S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: Evidence against a role for glutathione disulfide

Archives of Biochemistry and Biophysics

Volumn 310, Issue 1, 1994, Pages 273-281

  Chai, Yuh Cherng ^a   Ashraf, Syed S ^a   Rokutan, Kazuhito ^b   Johnston, Richard B ^c   Thomas, James A ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF TOKUSHIMA   (Japan)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GLUTATHIONE DISULFIDE; THIOL GROUP;

ARTICLE; HUMAN; HUMAN CELL; NEUTROPHIL; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN THIOLATION; RESPIRATORY BURST;

ACTINS; DISULFIDES; GLUTATHIONE; GLUTATHIONE DISULFIDE; HUMAN; NEUTROPHILS; PROTEINS; RESPIRATORY BURST; SULFHYDRYL COMPOUNDS; SULFUR RADIOISOTOPES; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TETRADECANOYLPHORBOL ACETATE;

EID: 0028298361     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1006/abbi.1994.1167     Document Type: Article

References (45)

1. Collison, M. W., Beidler, D., Grimm, L. M., and Thomas, J. A. (1986) Biochim. Biophys. Acta 885, 58-67.
2. Collison, M. W., and Thomas, J. A. (1987) Biochim. Biophys. Acta 928, 121-129.
3. Rokutan, K., Thomas, J. A., and Sies, H. (1989) Eur. J. Biochem. 179, 233-239.
4. Thomas, J. A., Park, E.-M., Chai, Y.-C., Brooks, R., Rokutan, K., and Johnston, R. B., Jr. (1991) in Biological Reactive Intermediates. IV. Molecular and Cellular Effects, and Human Impact (Snyder R and Sipes G Eds), Adv. Exptl. Med. Biol. 283, 95-104, Plenum, New York.
5. Rokutan, K., Thomas, J. A., and Johnston, R. B., Jr. (1991) J. Im-munol. 147, 260-264.
6. Chai, Y.-C., Jung, C.-H., Lii, C.-K., Ashraf, S. S., Hendrich, S., Wolf, B., Sies, H., and Thomas, J. A. (1991) Arch. Biochem. Biophys. 384, 270-278.
7. Thomas, J. A., and Sies, H. (1992) in The Post-Translational Mod-ification of Proteins (Tuboi S Taniguchi N and Katunuma N Eds), pp. 35-51. CRC Press, Boca Raton, FL.
8. Gilbert, H. F. (1982) J. Biol. Chem. 257, 12086-12091.
9. Morel, F., Doussiere, J., and Vignais, P. V. (1991) Eur. J. Biochem. 201, 523-542.
10. Volpp, B. D., Nauseef, W. M., and Clark, R. A. (1988) Science 242, 1295-1297.
11. Ohno, Y., and Gallin, J. I. (1985) J. Biol. Chem. 260, 8438-8446.
12. Voetman, A. A., Loos, J. A., and Roos, D. (1980) Blood 55, 741-747.
13. Bilzer, M., and Lauterberg, B. H. (1991) Eur. J. Clin. Invest. 21, 316-322.
14. Burchill, B. R., Oliver, J. M., Pearson, C. B., Leinbach, E. D., and Berlin, D. (1978) J. Cell Biol. 76, 439-447.
15. Guthrie, L. A., McPhail, L. C., Henson, P. M., and Johnston, R. B., Jr. (1984) J. Exp. Med. 160, 1656-1671.
16. Fariss, M. W., and Reed, D. J. (1987) Methods Enzymol. 143, 101-109.
17. Grimm, L. M., Collison, M. W., Fisher, R. A., and Thomas, J. A. (1985) Biochim. Biophys. Acta 844, 50-54.
18. Laemmli, U. K. (1970) Nature 227, 680-685.
19. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol Chem. 193, 265-275.
20. Ozols, J. (1990) Methods Enzymol. 182, 587-601.
21. Johnston, R. B., Jr., and Lehmeyer, L. E. (1976) J. Clin. Invest. 57, 836-841.
22. Al-Mohanna, F. A., and Hallet, M. B. (1990) Biochem. Biophys. Res. Commun. 169, 1222-1228.
23. Lazarides, L., and Lindberg, U. (1974) Proc. Nat. Acad. Sci. USA 71, 4742-4752.
24. Cleveland, D. W., Fischer, S. G., Kirschner, M. W., and Laemmli, U. K. (1977) J. Biol Chem. 252, 1102-1106.
25. Brigelius, R., Muckel, C., Ackerboom, T. P. M., and Sies, H. (1983) Biochem. Pharmacol. 32, 2529-2534.
26. Bellomo, G., Mirabelli, F., Dimonte, D., Richelmi, P., Thor, H., Orrenius, C., and Orrenius, S. (1987) Biochem. Pharmacol 36, 1313-1320.
27. Brodie, A. E., and Reed, D. J. (1987) Biochem. Biophys. Res. Commun. 148, 120-125.
28. Tsukahara, T., Kominami, E., and Katunuma, N. (1987) J. Biochem. 101, 1447-1456.
29. Gilbert, H. (1990) Adv. Enzymol. 63, 69-173.
30. Mannervik, B., and Axelsson, K. (1980) Biochem. J. 190, 125-130.
31. Wells, W. W. (1993) Adv. Enzymol. 66, 149-201.
32. Freedman, R. B. (1989) Cell 57, 1069-1072.
33. Noiva, R., and Lennarz, W. J. (1992) J. Biol. Chem. 267, 3553-3556.
34. Park, E.-M., and Thomas, J. A. (1989) Arch. Biochem. Biophys. 274, 47-54.
35. Meiyal, J. J., Starke, D. W., Gravina, S. A., Dothey, C., and Chung, J. S. (1991) Biochemistry 30, 6088-6097.
36. Terada, T., Oshida, T., Nishimura, M., Maeda, H., Hara, T., Hosomi, S., Miyoguchi, T., and Nishihura, T. (1992) J. Biochem. 3, 688-692.
37. Miller, R. M., Park, E.-M., and Thomas, J. A. (1991) Arch. Biochem. Biophys. 287, 112-120.
38. Park, E.-M., and Thomas, J. A. (1988) Biochim. Biophys. Acta 964, 151-160.
39. Tamba, J., Simone, G., and Quintiliani, M. (1986) Inti. J. Radiation Biol. 50, 595-600.
40. Ross, D. (1988) Pharm. Ther. 37, 231-249.
41. Chai, Y.-C., Hendrich, S., and Thomas, J. A. (1994) Arch. Biochem. Biophys. 310, 264-272.
42. Maples, K. R., Kennedy, C. H., Jordan, S. J., and Mason, R. P. (1990) Arch. Biochem. Biophys. 277, 402-409.
43. Lii, C.-K., Chai, Y.-C., Zhao, W., Thomas, J. A., and Hendrich, S. (1994) Arch. Biochem. Biophys. 308, 231-239.
44. Sha’afi, R. I., White, J. R., Molski, T. F. P., Shefcyk, J., Naccache, P. H., Volpi, M., and Feinstein, M. B. (1983) Biochem. Biophys. Res. Commun. 114, 635-645.
45. Cooper, J. A. (1987) J. Cell Biol. 105, 1473-1478.