Decavanadate inhibits the cell-free activation of neutrophil NADPH oxidase without affecting tyrosine phosphorylation

Biological and Pharmaceutical Bulletin

Volumn 22, Issue 8, 1999, Pages 799-804

  Okamura, Naoki ^a   Sakai, Tomoko ^a   Nishimura, Yuko ^a   Sakai, Makiko ^a   Araki, Shiho ^a   Yamaguchi, Masafumi ^a   Ishibashi, Sadahiko ^a  

^a HIROSHIMA UNIV SCHOOL OF MEDICINE   (Japan)

Author keywords

Cell free activation; Decavanadate; Guinea pig neutrophil; NADPH oxidase; Superoxide anion; Tyrosine phosphorylation

Indexed keywords

ARACHIDONIC ACID; PERVANADATE; POLYANION; PROTEIN TYROSINE PHOSPHATASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; VANADIC ACID;

ANIMAL CELL; ARTICLE; CELL FREE SYSTEM; CELL MEMBRANE; CELL PH; CONTROLLED STUDY; CYTOSOL; ENZYME INHIBITION; FEMALE; GUINEA PIG; NEUTROPHIL; NONHUMAN; PROTEIN PHOSPHORYLATION;

EID: 0032881184     PISSN: 09186158     EISSN: None     Source Type: Journal    
DOI: 10.1248/bpb.22.799     Document Type: Article

References (24)

1. Babior B. M., Am. J. Hematol., 37, 263-266 (1991).
2. Smith R. M., Curnutte J. T., Blood, 77, 673-686 (1991).
3. Grisham M. B., Granger D. N., Dig. Dis. Sci., 33, 6S-15S (1988).
4. Segal A. W., Abo A., Trends. Biochem. Sci., 18, 43-47 (1993).
5. Cox J. A., Jeng A. Y., Blumberg P. M., Tauber A. I., J. Immunol., 138, 1884-1888 (1987).
6. Tamura S., Brown T. A., Whipple J. H., Fujita-Yamaguchi Y., Dubler R. E., Cheng K., Larner J., J. Biol. Chem., 259, 6650-6658 (1984).
7. Salvo J. D., Pfitzer G., Semenchuk L. A., Can. J. Physiol. Pharmacol., 72, 1434-1439 (1994).
8. Trudel S., Downey G. P., Grinstein S., Pâquet M. R., Biochem. J., 269, 127-131 (1990).
9. Trudel S., Pâquet M. R., Grinstein S., Biochem. J., 276, 611-619 (1991).
10. Yamaguchi M., Oishi H., Araki S., Saeki S., Yamane H., Okamura N., Ishibashi S., Arch. Biochem. Biophys., 323, 382-386 (1995).
11. Yamaguchi M., Saeki S., Yamane H., Okamura N., Ishibashi S., Biochem. Biophys. Res. Commun., 216, 203-208 (1996).
12. Sbarra A. J., Karnovsky M. L., J. Biol. Chem., 234, 1355-1362 (1959).
13. Borregaard N., Tauber A. I., J. Biol. Chem., 259, 47-52 (1984).
14. Laemmli U. K., Nature (London), 227, 680-685 (1970).
15. Harlow E., Lane D., ̂Antibodies: A Laboratory Manual,̂ Cold Spring Harbor Laboratory, New York, 1988.
16. Park J.-W., Babior B. M., J. Biol. Chem., 267, 19901-19906 (1992).
17. Goddard J. B. and Gonas A. M., Inorg. Chem., 12, 574-579 (1973).
18. Boyd D. W., Kustin K., Adv. Inorg. Biochem., 6, 311-362 (1984).
19. Grinstein S., Furuya W., Lu D. J., Mills G. B., J. Biol. Chem. 265, 318-327 (1990).
20. Liochev S. I., Fridovich I., Arch. Biochem. Biophys., 279, 1-7 (1990).
21. Goldman R., Ferber E., Meller R., Zor U., Biochim. Biophys. Acta, 1222, 265-276 (1994).
22. Boyd D. W., Kenneth K., Niwa M., Biochim. Biophys. Acta, 827, 472-475 (1985).
23. Coan C., Scales D. J., Murphy A. J., J. Biol. Chem., 261, 10394-10403 (1986).
24. Le Hir M., Biochem. J., 273, 795-798 (1991).