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Prepublished online as a Blood First Edition Paper on January 16, 2003; DOI 10.1182/blood-2002-07-2346.
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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. We conclude
that, in contrast to previous reports, Syk does not play a major role
in GPCR signaling.
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