Native and multimeric vitronectin exhibit similar affinity for heparin: Differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form

Journal of Biological Chemistry

Volumn 272, Issue 11, 1997, Pages 6858-6867

  Zhuang, Ping ^a   Chen, Anthony I ^a   Peterson, Cynthia B ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEPARIN; VITRONECTIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; FLUORESCENCE; IONIC STRENGTH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANIMALS; BINDING SITES; CHROMATOGRAPHY, AFFINITY; HEPARIN; HUMANS; PROTEIN BINDING; PROTEIN DENATURATION; THERMODYNAMICS; VITRONECTIN;

EID: 0030900930     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.11.6858     Document Type: Article

References (52)

1. Preissner, K. T. (1989) Blut 59, 419-431
2. Preissner, K. T., and Jenne, D. (1991) Thromb. Haemostasis 66, 123-132
3. Preissner, K. T. (1991) Annu. Rev. Cell. Biol. 7, 275-310
4. Tomasini, B. R., and Mosher, D. F. (1991) Prag. Hemost. Thromb. 10, 269-305
5. Preissner, K. T., and Jenne, D. (1991) Thromb. Haemostasis 66, 189-194
6. Pollanen, J., Stephens, R. W., and Vaheri, A. (1991) Adv. Cancer Res. 57, 273-328
7. Silnutzer, J., and Barnes, D. W. (1984) Biochem. Biophys. Res. Commun. 118, 339-343
8. Barnes, D. W., and Silnutzer, J. (1983) J. Biol. Chem. 258, 12548-12552
9. Barnes, D. W., Reing, J. E., and Amos, B. (1985) J. Biol. Chem. 260, 9117-9122
10. Preissner, K. T., Wassmuth, R., and Muller-Berghaus, G. (1985) Biochem. J. 231, 349-355
11. Hayashi, M., Akama, T., Kono, I., and Kashiwagi, H. (1985) J. Biochem. (Tokyo) 98, 1135-1138
12. Suzuki, S., Pierschbacher, M. D., Hayman, E. G., Nguyen, K., Ohgren, Y., and Ruoslahti, E. (1984) J. Biol. Chem. 258, 15307-15314
13. Akama, T., Yamade, K. M., Seno, N., Marsumoto, I., Kono, I., Kashiwagi, H., Funaki, T., and Hayashi, M. (1986) J. Biochem. (Tokyo) 100, 1343-1351
14. Lane, D. A., Flynn, A. M., Pejler, G., Lindahl, U., Choay, J., and Preissner, K. (1987) J. Biol. Chem. 262, 16343-16348
15. Preissner, K. T., and Muller-Berghaus, G. (1986) Eur. J. Biochem. 156, 645-650
16. Preissner, K. T., and Muller-Berghaus, G. (1987) J. Biol. Chem. 262, 12247-12253
17. Yatohgo, T., Izumi, M., Kashiwagi, H., and Hayashi, M. (1988) Cell Struct. Funct. 13, 281-292
18. Liang, O. D., Flock, J. I., and Wadstrom, T. (1994) J. Biochem. (Tokyo) 116, 457-463
19. deBoer, H. C., Preissner, K. T., Bouma, B. N., and de Groot, P. G. (1992) J. Biol. Chem. 267, 2264-2268
20. Hogasen, K., Mollnes, T. E., and Harboe, M. (1992) J. Biol. Chem. 267, 23076-23082
21. Wisniowski, P., and Martin, W. J. N. (1995) J. Lab. Clin. Med. 125, 38-45
22. Sheehan, M., Morris, C. A., Pussell, B. A., and Charlesworth, J. A. (1995) Clin. Exp. Immunol. 101, 136-141
23. Chain, D., Korc-Grodzicki, B., Kreizman, T., and Shaltiel, S. (1991) Biochem. J. 274, 387-394
24. Tomasini, B. R., Owen, M. C., Fenton, J. W., II, and Mosher, D. F. (1989) Biochemistry 28, 7617-7623
25. Ishikawa, M., and Hayashi, M. (1992) Biochim. Biophys. Acta 1121, 173-177
26. Naski, M. C., Lawrence, D. A., Mosher, D. F., Podor, T. J., and Ginsburg, D. (1993) J. Biol. Chem. 268, 12367-12372
27. Panetti, T. S., and McKeown-Longo, P. J. (1993) J. Biol. Chem. 268, 11988-11993
28. Bittorf, S. V., Williams, E. C., and Mosher, D. F. (1993) J. Biol. Chem. 268, 24838-24846
29. Stockmann, A., Hess, S., Declerck, P., Timpl, R., and Preissner, K. T. (1993) J. Biol. Chem. 268, 22874-22882
30. Seiffert, D. (1995) FEBS Lett. 368, 155-159
31. Zhuang, P., Li, H., Williams, J. G., Wagner, N., Seiffert, D., and Peterson, C. B. (1996) J. Biol. Chem. 271, 14333-14343
32. Zhuang, P., Blackburn, M. N., and Peterson, C. B. (1996) J. Biol. Chem. 271, 14323-14332
33. Preissner, K. T., and Sie, P. (1988) Thromb. Haemostasia 60, 399-406
34. Dahlback, B., and Podack, E. R. (1985) Biochemistry 24, 2368-2374
35. Nesheim, M., Blackburn, M. N., Lawler, C. M., and Mann, K. G. (1986) J. Biol. Chem. 261, 3214-3221
36. Jaques, L. B. (1977) Methods Biochem. Anal. 24, 203-212
37. Lasker, S. E., and Stivala, S. S. (1966) Arch. Biochem. Biophys. 115, 360-372
38. Peterson, C. B., Morgan, W. T., and Blackburn, M. N. (1987) J. Biol. Chem. 262, 7567-7574
39. Bock, P. E., and Shore, J. D. (1983) J. Biol. Chem. 258, 15079-15086
40. Bock, P. E., Shore, J. D., Tans, G., and Griffin, J. H. (1985) J. Biol. Chem. 260, 12434-12443
41. Johnson, C. R., Morin, P. E., Arrowsmith, C. H., and Freire, E. (1995) Biochemistry 34, 5309-5316
42. Evington, J. R., Feldman, P. A., Luscombe, M., and Holbrook, J. J. (1986) Biochim. Biophys. Acta 871, 85-92
43. Piepkorn, M. W., Lagunoff, D., and Schmer, G. (1980) Arch. Biochem. Biophys. 205, 315-322
44. Piepkorn, M. W. (1981) Biochem. J. 196, 649-651
45. Ingham, K. C., Brew, S. A., and Atha, D. H. (1990) Biochem. J. 272, 605-611
46. Ingham, K. C., Brew, S. A., Migliorini, M. M., and Busby, T. F. (1993) Biochemistry 32, 12548-12553
47. Ross, P. D., and Subramanian, S. (1981) Biochemistry 20, 3096-3102
48. Seiffert, D., Geiger, M., Ecke, S., and Binder, B. R. (1992) Thromb. Haemostasis 68, 657-661
49. Rovelli, G., Stone, S. R., Preissner, K. T., and Monard, D. (1990) Eur. J. Biochem. 192, 797-803
50. Tomasini, B. R., and Mosher, D. F. (1988) Blood 72, 903-912
51. Olson, S. T., Halvorson, H. R., and Bjork, I. (1991) J. Biol. Chem. 266, 6342-6352
52. Gibson, A. D., Baburaj, K., Day, D., Verhamme, I., Shore, J. D., and Peterson, C. B. (1997) J. Biol. Chem. 272, 5112-5121