BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Involvement of Protein Tyrosine Kinase in Stimulated Neutrophil Responses by Sodium Fluoride

  • Chung, Ki-Kwang (Department of Pharmacology, College of Medicine, Chung-Ang University) ;
  • Han, Eun-Sook (Department of Pharmacology, College of Medicine, Chung-Ang University) ;
  • Lee, Chung-Soo (Department of Pharmacology, College of Medicine, Chung-Ang University)
  • Received : 1996.11.26
  • Published : 1997.03.31
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Abstract

In this study, during the activation of neutrophil responses by sodium fluoride. involvement of protein tyrosine kinase was studied. Respiratory burst lysosomal enzyme release and elevation of $[Ca^{2+}]_i$stimulated by sodium fluoride in neutrophils were inhibited by protein kinase inhibitors, genistein and tyrphostin. The inhibitory effect of genistein and tyrphostin on superoxide and $H_{2}O_{2}$ production was less than that of protein kinase C inhibitors, staurosporine and H-7. Staurosporine and H-7 had little or no effect on the release of myeloperoxidase and acid phosphatase stimulated by sodium fluoride. EGTA and verapamil inhibited the elevation of $[Ca^{2+}]_i$ evoked by sodium fluoride. The inhibitory effect of staurosporine on the elevation of $[Ca^{2+}]_i$ was less than that of genistein. Phorbol 12-myristate 13-acetate (PMA)-stimulated superoxide production, which is sensitive to staurosporine, was further enhanced by genistein, whereas the stimulatory action of PMA on myeloperoxidase release was inhibited by genistein. A pretreatment of neutrophils with PMA signifcantly attenuated sodium fluoride-evoked elevation of $[Ca^{2+}]_i$ These results suggest that protein tyrosine kinase may be involved in the activation process of neutrophil responses due to direct stimulation of guanine nucleotide regulatory proteins. In neutrophil responses, PMA-stimulated neutrophils appear to show a different type of inhibition of protein tyrosine kinase.

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References

  1. N. Engl. J. Med. v.298 Babior, B.M. https://doi.org/10.1056/NEJM197803232981205
  2. J. Cell Biol. v.93 Bareis, D.L.;Hirata, F.;Schiffmann, E.;Axelrod, J. https://doi.org/10.1083/jcb.93.3.690
  3. Blood v.75 Berkow, R.L.;Dodson, R.W.
  4. Ann. Rev. Biochem. v.56 Berridge, M.J. https://doi.org/10.1146/annurev.bi.56.070187.001111
  5. J. Biol. Chem. v.260 Blackmore, P.F.;Bocckino, S.B.;Waynick, L.E.;Exton, J.H.
  6. Biochem. J. v.248 Cobbold, P.H.;Rink, T.J. https://doi.org/10.1042/bj2480313
  7. Biochem. J. v.241 Cockcroft, S.;Taylor, J.A. https://doi.org/10.1042/bj2410409
  8. J. Gen. Physiol. v.82 Corson, D.W.;Fein, A. https://doi.org/10.1085/jgp.82.5.639
  9. J. Clin. Invest. v.63 Curnutte, J.T.;Babior, B.M.;Karnovsky, M.L. https://doi.org/10.1172/JCI109346
  10. Biochem. Biophys. Res. Commun. v.135 Della Bianca, V.;Grzeskowiak, M.;Cassatella, M.;Zeni, L.;Rossi. F. https://doi.org/10.1016/0006-291X(86)90030-6
  11. J. Clin. Invest. v.80 English, D.;Debono, D.J.;Gabig, T.G. https://doi.org/10.1172/JCI113040
  12. J. Immunol. v.143 English, D.;Rizzo, M.T.;Tricot, G.;Hoffman, R.
  13. Am. J. Pathol. v.107 Fantone, J.C.;Ward, P.A.
  14. Ann. Rev. Biochem. v.44 Fridovich, I. https://doi.org/10.1146/annurev.bi.44.070175.001051
  15. J. Biochem. Mol. Biol. (formerly Korean Biochem. J.) v.28 Ha, S.H.;Lee, C.S.
  16. J. Biol. Chem. v.260 Kanaho, Y.;Moss, J.;Vaughan, M.
  17. Agents Actions v.12 Kuza, M.;Kazimierczak, W. https://doi.org/10.1007/BF01965391
  18. Biochem. Pharmacol. v.39 Luscinskas, F.W.;Nicolaou, K.C.;Webber, S.E.;Veale, C.A.;Gimbrone, M.A. Jr.;Serhan, C.N. https://doi.org/10.1016/0006-2952(90)90035-J
  19. Methods Enzymol. Vol. 105 Markert, M.;Andrews, P.C.;Babior, B.M.;Parker, L.(ed.)
  20. Biochem. J. v.264 McCarthy, S.A.;Hallam, T.J.;Merritt, J.E. https://doi.org/10.1042/bj2640357
  21. J. Clin. Invest. v.53 Root, R.K.;Metcalf, J.;Oshino, N.;Chance, B.
  22. Korean J. Pharmacol. v.25 Shin, J.H.;Lee, C.S.;Han, E.S.;Shin, Y.K.;Lee, K.S.
  23. Chemoattractant stimulus-response coupling. Inflammation: Basic Principles and Clinical Correlates Snyderman, R.;Uhing, R.J.;Gallin, J.I.(ed.);Goldstein, I.M.(ed.);Synderman, R.(ed.)
  24. J. Immunol. v.135 Spangrude, G.J.;Sacchi, F.;Hill, H.R.;Van Epps, D.E.;Daynes, R.A.
  25. Biochem. Pharmacol. v.44 Tanimura, M.;Kobuchi, H.;Utsumi, T.;Yoshioka, T.;Kataoka, S.;Fujita, Y.;Utsumi, K. https://doi.org/10.1016/0006-2952(92)90366-Q
  26. N. Engl. J. Med. v.320 Weiss, S.J. https://doi.org/10.1056/NEJM198902093200606
  27. Agents Actions v.19 Westwick, J.;Poll, C. https://doi.org/10.1007/BF01977262