Transcriptional regulation of the AP-1 and Nrf2 target gene sulfiredoxin. Export

@article{citeulike:4260819, abstract = {"Two-cysteine" peroxiredoxins are antioxidant enzymes that exert a cytoprotective effect in many models of oxidative stress. However, under highly oxidizing conditions they can be inactivated through hyperoxidation of their peroxidatic active site cysteine residue. Sulfiredoxin can reverse this hyperoxidation, thus reactivating peroxiredoxins. Here we review recent investigations that have shed further light on sulfiredoxin's role and regulation. Studies have revealed sulfiredoxin to be a dynamically regulated gene whose transcription is induced by a variety of signals and stimuli. Sulfiredoxin expression is regulated by the transcription factor AP-1, which mediates its up-regulation by synaptic activity in neurons, resulting in protection against oxidative stress. Furthermore, sulfiredoxin has been identified as a new member of the family of genes regulated by nuclear factor erythroid 2-related factor (Nrf2) via a conserved A\'{a}\"{e}-acting antioxidant response element (ARE). As such, sulfiredoxin is likely to contribute to the net antioxidative effect of small molecule activators of Nrf2. As discussed here, the proximal AP-1 site of the sulfiredoxin promoter is embedded within the ARE, as is common with Nrf2 target genes. Other recent studies have shown that sulfiredoxin induction via Nrf2 may form an important part of the protective response to oxidative stress in the lung, preventing peroxiredoxin hyperoxidation and, in certain cases, subsequent degradation. We illustrate here that sulfiredoxin can be rapidly induced in vivo by administration of CDDO-TFEA, a synthetic triterpenoid inducer of endogenous Nrf2, which may offer a way of reversing peroxiredoxin hyperoxidation in vivo following chronic or acute oxidative stress.}, author = {Soriano, Francesc X. and Baxter, Paul and Murray, Lyndsay M. and Sporn, Michael B. and Gillingwater, Thomas H. and Hardingham, Giles E.}, citeulike-article-id = {4260819}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s10059-009-0050-y}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19326073}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19326073}, citeulike-linkout-3 = {http://www.springerlink.com/content/x60r1121702w426t}, day = {1}, doi = {10.1007/s10059-009-0050-y}, issn = {0219-1032}, journal = {Molecules and cells}, keywords = {basic-science, lmm\_papers, xrw}, month = {March}, number = {3}, pages = {279--282}, posted-at = {2009-10-19 09:46:32}, priority = {2}, title = {Transcriptional regulation of the AP-1 and Nrf2 target gene sulfiredoxin.}, url = {http://dx.doi.org/10.1007/s10059-009-0050-y}, volume = {27}, year = {2009} }

TY - JOUR ID - citeulike:4260819 L3 - citeulike-article-id:4260819 N2 - "Two-cysteine" peroxiredoxins are antioxidant enzymes that exert a cytoprotective effect in many models of oxidative stress. However, under highly oxidizing conditions they can be inactivated through hyperoxidation of their peroxidatic active site cysteine residue. Sulfiredoxin can reverse this hyperoxidation, thus reactivating peroxiredoxins. Here we review recent investigations that have shed further light on sulfiredoxin's role and regulation. Studies have revealed sulfiredoxin to be a dynamically regulated gene whose transcription is induced by a variety of signals and stimuli. Sulfiredoxin expression is regulated by the transcription factor AP-1, which mediates its up-regulation by synaptic activity in neurons, resulting in protection against oxidative stress. Furthermore, sulfiredoxin has been identified as a new member of the family of genes regulated by nuclear factor erythroid 2-related factor (Nrf2) via a conserved Aáë-acting antioxidant response element (ARE). As such, sulfiredoxin is likely to contribute to the net antioxidative effect of small molecule activators of Nrf2. As discussed here, the proximal AP-1 site of the sulfiredoxin promoter is embedded within the ARE, as is common with Nrf2 target genes. Other recent studies have shown that sulfiredoxin induction via Nrf2 may form an important part of the protective response to oxidative stress in the lung, preventing peroxiredoxin hyperoxidation and, in certain cases, subsequent degradation. We illustrate here that sulfiredoxin can be rapidly induced in vivo by administration of CDDO-TFEA, a synthetic triterpenoid inducer of endogenous Nrf2, which may offer a way of reversing peroxiredoxin hyperoxidation in vivo following chronic or acute oxidative stress. IS - 3 JF - Molecules and cells SN - 0219-1032 EP - 282 TI - Transcriptional regulation of the AP-1 and Nrf2 target gene sulfiredoxin. VL - 27 SP - 279 KW - basic-science KW - lmm_papers KW - xrw AU - Soriano, Francesc AU - Baxter, Paul AU - Murray, Lyndsay AU - Sporn, Michael AU - Gillingwater, Thomas AU - Hardingham, Giles PY - 2009/03/01/ UR - http://dx.doi.org/10.1007/s10059-009-0050-y ER -