| Stress granules contribute to α-globin homeostasis in differentiating erythroid cells. | |
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MedLine Citation:
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PMID: 22452989 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Hemoglobin is the major biosynthetic product of developing erythroid cells. Assembly of hemoglobin requires the balanced production of globin proteins and the oxygen-carrying heme moiety. The heme-regulated inhibitor kinase (HRI) participates in this process by phosphorylating eIF2α and inhibiting the translation of globin proteins when levels of free heme are limiting. HRI is also activated in erythroid cells subjected to oxidative stress. Phospho-eIF2α-mediated translational repression induces the assembly of stress granules (SG), cytoplasmic foci that harbor untranslated mRNAs and promote the survival of cells subjected to adverse environmental conditions. We have found that differentiating erythroid, but not myelomonocytic or megakaryocytic, murine and human progenitor cells assemble SGs, in vitro and in vivo. Targeted knockdown of HRI or G3BP, a protein required for SG assembly, inhibits spontaneous and arsenite-induced assembly of SGs in erythroid progenitor cells. This is accompanied by reduced α-globin production and increased apoptosis suggesting that G3BP+ SGs facilitate the survival of developing erythroid cells. |
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Authors:
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Laura Ghisolfi; Shilpee Dutt; Marie E McConkey; Benjamin L Ebert; Paul Anderson |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2012-03-20 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 420 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2012 Apr |
Date Detail:
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Created Date: 2012-04-23 Completed Date: 2012-06-22 Revised Date: 2013-05-16 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 768-74 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Elsevier Inc. All rights reserved. |
Affiliation:
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Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, One Jimmy Fund Way, Smith 652, Boston, MA 02115, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis Carrier Proteins / genetics, metabolism Cells, Cultured Cytoplasmic Granules / metabolism, physiology* Erythroid Cells / cytology*, metabolism Erythropoiesis* Homeostasis* Humans Mice Mice, Inbred BALB C Transcription, Genetic alpha-Globins / biosynthesis*, genetics eIF-2 Kinase / genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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P01 AI065858-01A1/AI/NIAID NIH HHS; R01 HL082945/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/G3BP protein, human; 0/alpha-Globins; EC 2.7.11.1/eIF-2 Kinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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