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Prepublished online as a Blood First Edition Paper on January 16, 2003; DOI 10.1182/blood-2002-07-2346. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-07-2346v1 101/10/4155    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mócsai, A. Articles by Lowell, C. A. Search for Related Content PubMed PubMed Citation Articles by Mócsai, A. Articles by Lowell, C. A. Related Collections Immunobiology Phagocytes Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 May 2003, Vol. 101, No. 10, pp. 4155-4163 PHAGOCYTES G-protein-coupled receptor signaling in Syk-deficient neutrophils and mast cells Attila Mócsai, Hong Zhang, Zoltán Jakus, Jiro Kitaura, Toshiaki Kawakami, and Clifford A. Lowell From the Department of Laboratory Medicine, University of California, San Francisco, CA; the Department of Physiology, Semmelweis University, Budapest, Hungary; and the Division of Allergy, La Jolla Institute for Allergy and Immunology, San Diego, CA. The Syk tyrosine kinase is essential for immunoreceptor and multiple integrin functions as well as being implicated in signaling from G-protein-coupled receptors (GPCR) in cell lines, transfection systems, and pharmacologic studies. In contrast, using Syk-deficient primary cells, we show here that Syk does not play a major functional role in chemoattractant/chemokine signaling in neutrophils and mast cells. syk/ neutrophils showed normal respiratory burst and degranulation in response to the bacterial peptide formyl-Met-Leu-Phe (fMLP). The migration of neutrophils toward fMLP was similarly not affected by the syk/ mutation. fMLP initiated normal Ca2+-signal, activation of the extracellular signal-related kinase (ERK) and p38 mitogen-activated protein (MAP) kinase cascades, and polymerization of cellular actin in the absence of Syk. syk/ and wild-type neutrophils also responded similarly to LTB4, C5a, and the chemokines macrophage inflammatory protein-1 (MIP-1) or MIP-2, both in functional assays and in intracellular signaling mechanisms. Furthermore, bone marrow-derived syk/ mast cells showed normal activation of the Akt, ERK, and p38 MAP kinase pathways when stimulated by the GPCR ligand adenosine. 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