, R.B. and Herscovics, A. (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology, 4, 113-125.
42. Nilsson, T. and Warren, G. (1994) Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol., 6, 517-21.
43. Rizzolo, L.J. and Kornfeld, R. (1988) Post-translational protein modification in the endoplasmic retculum: demonstration of fatty acylase and deoxymannojirimycin-sensitive α-mannosidase activities. J. Biol. Chem., 263, 9520-9525.
44. Scaman, C.H., Lipari, F. and Herscovics, A. (1996) A spectrophotometric assay for α-mannosidase activity. Glycobiology, 6, 265-270.
45. Schneikert, J. and Herscovics, A. (1994) Characterization of a novel mouse recombinant processing α-mannosidase. Glycobiology, 4, 445-450.
46. Schweden, J. and Bause, E. (1989) Characterization of trimming Man9-mannosidase from pig liver. Purification of a catalytically active fragment and evidence for the transmembrane nature of the intact 65 kDa enzyme. Biochem. J., 264, 347-355.
47. Schweden, J., Legler, G. and Bause, E. (1986) Purification and characterization of a neutral processing mannosidase from calf liver acting on (Man)9(GlcNAc)2 oligosaccharides. Eur. J. Biochem., 157, 563-570.
48. Swanson, M.A. (1955) Glucose-6-phosphatase from liver. Methods Enzymol., 2, 541-543.
49. Tabas, I. and Kornfeld, S. (1979) Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem., 254, 11655-11663.
50. Tremblay, L.O., Cambell Dyke, N. and Herscovics, A. (1998) Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human α1,2-mannosidase gene involved in N-glycan maturation. Glycobiology, 8, 585-595.
51. Tulsiani, D.R. and Touster, O. (1988) The purification and characterization of mannosidase IA from rat liver Golgi membranes. J. Biol. Chem., 263, 5408-5417.
52. Tulsiani, D.R.P., Hubbard, S.C., Robbins, P.W. and Touster, O. (1982) α-D-mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAc-Man5-cleaving enzyme in glycoprotein biosynthesis and Mannosidase IA and IB are the enzymes converting Man9 precursors to Man5 intermediates. J. Biol. Chem., 257, 3660-3668.
53. Velasco, A., Hendricks, L., Moremen, K.W., Tulsiani, D.R., Touster, O. and Farquhar, M.G. (1993) Cell type-dependent variations in the subcellular distribution of α-mannosidase I and II. J. Cell Biol., 122, 39-51.
54. Verostek, M., Atkinson, P. and Trimble, R. (1993) Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. I. Role of glucose in the initial glycosylation of invertase in the endoplasmic reticulum. J. Biol. Chem., 268, 12095-12103.
55. Weng, S. and Spiro, R.G. (1993) Demonstration that a kifunensine-resistant α-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. J. Biol. Chem., 268, 25656-25663.
56. Weng, S. and Spiro, R.G. (1996a) Endoplasmic reticulum kifunensine-resistant α-mannosidase is enzymatically and immunologically related to the cytosolic α-mannosidase. Arch. Biochem. Biophys., 325, 113-123.
57. Weng, S. and Spiro, R.G. (1996b) Evaluation of the early processing routes of N-linked oligosaccharides of glycoproteins through the characterization of Man8GlcNAc2 isomers: evidence that endomannosidase functions in vivo in the absence of a glucosidase blockade. Glycobiology, 6, 861-868.