@misc{oai:repo.qst.go.jp:00070158,
 author = {安田, 武嗣 and 安田 武嗣},
 month = {Dec},
 note = {PIDD (p53-induced protein with a death domain) plays a critical role in the activation of caspase-2 to trigger apoptosis induced by DNA damage through the formation of a so-called PIDDosome, which contains the adaptor protein RAIDD and caspase-2.     We found that transcription of PIDD was induced after exposure to ionizing radiation in rat small intestinal epithelial cell line (IEC6) cells.  Yeast two-hybrid analysis indicated that the death domain of rat PIDD interacts with RAIDD.  Interestingly, a rat C-terminal PIDD fragment (residues 773-917) containing the death domain interacts with RAIDD much more tightly than the longer PIDD fragment (residues 610-917).  When the PIDD (773-917) fragment was overexpressed in theses cells, the PIDD-mediated activation of caspase-2 was dominant-negatively inhibited.  In order to use the PIDD (773-917) fragment as an anti-apoptotic drug, we purified a recombinant PIDD (773-917) fragment fused with a basic 11-amino acid peptide derived from the HIV-Tat protein which facilitates uptake of the protein into mammalian cells with high efficiency.  When PIDD (773-917)-TAT was added to the IEC6 cells, the protein was efficiently delivered into the cells within an hour.  Furthermore, we observed that ionizing radiation-induced activation of caspase-2 and caspase-9 was inhibited when PIDD (773-917)-TAT was added to the IEC6 cells.  These results suggest that PIDD (773-917)-TAT could protect gastrointestinal cells from ionizing radiation-induced cell death., 第32回日本分子生物学会年会},
 title = {第32回日本分子生物学会年会},
 year = {2009}
}