pubmed-article:9002972 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C1257751 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0014822 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0034845 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0378503 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0041904 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0596803 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0597360 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:9002972 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9002972 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9002972 | pubmed:dateCreated | 1997-2-24 | lld:pubmed |
pubmed-article:9002972 | pubmed:abstractText | Erythropoietin (Epo) is the central regulator of red blood cell production and acts primarily by inducing proliferation and differentiation of erythroid progenitor cells. Because a sufficient supply of iron is a prerequisite for erythroid proliferation and hemoglobin synthesis, we have investigated whether Epo can regulate cellular iron metabolism. We present here a novel biologic function of Epo, namely as a potential modulator of cellular iron homeostasis. We show that, in human (K562) and murine erythroleukemic cells (MEL), Epo enhances the binding affinity of iron-regulatory protein (IRP)-1, the central regulator of cellular iron metabolism, to specific RNA stem-loop structures, known as iron-responsive elements (IREs). Activation of IRP-1 by Epo is associated with a marked increase in transferrin receptor (trf-rec) mRNA levels in K562 and MEL, enhanced cell surface expression of trf-recs, and increased uptake of iron into cells. These findings are in agreement with the well-established mechanism whereby high-affinity binding of IRPs to IREs stabilizes trf-rec mRNA by protecting it from degradation by a specific RNase. The effects of Epo on IRE-binding of IRPs were not observed in human myelomonocytic cells (THP-1), which indicates that this response to Epo is not a general mechanism observed in all cells but is likely to be erythroid-specific. Our results provide evidence for a direct functional connection between Epo biology and iron metabolism by which Epo increases iron uptake into erythroid progenitor cells via posttranscriptional induction of trf-rec expression. Our data suggest that sequential administration of Epo and iron might improve the response to Epo therapy in some anemias. | lld:pubmed |
pubmed-article:9002972 | pubmed:language | eng | lld:pubmed |
pubmed-article:9002972 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9002972 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9002972 | pubmed:month | Jan | lld:pubmed |
pubmed-article:9002972 | pubmed:issn | 0006-4971 | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:WeissGG | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:BrockJ HJH | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:GrünewaldKK | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:HoustonTT | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:KastnerSS | lld:pubmed |
pubmed-article:9002972 | pubmed:author | pubmed-author:JöhrerKK | lld:pubmed |
pubmed-article:9002972 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9002972 | pubmed:day | 15 | lld:pubmed |
pubmed-article:9002972 | pubmed:volume | 89 | lld:pubmed |
pubmed-article:9002972 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9002972 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9002972 | pubmed:pagination | 680-7 | lld:pubmed |
pubmed-article:9002972 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:9002972 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9002972 | pubmed:articleTitle | Regulation of cellular iron metabolism by erythropoietin: activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells. | lld:pubmed |
pubmed-article:9002972 | pubmed:affiliation | Department of Internal Medicine, University Hospital, Innsbruck, Austria. | lld:pubmed |
pubmed-article:9002972 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9002972 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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