SEARCH:   Advanced

Blood, 1 May 2005, Vol. 105, No. 9, pp. 3663-3670. Prepublished online as a Blood First Edition Paper on January 18, 2005; DOI 10.1182/blood-2004-08-3325. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-08-3325v1 105/9/3663    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 Bannas, P. Articles by Koch-Nolte, F. Search for Related Content PubMed PubMed Citation Articles by Bannas, P. Articles by Koch-Nolte, F. Related Collections Cell Adhesion and Motility Signal Transduction Immunobiology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Activity and specificity of toxin-related mouse T cell ecto–ADP-ribosyltransferase ART2.2 depends on its association with lipid rafts Peter Bannas, Sahil Adriouch, Sarah Kahl, Fenja Braasch, Friedrich Haag, and Friedrich Koch-Nolte From the Institute of Immunology, University Hospital, Hamburg, Germany. Adenosine diphosphate (ADP)–ribosyl-transferases (ARTs) transfer ADP-ribose from nicotinamide adenine dinucleotide (NAD) onto target proteins. T cells express ART2.2, a toxin-related, glycosylphosphatidylinositol (GPI)–anchored ecto-enzyme. After the release of NAD from cells, ART2.2 ADP-ribosylates the P2X7 purinoceptor, lymphocyte function–associated antigen (LFA-1), and other membrane. Using lymphoma transfectants expressing either ART2.2 with its native GPI anchor (ART2.2-GPI) or ART2.2 with a grafted transmembrane anchor (ART2.2-Tm), we demonstrated that ART2.2-GPI but not ART2.2-Tm associated with glycosphingolipid-enriched microdomains (lipid rafts). At limiting substrate concentrations, ART2.2-GPI exhibited more than 10-fold higher activity than ART2.2-Tm. On intact cells, ART2.2-GPI ADP-ribosylated a small number of distinct target proteins. Strikingly, the disruption of lipid rafts by cyclodextrin or membrane solubilization by Triton X-100 increased the spectrum of modified target proteins. However, ART2.2 itself was a prominent target for ADP-ribosylation only when GPI anchored. Furthermore, cholesterol depletion or detergent solubilization abolished the auto-ADP-ribosylation of ART2.2. These findings imply that ART2.2-GPI, but not ART2.2-Tm, molecules are closely associated on the plasma membrane and lend support to the hypothesis that lipid rafts exist on living cells as platforms to which certain proteins are admitted and others are excluded. Our results further suggest that raft association focuses ART2.2 on specific targets that constitutively or inducibly associate with lipid rafts. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Adriouch, P. Bannas, N. Schwarz, R. Fliegert, A. H. Guse, M. Seman, F. Haag, and F. Koch-Nolte ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site FASEB J, March 1, 2008; 22(3): 861 - 869. [Abstract] [Full Text] [PDF] F. Koch-Nolte, J. Reyelt, B. Schossow, N. Schwarz, F. Scheuplein, S. Rothenburg, F. Haag, V. Alzogaray, A. Cauerhff, and F. A. Goldbaum Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2 in vivo FASEB J, November 1, 2007; 21(13): 3490 - 3498. [Abstract] [Full Text] [PDF] S. Adriouch, S. Hubert, S. Pechberty, F. Koch-Nolte, F. Haag, and M. Seman NAD+ Released during Inflammation Participates in T Cell Homeostasis by Inducing ART2-Mediated Death of Naive T Cells In Vivo J. Immunol., July 1, 2007; 179(1): 186 - 194. [Abstract] [Full Text] [PDF] C. M. Cruz, A. Rinna, H. J. Forman, A. L. M. Ventura, P. M. Persechini, and D. M. Ojcius ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages J. Biol. Chem., February 2, 2007; 282(5): 2871 - 2879. [Abstract] [Full Text] [PDF] S. D. Liao and D. G. Puro NAD+-Induced Vasotoxicity in the Pericyte-Containing Microvasculature of the Rat Retina: Effect of Diabetes Invest. Ophthalmol. Vis. Sci., November 1, 2006; 47(11): 5032 - 5038. [Abstract] [Full Text] [PDF] M. Garcia-Marcos, E. Perez-Andres, S. Tandel, U. Fontanils, A. Kumps, E. Kabre, A. Gomez-Munoz, A. Marino, J.-P. Dehaye, and S. Pochet Coupling of two pools of P2X7 receptors to distinct intracellular signaling pathways in rat submandibular gland J. Lipid Res., April 1, 2006; 47(4): 705 - 714. [Abstract] [Full Text] [PDF]

	Blood Online is supported in part by Genentech BioOncology and Biogen Idec
	Copyright © 2005 by American Society of Hematology         Online ISSN: 1528-0020