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Blood, 15 December 2006, Vol. 108, No. 13, pp. 4094-4101. Prepublished online as a Blood First Edition Paper on August 15, 2006; DOI 10.1182/blood-2006-03-011742. This Article Full Text (PDF) All Versions of this Article: blood-2006-03-011742v1 108/13/4094    most recent Alert me when this article is cited Alert me if a correction is posted 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 Fischer, K. Articles by Mackensen, A. Search for Related Content PubMed PubMed Citation Articles by Fischer, K. Articles by Mackensen, A. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted March 28, 2006 Accepted July 31, 2006 Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells Karin Fischer*, Simon Voelkl, Jana Berger, Reinhard Andreesen, Thomas Pomorski, and Andreas Mackensen Dept. of Hematology/Oncology, University of Regensburg, Regensburg, Germany Institute of Biology, Cell Biophysics, Humboldt University Berlin, Berlin, Germany * Corresponding author; email: karin.fischer{at}klinik.uni-regensburg.de. In eukaryotic cells the phospholipid phosphatidylserine (PS) is restricted to the inner plasma membrane leaflet. This lipid asymmetry which is maintained by the concerted action of phospholipid transport proteins is mainly lost during apoptosis. Here, we demonstrate that primary human CD8+ cytotoxic T lymphocytes (CTL) expose PS upon T cell receptor (TCR)-mediated antigen (Ag) recognition. In contrast to PS externalisation on apoptotic cells, activation-induced PS exposure is less pronounced and reversible. Fluorescence microscopic analysis revealed that PS is distributed inhomogenously over the plasma membrane and concentrated in membrane lipid raft domains at the immunological synapse. By studying the activity of PS transport proteins using a fluorescence-labeled PS analogue, we found that activation of CTL inhibited the flippase-mediated inward directed PS transport without affecting the outward transport. Shielding of exposed PS by annexinV protein during Ag recognition diminished cytokine secretion, activation and cell-cell clustering of Ag-specific CTL. In summary, our data demonstrate for the first time that externalized PS on Ag-stimulated CTL is linked to T cell activation and probably involved in cell-cell contact formation at the immunological synapse. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: D. Schilling, M. Gehrmann, C. Steinem, A. De Maio, A. G. Pockley, M. Abend, M. Molls, and G. Multhoff Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells FASEB J, August 1, 2009; 23(8): 2467 - 2477. [Abstract] [Full Text] [PDF] S. R. Stowell, S. Karmakar, C. M. Arthur, T. Ju, L. C. Rodrigues, T. B. Riul, M. Dias-Baruffi, J. Miner, R. P. McEver, and R. D. Cummings Galectin-1 Induces Reversible Phosphatidylserine Exposure at the Plasma Membrane Mol. Biol. Cell, March 1, 2009; 20(5): 1408 - 1418. [Abstract] [Full Text] [PDF] F. G. Blankenberg In Vivo Detection of Apoptosis J. Nucl. Med., June 1, 2008; 49(Suppl_2): 81S - 95S. [Abstract] [Full Text] [PDF] D. Smrz, P. Lebduska, L. Draberova, J. Korb, and P. Draber Engagement of Phospholipid Scramblase 1 in Activated Cells: IMPLICATION FOR PHOSPHATIDYLSERINE EXTERNALIZATION AND EXOCYTOSIS J. Biol. 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