Pan-genomic binding of hypoxia-inducible transcription factors
-
Johannes Schödel
,
David Robert Mole
Abstract
Hypoxia-inducible transcription factors (HIFs) mediate the cellular response to hypoxia. HIF-DNA binding triggers a transcriptional program that acts to both restore oxygen homeostasis and adapt cells to low oxygen availability. In this context, HIF is centrally involved in many physiologic and pathophysiological processes such as development, high altitude adaptation, ischemic disease, inflammation, and cancer. The recent development of chromatin immunoprecipitation coupled to genome-wide DNA sequence analysis allows the position and extent of HIF binding to DNA to be characterized across the entire genome and correlated with genetic, epigenetic, and transcriptional analyses. This review summarizes recent pan-genomic analyses of HIF binding and HIF-dependent transcriptional regulation.
©2013 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: sensing hypoxia in the cell and the organism
- Highlight: Sensing Hypoxia in the Cell and the Organism
- Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles
- The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3
- Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade
- Hypoxia, the HIF pathway and neutrophilic inflammatory responses
- Hydroxylase-dependent regulation of the NF-κB pathway
- Role of hypoxia inducible factor-1α for interferon synthesis in mouse dendritic cells
- Pan-genomic binding of hypoxia-inducible transcription factors
- HIF mediated and DNA damage independent histone H2AX phosphorylation in chronic hypoxia
- Noninvasive assessment of hypoxia with 3-[18F]-fluoro-1-(2-nitro-1-imidazolyl)-2-propanol ([18F]-FMISO): a PET study in two experimental models of human glioma
- Research Articles/Short Communications
- Protein Structure and Function
- Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii
- Proteolysis
- Combination of quercetin and tannic acid in inhibiting 26S proteasome affects S5a and 20S expression, and accumulation of ubiquitin resulted in apoptosis in cancer chemoprevention
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: sensing hypoxia in the cell and the organism
- Highlight: Sensing Hypoxia in the Cell and the Organism
- Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles
- The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3
- Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade
- Hypoxia, the HIF pathway and neutrophilic inflammatory responses
- Hydroxylase-dependent regulation of the NF-κB pathway
- Role of hypoxia inducible factor-1α for interferon synthesis in mouse dendritic cells
- Pan-genomic binding of hypoxia-inducible transcription factors
- HIF mediated and DNA damage independent histone H2AX phosphorylation in chronic hypoxia
- Noninvasive assessment of hypoxia with 3-[18F]-fluoro-1-(2-nitro-1-imidazolyl)-2-propanol ([18F]-FMISO): a PET study in two experimental models of human glioma
- Research Articles/Short Communications
- Protein Structure and Function
- Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii
- Proteolysis
- Combination of quercetin and tannic acid in inhibiting 26S proteasome affects S5a and 20S expression, and accumulation of ubiquitin resulted in apoptosis in cancer chemoprevention
