Purification, characterization, and localization of an ADP-ribosylactin hydrolase that uses ADP-ribosylated actin from rat brains as a substrate

Journal of Biological Chemistry

Volumn 272, Issue 44, 1997, Pages 28116-28125

  Okamoto, Hideaki ^a   Fujita, Hiromi ^a   Matsuyama, Satoshi ^a   Tsuyama, Shingo ^a  

^a Osaka Prefecture University   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE TRIPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

ACTIN POLYMERIZATION; ADENOSINE DIPHOSPHATE RIBOSYLATION; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BRAIN NERVE CELL; BRAIN SYNAPTOSOME; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; SIGNAL TRANSDUCTION;

ACTINS; ADENOSINE DIPHOSPHATE RIBOSE; ANIMALS; ANTIBODIES, MONOCLONAL; BRAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, ION EXCHANGE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSIDE HYDROLASES; IMMUNOHISTOCHEMISTRY; MALE; N-GLYCOSYL HYDROLASES; RATS; RATS, WISTAR; SUBCELLULAR FRACTIONS; SUBSTRATE SPECIFICITY;

ANIMALIA; BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 0030788808     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.44.28116     Document Type: Article

References (46)

1. Cassel, D., and Pfeuffer, T. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 2669-2673
2. Katada, T., and Ui, M. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 3129-3133
3. Honjo, T., Nishizuka, Y., and Hayaishi, O., (1968) J. Biol. Chem. 243, 3553-3555
4. Aktories, K., Barmann, M., Ohishi, I., Tsuyama, S., Jakobs, K. H., and Habermann, E. (1986) Nature 322, 390-392
5. Singer, S. J., and Kupfer, A. (1986) Annu. Rev. Cell Biol. 2, 337-365
6. Burgoyne, R. D., and Cheek, T. R. (1987) Biosci. Rep. 7, 281-288
7. De Camilli, P., Benfenai, F., Valtorta, F., and Greengard, P. (1990) Annu. Rev. Cell Biol. 6, 433-460
8. Vandekerckhove, J., Schering, B., Barmann, M., and Aktories, K. (1988) J. Biol. Chem. 263, 696-700
9. Matter, K., Dreyer, F., and Aktories, K. (1989) J. Neurochem. 52, 370-376
10. Moss, J., Stanley, S. J., and Watkins, P. A. (1980) J. Biol. Chem. 255, 5838-5840.
11. Tanigawa, Y., Tsuchiya, M., Imai, Y., and Shimoyama, M. (1984) J. Biol. Chem. 259, 2022-2029
12. Tanuma, S., Kawashima, K., and Endo, H. (1988) J. Biol. Chem. 263, 5485-5489
13. Paterson, J. E., Larew, J. S.-A., and Graves, D. J. (1990) J. Biol. Chem. 265, 17062-17069
14. Quist, E. E., Coyle, D. L., Vasan, R., Satumtira, N., Jacobson, E. L., and Jacobson, M. K. (1994) J. Mol. Cell. Cardiol. 26, 251-260
15. Zolkiewska, A., Nightingale, M. S., and Moss, J. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11352-11356
16. Matsuyama, S., and Tsuyama, S. (1991) J. Neurochem. 57, 1380-1387
17. Fujita, H., Okamoto, H., and Tsuyama, S. (1995) Int. J. Biochem. Cell Biol. 27, 1065-1078
18. Moss, J., Oppenheimer, N. J., West, R. E., Jr., and Stanley, S. J. (1986) Biochemistry 25, 5408-5414
19. Moss, J., Stanley, S. J., Nightingale, M. S., Murtagh, J. J., Jr., Monaco, L., Mishima, K., Chen, H.-C., Williamson, K. C., and Tsai, S.-C. (1992) J. Biol. Chem. 267, 10481-10488
20. Takada, T., Iida, K., and Moss, J. (1993) J. Biol. Chem. 268, 17837-17843
21. Lelkes, P. I., Friedman, J. E., Rosenheck, K., and Oplatka, A. (1986) FEBS Lett. 208, 357-363
22. Ohishi, I., and Tsuyama, S. (1986) Biochem. Biophys. Res. Commun. 136, 802-806
23. Just, I., Wollenberg, P., Moss, J., and Aktories, K. (1994) Eur. J. Biochem. 221, 1047-1054
24. Lee, H., and Iglewski, W. J. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 2703-2707
25. Huang, K.-P., and Robinson, J. C. (1976) Anal. Biochem, 72, 593-599
26. Kim, H., Jacobson, E. L., and Jacobson, M. K. (1993) Science 261, 1330-1333
27. Titanji, V. P. K. (1977) Biochim. Biophys. Acta 481, 140-151
28. Goding, J. W. (1986) Monoclonal Antibodies: Principles and Practice, 2nd Ed., Academic Press Ltd., London
29. Bolton, A. E., and Hunter, W. M. (1973) Biochem. J. 133, 529-538
30. Ueda, T., Greengard, P., Berzins, K., Cohen, R. S., Blomberg, F., Grab, D. J., and Siekevitz, P. (1979) J. Cell Biol. 83, 308-319
31. Earl, D. C. N., and Korner, A. (1965) Biochem. J. 94, 721-734
32. Sottocasa, G. L., Kuylenstierna, B., Ernster, L., and Bergstrand, A. (1967) J. Cell Biol. 32, 415-438
33. Wood, T. (1964) Biochem. J. 91, 453-460
34. Weir, J. P., and Frederiksen, D. W. (1982) Methods Enzymol. 85, 371-373
35. Sternweis, P. C., and Robishaw, J. D. (1984) J. Biol. Chem. 259, 13806-13813
36. Kobayashi, I., Shibasaki, H., Takahashi, K., Tohyama, K., Kurachi, Y., Itoh, H., Ui, M., and Katada, T. (1990) Eur. J. Biochem. 191, 499-506
37. Sayhan, O., Ozdemirli, M., Nurten, R., and Bermek, E. (1986) Biochem. Biophys. Res. Commun. 139, 1210-1214
38. Pollard, T. D., and Cooper, J. A. (1982) Methods Enzymol. 85, 211-233
39. Laemmli, U. K. (1970) Nature 227, 680-685
40. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
41. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
42. Moss, J., Jacobson, M. K., and Stanley, S. J. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 5603-5607
43. Obara, S., Mishima, K., Yamada, K., Taniguchi, M., and Shimoyama, M. (1989) Biochem. Biophys. Res. Commun. 163, 452-457
44. Wegner, A., and Aktories, K. (1988) J. Biol. Chem. 263, 13739-13742
45. Geipel, U., Just, I., Schering, B., Haas, D., and Aktories, K. (1989) Eur. J. Biochem. 179, 229-232
46. Hirokawa, N., Sobue, K., Kanda, K., Harada, A., and Yonfuji, H. (1989) J. Cell Biol. 108, 111-126