Long lasting heat shock stimulation of TRAIL-induced apoptosis in transformed T lymphocytes.
We report that a mild heat shock, that did not impair cell growth, stimulated TNF-related apoptosis inducing ligand (TRAIL)-mediated apoptosis of leukemic T lymphocytes and promyelocytic cells, but not normal human T lymphocytes. The death stimulation was maximal when the heat shock was performed at the beginning of the exposure to TRAIL. However, enhanced apoptosis was still observed when TRAIL was added one day after heat shock. The phenomenon was transcription and translation independent suggesting that newly made heat shock proteins were not involved. TRAIL-induced apoptosis after heat shock was dependent on caspases and FADD and an enhanced FlipL/S processing was noticed. However, since after the heat shock FlipL/S processing was transient, events upstream of caspase 8 and FADD may be responsible of the long lasting enhanced TRAIL apoptosis observed after heat shock. No heat-mediated alteration in the antibody recognition of cell surface DR4 and DR5 TRAIL receptors was observed. However, in the presence of TRAIL, a long lasting attenuation in the antibody detection of DR4 and DR5 was observed in heat shock-treated cells that correlated with the enhanced apoptogenic efficiency of TRAIL.
Laboratoire stress oxydant, chaperons et apoptose, CNRS UMR 5534, Centre de Génétique Moléculaire et Cellulaire, Université Claude Bernard, LYON-1, 43, Bd du 11 Novembre, 69622 Villeurbanne Cedex, France.
Maryline
M
Moulin
André-Patrick
AP
Arrigo
D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D017209:Apoptosis / Q000502:physiology*; D051017:Apoptosis Regulatory Proteins / Q000235:genetics / Q000378:metabolism*; D053446:CASP8 and FADD-Like Apoptosis Regulating Protein; D053181:Caspase 8; D020169:Caspases / Q000378:metabolism; D002453:Cell Cycle / Q000502:physiology; D002458:Cell Fractionation; D002471:Cell Transformation, Neoplastic; D053938:DNA Fragmentation; D053200:Fas-Associated Death Domain Protein; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D019169:Jurkat Cells; D008213:Lymphocyte Activation; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism; D018124:Receptors, Tumor Necrosis Factor / Q000378:metabolism; D013601:T-Lymphocytes / Q000502:physiology*; D053221:TNF-Related Apoptosis-Inducing Ligand; D014409:Tumor Necrosis Factor-alpha / Q000235:genetics / Q000378:metabolism*
D048868:Adaptor Proteins, Signal Transducing; D051017:Apoptosis Regulatory Proteins; D053446:CASP8 and FADD-Like Apoptosis Regulating Protein; C506386:CFLAR protein, human; C505533:FADD protein, human; D053200:Fas-Associated Death Domain Protein; D006360:Heat-Shock Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins; D011956:Receptors, Cell Surface; D018124:Receptors, Tumor Necrosis Factor; D053221:TNF-Related Apoptosis-Inducing Ligand; C505653:TNFSF10 protein, human; D014409:Tumor Necrosis Factor-alpha; C505530:CASP8 protein, human; D053181:Caspase 8; D020169:Caspases