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J. Biol. Chem., Vol. 278, Issue 26, 23915-23921, June 27, 2003

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CD47 and the 19 kDa Interacting Protein-3 (BNIP3) in T Cell Apoptosis^*

Laurence Lamy , Michel Ticchioni , Alexandre K. Rouquette-Jazdanian , Michel Samson ¶, Marcel Deckert , Arnold H. Greenberg || and Alain Bernard  

From the Unité INSERM 576 et Laboratoire d'Immunologie, 06202 Nice cedex 3, France, the ^¶Unité INSERM 364, Faculté de Médecine Pasteur, 06107 Nice cedex 2, France, and the ^||Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Canada R3E OV9

CD47 is a surface receptor that induces either coactivation or apoptosis in lymphocytes, depending on the ligand(s) bound. Interestingly, the apoptotic pathway is independent of caspase activation and cytochrome c release and is accompanied by early mitochondrial dysfunction with suppression of mitochondrial membrane potential (m). Using CD47 as bait in a yeast two-hybrid system, we identified the Bcl-2 homology 3 (BH3)-only protein 19 kDa interacting protein-3 (BNIP3), a pro-apoptotic member of the Bcl-2 family, as a novel partner. Interaction between CD47 and the BH3-only protein was confirmed by immunoprecipitation analysis, and CD47-induced apoptosis was inhibited by attenuating BNIP3 expression with antisense oligonucleotides. Finally, we showed that the C-terminal domain of thrombospondin-1 (TSP-1), but not signal-regulatory protein (SIRP1), is the ligand for CD47 involved in inducing cell death. Immunofluorescence analysis of CD47 and BNIP3 revealed a partial colocalization of both molecules under basal conditions. After T cell stimulation via CD47, BNIP3 translocates to the mitochondria to induce apoptosis. These results show that the BH3-dependent apoptotic pathways, previously shown to be activated by intracellular pro-apoptotic events, can also be turned on by surface receptors. This new pathway results in a fast induction of cell death resembling necrosis, which is likely to play an important role in lymphocyte regulation at inflammatory sites and/or in the vicinity of thrombosis.

Received for publication, February 21, 2003 , and in revised form, April 9, 2003.

^* This work was supported by grants from the Institut National de la Santé et de la Recherche Médicale, the Association pour la Recherche sur le Cancer, the Etablissement Français des Greffes, and the Fondation pour la Recherche Médicale. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: INSERM U576, IFR 50, Hôpital de l'Archet 1, 06202 Nice cedex 3, France. Tel.: 33-492-157-700; Fax: 33-492-157-709; E-mail: abernard{at}unice.fr.

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