Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi

Journal of Biological Chemistry

Volumn 271, Issue 19, 1996, Pages 11588-11594

  Spiro, Robert G ^a   Zhu, Qin ^a   Bhoyroo, Vishnu ^a   Söling, Hans Dieter ^b  

^a JOSLIN DIABETES CENTER   (United States)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CALRETICULIN; CHAPERONE; GLYCOPEPTIDE; LECTIN; LIVER ENZYME; MANNOSIDASE; OLIGOSACCHARIDE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; GOLGI COMPLEX; LIVER MEMBRANE; MALE; NONHUMAN; PEPTIDE ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; RAT; ROUGH ENDOPLASMIC RETICULUM;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM-BINDING PROTEINS; CALRETICULIN; CARBOHYDRATE SEQUENCE; CELL LINE; CHROMATOGRAPHY, AFFINITY; ENDOPLASMIC RETICULUM, ROUGH; GOLGI APPARATUS; HUMANS; LECTINS; LIVER; MALE; MANNOSIDASES; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PROTEIN FOLDING; RATS; RATS, INBRED STRAINS; RIBONUCLEOPROTEINS; SUBSTRATE SPECIFICITY;

EID: 15844386822     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.19.11588     Document Type: Article

References (51)

1. Helenius, A. (1994) Mol. Cell. Biol. 5, 253-265
2. Ou, W.-J , Cameron, P H , Thomas, D. Y , and Bergeron, J. J M. (1993) Nature 364, 771-776
3. Fiedler, K., and Simons, K. (1995) Cell 81, 309-312
4. Moore, S. E. H., and Spiro, R G (1993) J. Biol Chem. 268, 3809-3812
5. Kearse, K. P., Williams, D B., and Singer, A. (1994) EMBO J. 13, 3678-3686
6. Lodish, H F., and Kong, N. (1984) J Cell Biol. 98, 1720-1729
7. Sasak, V. W., Ordovas, J. M., Elbein, A. D., and Berninger, R. W. (1985) Biochem J. 232, 759-766
8. Rabouille, C., and Spiro, R. G (1992) J. Biol. Chem. 267, 11573-11578
9. Hebert, D. N., Foellmer, B., and Helenius, A. (1995) Cell 81, 425-433
10. Ware, F. E., Vassilakos, A., Peterson, P. A., Jackson, M. R., Lehrman, M. A., and Williams, D. B (1995) J. Biol. Chem. 270, 4697-4704
11. Peterson, J. R., Ora, A., Van, P. N., and Helenius, A. (1995) Mol. Biol Cell 6, 1173-1184
12. Hiraizumi, S., Spohr, U., and Spiro, R. G. (1994) J. Biol. Chem. 269, 4697-4700
13. Lubas, W. A., and Spiro, R. G. (1987) J. Biol. Chem. 262, 3775-3781
14. Lubas, W. A., and Spins, R. G. (1988) J. Biol. Chem. 263, 3990-3998
15. Leelavathi, D. E., Estes, L. W., Feingold, D. S., and Lombardi, B. (1970) Biochim. Biophys. Acta 211, 124-138
16. Tulsiani, D. R. P., Opheim, D. J., and Touster, O., (1977) J. Biol. Chem. 252, 3227-3233
17. Depierre, J., and Dallner, G. (1976) in Biochemical Analysis of Membranes (Maddy, A. H., ed) pp. 79-131. John Wiley & Sons, New York
18. Van, P. N., Peter, F., and Soling, H. D. (1989) J. Biol. Chem. 264, 17494-17501
19. Moos, M., Jr., Nguyen, N. Y., and Liu, T.-Y. (1988) J. Biol. Chem. 263, 6005-6008
20. Lane, W S., Galat, A., Harding, M. W., and Schreiber, S. L. (1991) J. Protein Chem 10, 151-160
21. Laemmli, U. K. (1970) Nature 227, 680-685
22. Towbin, H., Staehelin, T., and Gordon, T. (1979) Proc. Natl. Acad. Sci. U S. A. 76, 4350-4354
23. Mohan, P. S., and Spiro, R. G. (1986) J. Biol. Chem. 261, 4328-4336
24. Spiro, M. J., Spiro, R. G., and Bhoyroo, V. D. (1976) J. Biol. Chem. 251, 6400-6408
25. Weng, S., and Spiro, R. G. (1996) Arch. Biochem. Biophys. 325, 113-123
26. Weng, S., and Spiro, R. G. (1993) J. Biol. Chem. 268, 25656-25663
27. Moore, S. E. H., and Spiro, R. G. (1994) J. Biol. Chem. 269, 12715-12721
28. Spiro, R. G., Spiro, M. J., and Bhoyroo, V. D. (1983) J. Biol. Chem. 258, 9469-9476
29. Anumula, K. R., and Spiro, R. G. (1983) J. Biol. Chem. 258, 15274-15282
30. Peterson, G. L. (1977) Anal. Biochem. 83, 346-356
31. Spiro, M. J., and Spiro, R. G. (1985) J. Biol. Chem. 260, 5808-5815
32. Michalak, M., Milner, R. E., Burns, K., and Opas, M. (1992) Biochem. J. 285, 681-692
33. Godelaine, D., Spiro, M. J., and Spiro, R. G. (1981) J Biol. Chem. 256, 10161-10168
34. Goldstein, I. J., and Poretz, R. D. (1986) in The Lectins (Liener, I. E., Sharon, N., and Goldstein, I. J., eds) pp. 33-247, Academic Press, New York
35. Moore, S. E. H., and Spiro, R. G. (1990) J. Biol. Chem. 265, 13104-13112
36. Nauseef, W. M., McCormick, S. J., and Clark, R. A. (1995) J. Biol. Chem 270, 4741-4747
37. Wada, I., Imai, S., Kai, M., Sakane, F., and Kanoh, H. (1995) J. Biol. Chem. 270, 20298-20304
38. Grinna, L. S., and Robbins, P. W. (1980) J. Biol. Chem. 255, 2255-2258
39. White, T. K., Zhu, Q., and Tanzer, M. L. (1995) J. Biol Chem. 270, 15926-15929
40. Wiest, D. L., Burgess, W. H., McKean, D., Kearse, K. P., and Singer, A. (1995) EMBO J. 14, 3425-3433
41. Nakamura, M., Moriya, M., Baba, T., Michikawa, Y., Yamanobe, T., Arai, K., Okinaga, S., and Kobayashi, T. (1993) Exp. Cell Res. 205, 101-110
42. Dupuis, M., Schaerer, E., Krause, K. H., and Tschopp, J. (1993) J. Exp. Med. 177, 1-7
43. Burns, K., Atkinson, E. A., Bleackley, R. C., and Michalak, M. (1994) Trends Cell Biol. 4, 152-154
44. Peter, F., Van, P. N., and Soling, H. D. (1992) J. Biol. Chem. 267, 10631-10637
45. Bergeron, J. J. M., Brenner, M. B., Thomas, D. Y., and Williams, D. B. (1994) Trends Biochem. Sci. 19, 124-128
46. Strous, G. J., Van Kerkhof, P., Brok, R., Roth, J., and Brada, D. (1987) J. Biol Chem. 262, 3620-3625
47. Huovila, A. P. J., Eder, A. M., and Fuller, S. D. (1992) J. Cell Biol 118, 1305-1320
48. Musil, L. S., and Goodenough, D. A. (1993) Cell 74, 1065-1077
49. Turco, S J., Stetson, B., and Robbins, P. W. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 4411-4414
50. Spiro, M. J., Spiro, R. G , and Bhoyroo, V. D. (1979) J. Biol. Chem. 254, 7668-7674
51. Zhang, Q., Tector, M., and Salter, R. D. (1995) J Biol Chem 270, 3944-3948