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The Journal of Immunology, Vol 158, Issue 12 5668-5675, Copyright © 1997 by American Association of Immunologists
ARTICLES |
SN Liossis, XZ Ding, JG Kiang and GC Tsokos
Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, D.C. 20307-5100, USA.
To investigate whether the protective effects of the 70-kDa heat shock protein (hsp70) extend to the apoptotic mode of cell death, we transfected Jurkat T cells with the gene for the human hsp70 and challenged the cells with an anti-Fas mAb or with two different murine anti-CD3 mAbs. The anti-Fas mAb-triggered apoptotic cell death and the anti-CD3 mAb-mediated activation-induced cell death were significantly enhanced in the gene-transfected Jurkat cells overexpressing hsp70 compared with the unmanipulated and the vector-transfected cells. On the other hand, the well-established protective effect that this protein offers to the cells was unaffected, as determined by enhanced viability of gene-transfected cells exposed to a lethal heat shock. To investigate the mechanisms that are responsible for the increased susceptibility of the gene-transfected cells to apoptotic death, we studied the TCR/CD3-initiated events that showed a significant down- regulation of the protein tyrosine phosphorylation levels and the cytoplasmic free Ca2+ responses. As for the Fas/Apo-1/CD95-mediated early events, the activity of protein serine/threonine phosphatases was markedly increased in the cells overexpressing hsp70. Our study demonstrates that hsp70 overexpression offers thermoprotection but enhances TCR/CD3- and the Fas-induced apoptotic cell death. This phenomenon is associated with a down-regulation of the Ag receptor- initiated early signal transduction pathways and with an up-regulation of Fas-mediated early metabolic events.
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