{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sripathy SP"],"funding":["NCI NIH HHS"],"pagination":["6376-84"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4094353"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(49)"],"pubmed_abstract":["In the presence of ERbeta, trans-hydroxytamoxifen (TOT) protects cells against 17beta-estradiol (E(2))-induced oxidative DNA damage (ODD) and this correlates with increased expression of the antioxidative enzyme quinone reductase (QR). Here, we investigate the molecular mechanism responsible for ERbeta-mediated protection against ODD. We observe constitutive interaction between ERbeta and the novel protein hPMC2. Using a combination of breast epithelial cell lines that are either positive or negative for ERalpha, we demonstrate TOT-dependent recruitment of both ERbeta and hPMC2 to the EpRE (electrophile response element)-regulated antioxidative enzyme QR. We further demonstrate TOT-dependent corecruitment of the coactivators Nrf2, PARP-1 (poly (ADP-ribose) polymerase 1) and topoisomerase I"],"journal":["Oncogene"],"pubmed_title":["hPMC2 is required for recruiting an ERbeta coactivator complex to mediate transcriptional upregulation of NQO1 and protection against oxidative DNA damage by tamoxifen."],"pmcid":["PMC4094353"],"funding_grant_id":["R03 CA130066","CA130066","CA92440","R01 CA092440"],"pubmed_authors":["Gaikwad NW","Chaplin LJ","Montano MM","Rogan EG","Sripathy SP"],"additional_accession":[]},"is_claimable":false,"name":"hPMC2 is required for recruiting an ERbeta coactivator complex to mediate transcriptional upregulation of NQO1 and protection against oxidative DNA damage by tamoxifen.","description":"In the presence of ERbeta, trans-hydroxytamoxifen (TOT) protects cells against 17beta-estradiol (E(2))-induced oxidative DNA damage (ODD) and this correlates with increased expression of the antioxidative enzyme quinone reductase (QR). Here, we investigate the molecular mechanism responsible for ERbeta-mediated protection against ODD. We observe constitutive interaction between ERbeta and the novel protein hPMC2. Using a combination of breast epithelial cell lines that are either positive or negative for ERalpha, we demonstrate TOT-dependent recruitment of both ERbeta and hPMC2 to the EpRE (electrophile response element)-regulated antioxidative enzyme QR. We further demonstrate TOT-dependent corecruitment of the coactivators Nrf2, PARP-1 (poly (ADP-ribose) polymerase 1) and topoisomerase I","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Oct","modification":"2025-04-26T09:14:43.034Z","creation":"2019-03-27T01:31:55Z"},"accession":"S-EPMC4094353","cross_references":{"pubmed":["18663360"],"doi":["10.1038/onc.2008.235"]}}