Hypoxia upregulates the histone demethylase JMJD1A via HIF-1

The histone demethylase Jumonji domain containing 1A (JMJD1A) demethylates H3K9 residues and thereby transactivates distinct target genes. Investigating the effect of hypoxia on JMJD1A expression, we found increased JMJD1A mRNA in different organs of rats exposed to normobaric hypoxia (8% O 2). Comp...

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Published inBiochemical and biophysical research communications Vol. 372; no. 4; pp. 892 - 897
Main Authors Wellmann, Sven, Bettkober, Maxi, Zelmer, Andrea, Seeger, Karl, Faigle, Marion, Eltzschig, Holger K., Bührer, Christoph
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 08.08.2008
Subjects
Anaerobiosis - genetics
Animals
Binding Sites
Cell Line
Fetus - metabolism
Gene Expression Regulation
HIF-1
Histone demethylase
Humans
Hypoxia
Hypoxia-Inducible Factor 1 - metabolism
JHDM2A
JMJD1A
Jumonji domain containing 1A
Jumonji Domain-Containing Histone Demethylases
Methylation
Oxidoreductases, N-Demethylating - genetics
Oxidoreductases, N-Demethylating - metabolism
Oxygen - metabolism
Promoter
Promoter Regions, Genetic
Rats
RNA, Messenger - metabolism
Tissue Distribution
Up-Regulation
Jumonji domain containing 1A
Promoter
HIF-1
Histone demethylase
Hypoxia
JMJD1A
JHDM2A
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Summary:The histone demethylase Jumonji domain containing 1A (JMJD1A) demethylates H3K9 residues and thereby transactivates distinct target genes. Investigating the effect of hypoxia on JMJD1A expression, we found increased JMJD1A mRNA in different organs of rats exposed to normobaric hypoxia (8% O 2). Compared to adult samples, JMJD1A was increased in most tissues of human fetuses in whom oxygen supply is low compared to postnatal levels. Upregulation of JMJD1A mRNA and protein in cultured human cells exposed to hypoxia or iron scavengers in vitro was abrogated when hypoxia-inducible factor-1 (HIF-1) signaling was blocked by siRNAs. A single pivotal hypoxia responsive element (HRE) in the promoter of the human JMJD1A gene was identified that mediates JMJD1A upregulation by hypoxia, iron scavengers, and HIF-1. These findings demonstrate that JMJD1A can be stimulated by hypoxia both in vitro and in vivo involving binding of HIF-1 to a specific HRE in the JMJD1A promoter.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2008.05.150