HIF-1-dependent induction of Jumonji domain-containing protein (JMJD) 3 under hypoxic conditions
| Autor: | Hookeun Oh, Hyunsung Park, Young-Kwon Park, Ho-Youl Lee, Kang Choi |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Transcriptional Activation
Hypoxia-Inducible Factor 1 Jumonji Domain-Containing Histone Demethylases Aryl hydrocarbon receptor nuclear translocator JMJD3 HIF-1α Response Elements Mice Arnt Species Specificity histone demethylase 3T3-L1 Cells Animals Humans Molecular Biology Cells Cultured biology Base Sequence Activator (genetics) hypoxia Aryl Hydrocarbon Receptor Nuclear Translocator Cell Biology General Medicine Articles Hypoxia-Inducible Factor 1 alpha Subunit Molecular biology Cell Hypoxia Mice Inbred C57BL Adult Stem Cells Histone HIF1A Regulatory sequence biology.protein Demethylase Chromatin immunoprecipitation |
| Zdroj: | Molecules and Cells |
| ISSN: | 0219-1032 |
| Popis: | Jumonji domain-containing proteins (JMJD) catalyze the oxidative demethylation of a methylated lysine residue of histones by using O2, α-ketoglutarate, vitamin C, and Fe(II). Several JMJDs are induced by hypoxic stress to compensate their presumed reduction in catalytic activity under hypoxia. In this study, we showed that an H3K27me3 specific histone demethylase, JMJD3 was induced by hypoxia-inducible factor (HIF)-1α/β under hypoxia and that treatment with Clioquinol, a HIF-1α activator, increased JMJD3 expression even under normoxia. Chromatin immunoprecipitation (ChIP) analyses showed that both HIF-1α and its dimerization partner HIF-1β/Arnt occupied the first intron region of the mouse JMJD3 gene, whereas the HIF-1α/β heterodimer bound to the upstream region of the human JMJD3, indicating that human and mouse JMJD3 have hypoxia-responsive regulatory regions in different locations. This study shows that both mouse and human JMJD3 are induced by HIF-1. |
| Databáze: | OpenAIRE |
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