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FasL-triggered death of Jurkat cells requires caspase 8-induced, ATP-dependent cross-talk between Fas and the purinergic receptor P2X7

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Autor Aguirre A.
Autor Shoji K.F.
Autor Saez J.C.
Autor Henriquez M.
Autor Quest A.F.
Fecha Ingreso 2014-04-05T00:23:18Z
Fecha Disponible 2014-04-05T00:23:18Z
Fecha en Repositorio 2014-04-04
dc.identifier 10.1002/jcp.24159
dc.description.abstract Fas ligation via the ligand FasL activates the caspase-8/caspase-3-dependent extrinsic death pathway. In so-called type II cells, an additional mechanism involving tBid-mediated caspase-9 activation is required to efficiently trigger cell death. Other pathways linking FasL-Fas interaction to activation of the intrinsic cell death pathway remain unknown. However, ATP release and subsequent activation of purinergic P2X7 receptors (P2X7Rs) favors cell death in some cells. Here, we evaluated the possibility that ATP release downstream of caspase-8 via pannexin1 hemichannels (Panx1 HCs) and subsequent activation of P2X7Rs participate in FasL-stimulated cell death. Indeed, upon FasL stimulation, ATP was released from Jurkat cells in a time- and caspase-8-dependent manner. Fas and Panx1 HCs colocalized and inhibition of the latter, but not connexin hemichannels, reduced FasL-induced ATP release. Extracellular apyrase, which hydrolyzes ATP, reduced FasL-induced death. Also, oxidized-ATP or Brilliant Blue G, two P2X7R blockers, reduced FasL-induced caspase-9 activation and cell death. These results represent the first evidence indicating that the two death receptors, Fas and P2X7R connect functionally via caspase-8 and Panx1 HC-mediated ATP release to promote caspase-9/caspase-3-dependent cell death in lymphoid cells. Thus, a hitherto unsuspected route was uncovered connecting the extrinsic to the intrinsic pathway to amplify death signals emanating from the Fas receptor in type II cells. © 2012 Wiley Periodicals, Inc. en_US
dc.source Journal of Cellular Physiology
Link Descarga dc.source.uri
Title dc.title FasL-triggered death of Jurkat cells requires caspase 8-induced, ATP-dependent cross-talk between Fas and the purinergic receptor P2X7 en_US
Tipo dc.type Article
dc.description.keywords adenosine triphosphate; annexin; apyrase; brilliant blue; caspase 3; caspase 8; caspase 9; Fas ligand; pannexin i hemichannel; purinergic P2X7 receptor; unclassified drug; article; cell activation; cell death; cell stimulation; cell viability; cellular distribution; controlled study; human; human cell; hydrolysis; leukemia cell line; molecular interaction; priority journal; protein expression; signal transduction; Adenosine Triphosphate; Antigens, CD95; Apoptosis; Apyrase; Caspase 3; Caspase 8; Caspase 9; Connexins; Fas Ligand Protein; Humans; Jurkat Cells; Nerve Tissue Proteins; Purinergic P2X Receptor Antagonists; Receptors, Purinergic P2X7; Rosaniline Dyes; Signal Transduction en_US

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