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  • hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
  • Gotoh T; Terada K; Oyadomari S; Mori M
  • Cell Death Differ 2004[Apr]; 11 (4): 390-402
  • We reported that the endoplasmic reticulum (ER) stress pathway involving CHOP, a member of the C/EBP transcription factor family, plays a key role in nitric oxide (NO)-mediated apoptosis of macrophages and pancreatic beta cells. We also showed that the cytosolic chaperone pair of hsp70 and dj1 (hsp40/hdj-1) or dj2 (HSDJ/hdj-2) prevents NO-mediated apoptosis upstream of cytochrome c release from mitochondria. To analyze roles of the chaperone pair in preventing apoptosis, RAW 264.7 macrophages stably expressing hsp70 and dj1 or dj2 were established. The chaperone pair prevented LPS/IFN-gamma-induced and NO-mediated apoptosis downstream of CHOP induction. hsp70 mutant protein lacking the ATPase domain or the C-terminal EEVD sequence were not effective in preventing CHOP-induced apoptosis. A mutant dj2 lacking the C-terminal prenylation CaaX motif, was also not effective. When wild-type RAW 264.7 cells were treated with LPS/IFN-gamma, NO-mediated apoptosis was induced, and proapoptotic Bcl-2 family protein Bax was translocated from cytosol to mitochondria. This translocation was prevented in cells stably expressing hsp70/dj2, and in CHOP knockout cells. Overexpression of CHOP in wild-type cells also induced translocation of Bax and this translocation was prevented in cells expressing hsp70/dj2. CHOP-induced apoptosis was prevented by Bax knock-down. Coimmunoprecipitation experiments showed that Bax interacts with both hsp70 and dj1/dj2. ATPase domain of hsp70 was necessary for the binding with Bax. These findings indicate that CHOP-induced apoptosis is mediated by translocation of Bax from the cytosol to the mitochondria, and hsp70/dj1 or dj2 chaperone pair prevents apoptosis by interacting with Bax and preventing translocation to the mitochondria.
  • |*Proto-Oncogene Proteins c-bcl-2[MESH]
  • |Adenosine Triphosphatases/metabolism[MESH]
  • |Animals[MESH]
  • |Apoptosis/physiology[MESH]
  • |CCAAT-Enhancer-Binding Proteins/*antagonists & inhibitors/metabolism[MESH]
  • |COS Cells[MESH]
  • |Cell Line[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Cytosol/metabolism[MESH]
  • |HSP40 Heat-Shock Proteins[MESH]
  • |HSP70 Heat-Shock Proteins/genetics/*physiology[MESH]
  • |Heat-Shock Proteins/genetics/*physiology[MESH]
  • |Macrophages/cytology/metabolism[MESH]
  • |Mice[MESH]
  • |Mice, Knockout[MESH]
  • |Mitochondria/metabolism[MESH]
  • |Molecular Chaperones/metabolism/*pharmacology[MESH]
  • |Nitric Oxide/*antagonists & inhibitors[MESH]
  • |Protein Transport/physiology[MESH]
  • |Proto-Oncogene Proteins/antagonists & inhibitors/*metabolism[MESH]
  • |Transcription Factor CHOP[MESH]
  • |Transcription Factors/*antagonists & inhibitors/metabolism[MESH]
  • |Transfection[MESH]
  • |bcl-2-Associated X Protein[MESH]

  • *{{pmid14752510}}
    *<b>[ hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria ]</b> Cell Death Differ 2004; 11(4) ; 390-402 Gotoh T; Terada K; Oyadomari S; Mori M


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    Cell Death Differ

    390 4.11 2004