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*
Department of Physiology, Semmelweis University of Medicine, Budapest, Hungary;
Joint Research Organization of the Hungarian Academy of Sciences and Department of Medical Chemistry, Molecular Biology, and Pathobiochemistry, Semmelweis University of Medicine, Budapest, Hungary;
Department of Pathology, Section of General Pathology, University of Verona, Verona, Italy; and
§
Department of Laboratory Medicine, University of California, San Francisco, CA 94143
The aim of the present study was to investigate the role of tyrosine phosphorylation pathways in fMLP-induced exocytosis of the different secretory compartments (primary and secondary granules, as well as secretory vesicles) of neutrophils. Genistein, a broad specificity tyrosine kinase inhibitor, blocked the exocytosis of primary and secondary granules, but had only a marginal effect on the release of secretory vesicles. Genistein also inhibited the phosphorylation of extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein kinases (MAPK), raising the possibility that inhibition of ERK and/or p38 MAPK might be responsible for the effect of the drug on the degranulation response. Indeed, SB203580, an inhibitor of p38 MAPK, decreased the release of primary and secondary granules, but not that of secretory vesicles. However, blocking the ERK pathway with PD98059 had no effect on any of the exocytic responses tested. PP1, an inhibitor of Src family kinases, also attenuated the release of primary and secondary granules, and neutrophils from mice deficient in the Src family kinases Hck, Fgr, and Lyn were also defective in secondary granule release. Furthermore, activation of p38 MAPK was blocked by both PP1 and the hck-/-fgr-/-lyn-/- mutation. Taken together, our data indicate that fMLP-induced degranulation of primary and secondary granules of neutrophils is mediated by p38 MAPK activated via Src family tyrosine kinases. Although piceatannol, a reportedly selective inhibitor of Syk, also prevented degranulation and activation of p38 MAPK, no fMLP-induced phosphorylation of Syk could be observed, raising doubts about the specificity of the inhibitor.
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 T. Sato, L. Koike, Y. Miyata, M. Hirata, Y. Mimaki, Y. Sashida, M. Yano, and A. Ito Inhibition of Activator Protein-1 Binding Activity and Phosphatidylinositol 3-Kinase Pathway by Nobiletin, a Polymethoxy Flavonoid, Results in Augmentation of Tissue Inhibitor of Metalloproteinases-1 Production and Suppression of Production of Matrix Metalloproteinases-1 and -9 in Human Fibrosarcoma HT-1080 Cells Cancer Res., February 1, 2002; 62(4): 1025 - 1029. [Abstract] [Full Text] [PDF]
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E. Nijhuis, J.-W. J Lammers, L. Koenderman, and P. J. Coffer Src kinases regulate PKB activation and modulate cytokine and chemoattractant-controlled neutrophil functioning J. Leukoc. Biol., January 1, 2002; 71(1): 115 - 124. [Abstract] [Full Text] [PDF]
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R. Liu, K. Aupperle, and R. Terkeltaub Src family protein tyrosine kinase signaling mediates monosodium urate crystal-induced IL-8 expression by monocytic THP-1 cells J. Leukoc. Biol., December 1, 2001; 70(6): 961 - 968. [Abstract] [Full Text] [PDF]
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 W. Kang, H. Saito, K. Fukatsu, A. Hidemura, H. Koyama, T. Sakamoto, and K. Maekawa Effects of Tyrosine Kinase Signaling Inhibition on Survival After Cecal Ligation and Puncture in Diet-Restricted Mice JPEN J Parenter Enteral Nutr, November 1, 2001; 25(6): 291 - 298. [Abstract] [PDF]
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P. Desaulniers, M. Fernandes, C. Gilbert, S. G. Bourgoin, and P. H. Naccache Crystal-induced neutrophil activation. VII. Involvement of Syk in the responses to monosodium urate crystals J. Leukoc. Biol., October 1, 2001; 70(4): 659 - 668. [Abstract] [Full Text] [PDF]
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M. O. Hannigan, L. Zhan, Y. Ai, A. Kotlyarov, M. Gaestel, and C.-K. Huang Abnormal Migration Phenotype of Mitogen-Activated Protein Kinase-Activated Protein Kinase 2-/- Neutrophils in Zigmond Chambers Containing Formyl-Methionyl-Leucyl-Phenylalanine Gradients J. Immunol., October 1, 2001; 167(7): 3953 - 3961. [Abstract] [Full Text] [PDF]
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X. Zhu, H. Sano, K. P. Kim, A. Sano, E. Boetticher, N. M. Munoz, W. Cho, and A. R. Leff Role of Mitogen-Activated Protein Kinase-Mediated Cytosolic Phospholipase A2 Activation in Arachidonic Acid Metabolism in Human Eosinophils J. Immunol., July 1, 2001; 167(1): 461 - 468. [Abstract] [Full Text] [PDF]
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Z. Korade-Mirnics and S. J. Corey Src kinase-mediated signaling in leukocytes J. Leukoc. Biol., November 1, 2000; 68(5): 603 - 613. [Abstract] [Full Text]
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R. A. Ward, M. Nakamura, and K. R. McLeish Priming of the Neutrophil Respiratory Burst Involves p38 Mitogen-activated Protein Kinase-dependent Exocytosis of Flavocytochrome b558-containing Granules J. Biol. Chem., November 17, 2000; 275(47): 36713 - 36719. [Abstract] [Full Text] [PDF]
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P. Kumar, S. Hosaka, and A. E. Koch Soluble E-selectin Induces Monocyte Chemotaxis through Src Family Tyrosine Kinases J. Biol. Chem., June 8, 2001; 276(24): 21039 - 21045. [Abstract] [Full Text] [PDF]
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