Effect of phosphotyrosine proteins on phorbol myristate acetate-induced NADPH oxidase activation in guinea pig peritoneal polymorphonuclear leukocytes

Biological and Pharmaceutical Bulletin

Volumn 26, Issue 7, 2003, Pages 1009-1012

  Takemasa, Hiroaki ^a   Imagawa, Naoki ^a   Kawakami Honda, Naoko ^a   Nagasawa, Kazuki ^a   Fujimoto, Sadaki ^a  

^a KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Guinea pig; NADPH oxidase; Phosphotyrosine protein; Polymorphonuclear leukocyte; ST638; Tyrosine kinase

Indexed keywords

ALPHA CYANO 3 ETHOXY 4 HYDROXY 5 (PHENYLTHIOMETHYL)CINNAMAMIDE; CYTOCHALASIN B; GENISTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOTYROSINE; PROTEIN P47; PROTEIN TYROSINE KINASE INHIBITOR; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; FREE RADICAL; PROTEIN;

ANIMAL CELL; ARTICLE; CELL LEVEL; CELL MEMBRANE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVATION; FEMALE; GUINEA PIG; IMMUNOHISTOCHEMISTRY; NEUTROPHIL; NONHUMAN; PERITONEUM; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; ANIMAL; DRUG EFFECT; METABOLISM; PERITONEAL CAVITY; PHYSIOLOGY;

ANIMALS; ENZYME ACTIVATION; FEMALE; FREE RADICALS; GUINEA PIGS; NADPH OXIDASE; NEUTROPHILS; PERITONEAL CAVITY; PHOSPHOTYROSINE; PROTEINS; TETRADECANOYLPHORBOL ACETATE;

EID: 1542707451     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.26.1009     Document Type: Article

References (24)

1. Goldstein I. M., Roos D., Kaplan H. B., Weissmann G., J. Clin. Invest., 56, 1155-1163 (1973).
2. Rossi F., Biochim. Biophys. Acta, 853, 65-89 (1986).
3. Chanock S. J., Benna J. E., Smith R. M., Babior B. M., J. Biol. Chem., 269, 24519-24522 (1994).
4. Smith R. M., Curnutte J. T., Blood, 77, 673-686 (1991).
5. Segal A. W., J. Clin. Invest., 83, 1785-1793 (1989).
6. Clark R. A., Volpp B. D., Leidal K. G., Nauseef W. M., J. Clin. Invest., 85, 714-721 (1990).
7. Park J. W., Ma M., Ruedi J. M., Smith R. M., Babior B. M., J. Biol. Chem., 267, 17327-17332 (1992).
8. Park J. W., Babior B. M., J. Biol. Chem., 267, 19901-19906 (1992).
9. Nauseef W. M., Volpp B. D., McCormick S., Leidal K. G., Clark R. A., J. Biol. Chem., 266, 5911-5917 (1991).
10. Benna E. J., Ruedi J. M., Babior B. M., J. Biol. Chem., 269, 6729-6734 (1994).
11. Gomez-Cambronero J., Huang C. K., Bonak V. A., Wang E., Casnellie J. E., Shiraishi T., Sha'afi R. I., Biochem. Biophys. Res. Commun., 162, 1478-1485 (1989).
12. Lloyds D., Brindle N. P., Hallet M. B., Biochem. Soc. Trans., 21, 436S (1993).
13. Conde M., Chiara M. D., Pintado E., Sobrino F., Free Rad. Biol. Med., 18, 343-348 (1995).
14. Kawakami N., Takemasa H., Yamaguchi T., Hayakawa T., Shimohama S., Fujimoto S., Arch. Biochem. Biophys., 349, 89-94 (1998).
15. Kawakami N., Shimohama S., Hayakawa T., Sumida Y., Fujimoto S., Biochim. Biophys. Acta, 1314, 167-174 (1996).
16. Curnutte J. T., Scott P. J., Mayo L. A., Proc. Natl. Acad. Sci. U.S.A., 86, 825-829 (1989).
17. Kawakami N., Takemasa H., Okamura N., Hayakawa T., Shimohama S., Fujimoto S., Biol. Pharm. Bull., 22, 556-560 (1999).
18. Market M., Andrews P. C., Babior M. B., "Methods in Enzymology," Vol. 105, ed. by Packer L., Academic Press, Orlando, FL, 1984, pp. 358-365.
19. Laemmli U. K., Nature (London), 227, 680-685 (1990).
20. Simon P. G., Wayne A. P., Biochim. Biophys. Acta, 1222, 241-248 (1994).
21. Trevillyan J. M., Lu Y., Atluru D., Phillips C. A., Bjorndahl J. M., J. Immunol., 145, 3223-3230 (1990).
22. Honeycutt P. J., Niedel J. E., J. Biol. Chem., 261, 15900-15905 (1991).
23. Harbecke O., Liu L., Karlsson A., Dahlgren C., J. Leukoc. Biol., 61, 753-758 (1997).
24. Johansson A., Sarndahl E., Andersson T., Bengtsson T., Lundqvist H., Dahlgren C., Inflammation, 19, 179-191 (1995).