Title: Oxygen tension modulates β‐globin switching in embryoid bodies
Abstract: The FASEB JournalVolume 13, Issue 2 p. 285-295 Research CommunicationFree to Read Oxygen tension modulates β-globin switching in embryoid bodies SANDRINE BICHET, SANDRINE BICHET Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorROLAND H. WENGER, ROLAND H. WENGER Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorGIERI CAMENISCH, GIERI CAMENISCH Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorANDREAS ROLFS, ANDREAS ROLFS Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorWILHELM EHLEBEN, WILHELM EHLEBEN Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorTORSTEN PORWOL, TORSTEN PORWOL Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorHELMUT ACKER, HELMUT ACKER Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorJOACHIM FANDREY, JOACHIM FANDREY Institute of Physiology, Medical University of Lübeck, 23538 Lübeck, GermanySearch for more papers by this authorCHRISTIAN BAUER, CHRISTIAN BAUER Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorMAX GASSMANN, Corresponding Author MAX GASSMANN [email protected] Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, Switzerland Correspondence: Institute of Physiology, University of Zürich-Irchel, Winterthurerstrasse 190, 8057 Zürich, Switzerland. E-mail: [email protected] for more papers by this author SANDRINE BICHET, SANDRINE BICHET Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorROLAND H. WENGER, ROLAND H. WENGER Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorGIERI CAMENISCH, GIERI CAMENISCH Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorANDREAS ROLFS, ANDREAS ROLFS Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorWILHELM EHLEBEN, WILHELM EHLEBEN Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorTORSTEN PORWOL, TORSTEN PORWOL Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorHELMUT ACKER, HELMUT ACKER Max-Planck-Institute for Molecular Physiology, 44026 Dortmund, GermanySearch for more papers by this authorJOACHIM FANDREY, JOACHIM FANDREY Institute of Physiology, Medical University of Lübeck, 23538 Lübeck, GermanySearch for more papers by this authorCHRISTIAN BAUER, CHRISTIAN BAUER Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, SwitzerlandSearch for more papers by this authorMAX GASSMANN, Corresponding Author MAX GASSMANN [email protected] Institute of Physiology, University of Zürich-Irchel, 8057 Zürich, Switzerland Correspondence: Institute of Physiology, University of Zürich-Irchel, Winterthurerstrasse 190, 8057 Zürich, Switzerland. E-mail: [email protected] for more papers by this author First published: 01 February 1999 https://doi.org/10.1096/fasebj.13.2.285Citations: 6Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat ABSTRACT Little is known about the factors influencing the hemoglobin switch in vertebrates during development. Inasmuch as the mammalian conceptus is exposed to changing oxygen tensions in utero, we examined the effect of different oxygen concentrations on β-globin switching. We used an in vitro model of mouse embryogenesis based on the differentiation of blastocyst-derived embryonic stem cells to embryoid bodies (EBs). Cultivation of EBs at increasing oxygen concentrations (starting at 1% O2) did not influence the temporal expression pattern of embryonic (βH1) globin compared to the normoxic controls (20% O2). In contrast, when compared to normoxically grown EBs, expression of fetal/adult (βmaj) globin in EBs cultured at varying oxygen concentrations was delayed by about 2 days and persisted throughout differentiation. Quantitation of hemoglobin in EBs using a 2,7-diaminofluorene-based colorimetric assay revealed the appearence of hemoglobin in two waves, an early and a late one. This observation was verified by spectrophotometric analysis of hemoglobin within single EBs. These two waves might reflect the switch of erythropoiesis from yolk sac to fetal liver. Reduced oxygenation is known to activate the hypoxia-inducible factor-1 (HIF-1), which in turn specifically induces expression of a variety of genes among them erythropoietin (EPO). Although EBs increased EPO expression upon hypoxic exposure, the altered β-globin appearance was not related to EPO levels as determined in EBs overexpressing EPO. Since mRNA from both mouse HIF-1α isoforms was detected in all EBs tested at different differentiation stages, we propose that HIF-1 modulates β-globin expression during development.—Bichet, S., Wenger, R. H., Camenisch, G., Rolfs, A., Ehleben, W., Porwol, T., Acker, H., Fandrey, J., Bauer, C., Gassmann, M. Oxygen tension modulates β-globin switching in embryoid bodies. FASEB J. 13, 285–295 (1999) Citing Literature Volume13, Issue2February 1999Pages 285-295 RelatedInformation