Hypoxia, the HIF pathway and neutrophilic inflammatory responses
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A.A. Roger Thompson
Abstract
Many inflammatory diseases are characterised by persistent and inappropriate neutrophil activation, systemic or localised hypoxia, and bacterial colonisation. Hypoxia represents an important regulator of inflammatory responses because it inhibits neutrophil apoptosis, a process central to the timely resolution of inflammation. Progress in understanding how cells respond to hypoxia has led to the identification of hypoxia-inducible transcription factors (HIFs) and their hydroxylation by the prolyl hydroxylase enzymes. There is now a significant body of data to support a critical role for this HIF pathway in regulating neutrophil function. Moreover, manipulations of specific components of this pathway have very divergent effects on myeloid cell function. In this review, we will discuss the role individual members of the HIF pathway play in regulating key neutrophil functions and the implications this has for the development of effective therapeutic strategies that selectively target inappropriate neutrophil persistence while maintaining a fully competent immune response.
©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
