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Investigation of neutrophil signal transduction using a specific inhibitor of phosphatidylinositol 3-kinase.

C J Vlahos, W F Matter, R F Brown, A E Traynor-Kaplan, P G Heyworth, E R Prossnitz, R D Ye, P Marder, J A Schelm and K J Rothfuss
J Immunol March 1, 1995, 154 (5) 2413-2422;
C J Vlahos
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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W F Matter
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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R F Brown
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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A E Traynor-Kaplan
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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P G Heyworth
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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E R Prossnitz
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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R D Ye
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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P Marder
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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J A Schelm
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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K J Rothfuss
Lilly Research Labortories, Eli Lilly and Company, Indianapolis, IN 46285.
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Abstract

Neutrophils contain a multicomponent NADPH oxidase system that is involved in the production of microbicidal oxidants. Stimulation of human neutrophils with the peptide FMLP activates this respiratory burst enzyme to produce superoxide and also has been shown to result in activation of phosphatidylinositol (Ptdlns) 3-kinase. Treatment of human neutrophils with 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002), a potent and specific inhibitor of Ptdlns 3-kinase, resulted in complete inhibition of Ptdlns 3-kinase activity as well as in inhibition of superoxide production in FMLP-treated neutrophils in suspension; FMLP-stimulated oxidant production in adherent cells was also abolished. Treatment of human neutrophils with PMA resulted in production of superoxide without activation of Ptdlns 3-kinase; LY294002 did not block superoxide production in neutrophils exposed to PMA. In addition, LY294002 did not inhibit cellfree NADPH oxidase activation, CD11b-dependent adhesion, actin polymerization in response to FMLP, or FMLP-induced calcium flux. These results suggest that the signal transduction pathway of the FMLP-receptor involves activation of Ptdlns 3-kinase, which is required for subsequent superoxide production induced by the chemotactic peptide. Furthermore, Ptdlns 3-kinase may be located directly upstream of protein kinase C or other protein kinases, which in turn activate the NADPH oxidase system.

  • Copyright © 1995 by American Association of Immunologists
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The Journal of Immunology
Vol. 154, Issue 5
1 Mar 1995
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Investigation of neutrophil signal transduction using a specific inhibitor of phosphatidylinositol 3-kinase.
C J Vlahos, W F Matter, R F Brown, A E Traynor-Kaplan, P G Heyworth, E R Prossnitz, R D Ye, P Marder, J A Schelm, K J Rothfuss
The Journal of Immunology March 1, 1995, 154 (5) 2413-2422;

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Investigation of neutrophil signal transduction using a specific inhibitor of phosphatidylinositol 3-kinase.
C J Vlahos, W F Matter, R F Brown, A E Traynor-Kaplan, P G Heyworth, E R Prossnitz, R D Ye, P Marder, J A Schelm, K J Rothfuss
The Journal of Immunology March 1, 1995, 154 (5) 2413-2422;
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Print ISSN 0022-1767        Online ISSN 1550-6606