pubmed-article:16537925 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0140145 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0600432 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0015879 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C1332102 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
pubmed-article:16537925 | lifeskim:mentions | umls-concept:C1516960 | lld:lifeskim |
pubmed-article:16537925 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:16537925 | pubmed:dateCreated | 2006-3-15 | lld:pubmed |
pubmed-article:16537925 | pubmed:abstractText | An effective utilization of intracellular iron is a prerequisite for erythroid differentiation and hemoglobinization. Ferritin, consisting of 24 subunits of H and L, plays a crucial role in iron homeostasis. Here, we have found that the H subunit of the ferritin gene is activated at the transcriptional level during hemin-induced differentiation of K562 human erythroleukemic cells. Transfection of various 5' regions of the human ferritin H gene fused to a luciferase reporter into K562 cells demonstrated that hemin activates ferritin H transcription through an antioxidant-responsive element (ARE) that is responsible for induction of a battery of phase II detoxification genes by oxidative stress. Gel retardation and chromatin immunoprecipitation assays demonstrated that hemin induced binding of cJun, JunD, FosB, and Nrf2 b-zip transcription factors to AP1 motifs of the ferritin H ARE, despite no significant change in expression levels or nuclear localization of these transcription factors. A Gal4-luciferase reporter assay did not show activation of these b-zip transcription factors after hemin treatment; however, redox factor 1 (Ref-1), which increases DNA binding of Jun/Fos family members via reduction of a conserved cysteine in their DNA binding domains, showed induced nuclear translocation after hemin treatment in K562 cells. Consistently, Ref-1 enhanced Nrf2 binding to the ARE and ferritin H transcription. Hemin also activated ARE sequences of other phase II genes, such as GSTpi and NQO1. Collectively, these results suggest that hemin activates the transcription of the ferritin H gene during K562 erythroid differentiation by Ref-1-mediated activation of these b-zip transcription factors to the ARE. | lld:pubmed |
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pubmed-article:16537925 | pubmed:language | eng | lld:pubmed |
pubmed-article:16537925 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |