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Blood, 15 November 2004, Vol. 104, No. 10, pp. 3233-3242.
Prepublished online as a Blood First Edition Paper on June 15, 2004; DOI 10.1182/blood-2003-05-1679.
Previous Article | Next Article 
Submitted May 29, 2003
Accepted May 17, 2004
Cross-linking of P-selectin glycoprotein ligand-1 induces death of activated T cells
Shu-Ching Chen, Chiu-Chen Huang, Chung-Liang Chien, Chung-Jiuan Jeng, Ho-Ting Su, Evelyn Chiang, Meng-Ru Liu, C H Wu, Chung-Nan Chang, and Rong-Hwa Lin*
Graduate Institute of Immunology, National Taiwan University, Taipei, Taiwan; AbGenomics Co., Taipei, Taiwan
AbGenomics Co., Taipei, Taiwan
Department of Anatomy and Cell Biology, National Taiwan University, Taipei, Taiwan
Department of Medicine, FuJen Catholic University, Taipei, Taiwan; AbGenomics Co., Taipei, Taiwan
* Corresponding author; email: rhlin{at}abgenomics.com.
Increasing evidence has shown that death signaling in T cells is regulated in a very complicated way. Molecules other than death receptors can also trigger T-cell death. Here we demonstrate for the first time that P-selectin glycoprotein ligand-1 (PSGL-1) or CD162 molecules cross-linked by an anti-PSGL-1 monoclonal antibody, TAB4, can trigger a death signal in activated T cells. In contrast to classical cell death, PSGL-1-mediated T cell death is caspase-independent. It involves translocation of apoptosis-inducing factor from mitochondria to nucleus and mitochondrial cytochrome c release. Ultrastructurally, both peripheral condensation of chromatin and apoptotic body were observed in PSGL-1-mediated T-cell death. Collectively, this study demonstrates a novel role of PSGL-1 in controlling activated T-cell death and thus advances our understanding of immune regulation.

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