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- W2899680415 abstract "Abstract Cyclosporine, a widely used immunosuppressant in organ transplantation and in treatment of various autoimmune diseases, activates the unfolded protein response (UPR), an ER stress coping response. In this study we discovered a new and unanticipated cyclosporine-dependent signaling pathway, with cyclosporine triggering direct activation of the UPR. COX-2 binds to and activates IRE1α, leading to IRE1α splicing of XBP1 mRNA. Molecular interaction and modeling analyses identified a novel interaction site for cyclosporine with COX-2 which caused enhancement of COX-2 enzymatic activity required for activation of the IRE1α branch of the UPR. Cyclosporine-dependent activation of COX-2 and IRE1α in mice indicated that cyclosporine-COX-2-IRE1α signaling pathway was functional in vivo . These findings identify COX-2 as a new IRE1α binding partner and regulator of the IRE1α branch of the UPR pathway, and establishes the mechanism underlying cytotoxicity associated with chronic cyclosporine exposure." @default.
- W2899680415 created "2018-11-16" @default.
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- W2899680415 date "2018-11-12" @default.
- W2899680415 modified "2023-10-17" @default.
- W2899680415 title "Cyclosporine A binding to COX-2 reveals a novel signaling pathway that activates the IRE1α unfolded protein response sensor" @default.
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- W2899680415 doi "https://doi.org/10.1038/s41598-018-34891-w" @default.
- W2899680415 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6232179" @default.
- W2899680415 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30420769" @default.
- W2899680415 hasPublicationYear "2018" @default.
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