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Related Collections Phagocytes Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 December 2001, Vol. 98, No. 12, pp. 3421-3428 PHAGOCYTES Functional coupling of FcRI to nicotinamide adenine dinucleotide phosphate (reduced form) oxidative burst and immune complex trafficking requires the activation of phospholipase D1 Alirio J. Melendez, Luce Bruetschy, R. Andres Floto, Margaret M. Harnett, and Janet M. Allen From the Department of Molecular and Cellular Biology, Pfizer Global Research and Development, Fresnes, France; the Department of Medicine, Imperial College School of Medicine, London, United Kingdom; and the Department of Immunology, the Department of Medicine and Therapeutics, and the Division of Biochemistry and Molecular Biology, University of Glasgow, Scotland. Immunoglobulin G (IgG) receptors (FcRs) on myeloid cells are responsible for the internalization of immune complexes. Activation of the oxidase burst is an important component of the integrated cellular response mediated by Fc receptors. Previous work has demonstrated that, in interferon--primed U937 cells, the high-affinity receptor for IgG, FcRI, is coupled to a novel intracellular signaling pathway that involves the sequential activation of phospholipase D (PLD), sphingosine kinase, and calcium transients. Here, it is shown that both known PLD isozymes, PLD1 and PLD2, were present in these cells. With the use of antisense oligonucleotides to specifically reduce the expression of either isozyme, PLD1, but not PLD2, was found to be coupled to FcRI activation and be required to mediate receptor activation of sphingosine kinase and calcium transients. In addition, coupling of FcRI to activation of the nicotinamide adenine dinucleotide phosphate (reduced form) (NADPH) oxidase burst was inhibited by pretreating cells with 0.3% butan-1-ol, indicating an absolute requirement for PLD. Furthermore, use of antisense oligonucleotides to reduce expression of PLD1 or PLD2 demonstrated that PLD1 is required to couple FcRI to the activation of NADPH oxidase and trafficking of internalized immune complexes for degradation. These studies demonstrate the critical role of PLD1 in the intracellular signaling cascades initiated by FcRI and its functional role in coordinating the response to antigen-antibody complexes. © 2001 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: P. D. A. Issuree, P. N. Pushparaj, S. Pervaiz, and A. J. Melendez Resveratrol attenuates C5a-induced inflammatory responses in vitro and in vivo by inhibiting phospholipase D and sphingosine kinase activities FASEB J, August 1, 2009; 23(8): 2412 - 2424. [Abstract] [Full Text] [PDF] X. Dai, M. Jayapal, H. K. Tay, R. Reghunathan, G. Lin, C. T. Too, Y. T. Lim, S. H. Chan, D. M. Kemeny, R. 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