{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Konno T"],"funding":["Wellcome Trust"],"pagination":["253-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4621842"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["211(2)"],"pubmed_abstract":["The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1). The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen. We report on a simple kinetic technique to track H2O2 equilibration between cellular compartments, suggesting that the ER is relatively isolated from cytosolic or mitochondrial H2O2 pools. Furthermore, expression of an ER-adapted catalase to degrade lumenal H2O2 attenuated PRDX4-mediated disulfide bond formation in cells lacking ERO1, whereas depletion of H2O2 in the cytosol or mitochondria had no similar effect. ER catalase did not effec"],"journal":["The Journal of cell biology"],"pubmed_title":["ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding."],"pmcid":["PMC4621842"],"funding_grant_id":["100140","084812"],"pubmed_authors":["Konno T","Ron D","Lopes C","Avezov E","Pinho Melo E","Lenzen S","Mehmeti I"],"additional_accession":[]},"is_claimable":false,"name":"ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding.","description":"The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1). The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen. We report on a simple kinetic technique to track H2O2 equilibration between cellular compartments, suggesting that the ER is relatively isolated from cytosolic or mitochondrial H2O2 pools. Furthermore, expression of an ER-adapted catalase to degrade lumenal H2O2 attenuated PRDX4-mediated disulfide bond formation in cells lacking ERO1, whereas depletion of H2O2 in the cytosol or mitochondria had no similar effect. ER catalase did not effec","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2025-04-06T19:45:21.961Z","creation":"2019-03-27T02:00:50Z"},"accession":"S-EPMC4621842","cross_references":{"pubmed":["26504166"],"doi":["10.1083/jcb.201506123"]}}