{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zito E"],"funding":["NIDDK NIH HHS","NIEHS NIH HHS","Medical Research Council","Wellcome Trust"],"pagination":["821-32"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2845084"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["188(6)"],"pubmed_abstract":["Mammals have two genes encoding homologues of the endoplasmic reticulum (ER) disulfide oxidase ERO1 (ER oxidoreductin 1). ERO1-beta is greatly enriched in the endocrine pancreas. We report in this study that homozygosity for a disrupting allele of Ero1lb selectively compromises oxidative folding of proinsulin and promotes glucose intolerance in mutant mice. Surprisingly, concomitant disruption of Ero1l, encoding the other ERO1 isoform, ERO1-alpha, does not exacerbate the ERO1-beta deficiency phenotype. Although immunoglobulin-producing cells normally express both isoforms of ERO1, disulfide bond formation and immunoglobulin secretion proceed at nearly normal pace in the double mutant. Moreover, although the more reducing environment of their ER protects cultured ERO1-beta knockdown Min6 ce"],"journal":["The Journal of cell biology"],"pubmed_title":["ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis."],"pmcid":["PMC2845084"],"funding_grant_id":["R01 ES008681","DK47119","ES08681","DK075311","G0600717B","R01 DK075311","R37 DK047119","084812","R01 DK047119"],"pubmed_authors":["Ron D","Blais J","Harding HP","Chin KT","Zito E"],"additional_accession":[]},"is_claimable":false,"name":"ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis.","description":"Mammals have two genes encoding homologues of the endoplasmic reticulum (ER) disulfide oxidase ERO1 (ER oxidoreductin 1). ERO1-beta is greatly enriched in the endocrine pancreas. We report in this study that homozygosity for a disrupting allele of Ero1lb selectively compromises oxidative folding of proinsulin and promotes glucose intolerance in mutant mice. Surprisingly, concomitant disruption of Ero1l, encoding the other ERO1 isoform, ERO1-alpha, does not exacerbate the ERO1-beta deficiency phenotype. Although immunoglobulin-producing cells normally express both isoforms of ERO1, disulfide bond formation and immunoglobulin secretion proceed at nearly normal pace in the double mutant. Moreover, although the more reducing environment of their ER protects cultured ERO1-beta knockdown Min6 ce","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Mar","modification":"2025-04-25T17:12:35.395Z","creation":"2019-03-27T00:29:40Z"},"accession":"S-EPMC2845084","cross_references":{"pubmed":["20308425"],"doi":["10.1083/jcb.200911086"]}}