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This Article Full Text Full Text (PDF) 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 Taylor, L. S. Articles by McVicar, D. W. Search for Related Content PubMed PubMed Citation Articles by Taylor, L. S. Articles by McVicar, D. W. Related Collections Phagocytes Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 94 No. 5 (September 1), 1999: pp. 1790-1796 Functional Association of FcRI With Arginine632 of Paired Immunoglobulin-Like Receptor (PIR)-A3 in Murine Macrophages Lynn S. Taylor and Daniel W. McVicar From Laboratory of Experimental Immunology, Division of Basic Sciences, National Cancer Institute, NCI-FCRDC, Frederick, MD. Paired immunoglobulin-like receptors (PIR) are expressed on B cells and macrophages and include inhibitory and putative activating receptors referred to as PIR-B and PIR-A, respectively. Although PIR-B's inhibitory pathway has been described, it is unknown whether PIR-A receptors can deliver activation signals to macrophages, and if so, through what mechanism. Here we use chimeric receptors to address the mechanisms of PIR-A signaling. Cotransfection of chimeric receptors comprised of the extracellular region of human CD4 and the transmembrane and cytoplasmic domains of murine PIR-A3 showed the ability of PIR-A3 to physically interact with the FcRI chain in 293T cells. This interaction is dependent on Arg632 within the PIR-A3 transmembrane domain. We also demonstrate PIR-A3 interaction with the endogenous FcRI of the ANA-1 macrophage cell line, again in an Arg632-dependent manner. Furthermore, we show that crosslinking of these chimeric receptors synergizes with IFN- in the production of nitric oxide. Our data are the first to show the potential of PIR-A3 to deliver activation signals to macrophages and establish its dependence on Arg632. These findings suggest that further study of the PIR-A receptors should be aggressively pursued toward a complete understanding of the intricate regulation of macrophage biology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: I. Torii, S. Oka, M. Hotomi, W. H. Benjamin Jr, T. Takai, J. F. Kearney, D. E. Briles, and H. Kubagawa PIR-B-Deficient Mice Are Susceptible to Salmonella Infection J. Immunol., September 15, 2008; 181(6): 4229 - 4239. [Abstract] [Full Text] [PDF] Z. Jakus, G. Berton, E. Ligeti, C. A. Lowell, and A. Mocsai Responses of Neutrophils to Anti-Integrin Antibodies Depends on Costimulation through Low Affinity Fc{gamma}Rs: Full Activation Requires Both Integrin and Nonintegrin Signals J. Immunol., August 1, 2004; 173(3): 2068 - 2077. [Abstract] [Full Text] [PDF] D. D. Mousseau, D. Banville, D. L'Abbe, P. Bouchard, and S.-H. Shen PILRalpha , a Novel Immunoreceptor Tyrosine-based Inhibitory Motif-bearing Protein, Recruits SHP-1 upon Tyrosine Phosphorylation and Is Paired with the Truncated Counterpart PILRbeta J. Biol. Chem., February 11, 2000; 275(6): 4467 - 4474. [Abstract] [Full Text] [PDF] L. H. Ho, T. Uehara, C.-C. Chen, H. Kubagawa, and M. D. Cooper Constitutive tyrosine phosphorylation of the inhibitory paired Ig-like receptor PIR-B PNAS, December 21, 1999; 96(26): 15086 - 15090. [Abstract] [Full Text] [PDF] Y.-M. Zheng, C. Liu, H. Chen, D. Locke, J. C. Ryan, and M. L. Kahn Expression of the Platelet Receptor GPVI Confers Signaling via the Fc Receptor gamma -Chain in Response to the Snake Venom Convulxin but Not to Collagen J. Biol. Chem., April 13, 2001; 276(16): 12999 - 13006. [Abstract] [Full Text] [PDF]

	Copyright © 1999 by American Society of Hematology         Online ISSN: 1528-0020