Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2013 Nov 12;110(46):18351-2.
doi: 10.1073/pnas.1318345110. Epub 2013 Nov 1.

Hypoxia and inflammation are two sides of the same coin

Karsten Bartels  1 , Almut Grenz, Holger K Eltzschig
Affiliations
Comment

Hypoxia and inflammation are two sides of the same coin

Karsten Bartels et al. Proc Natl Acad Sci U S A. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Schematic overview of the molecular interaction between the HIF and the NF-κB pathways. In hypoxic conditions (Left), hypoxia-inducible factor (HIF) α and HIF-β subunits translocate to the nucleus, where they bind as heterodimers to a hypoxia response promoter element (HRE), inducing transcription of numerous genes, including those of nuclear factor κB (NF-κB) and toll-like receptors (TLRs). In normoxia, HIF-α is hydroxylated by prolyl-hydroxylases (PHDs) and factor-inhibiting HIF (FIH), and is thereby targeted for proteasomal degradation (in the case of PHDs) or rendered transcriptionally less active (in the case of FIH; not shown here). In resting cells (Right), NF-κB, a heterodimer consisting of p50 and p65 subunits, is inactive in the cytosol because it is associated with nuclear factor of kappa light polypeptide gene enhancer in B cells alpha (IκBα), a regulatory component of NF-κB. At the time of cellular activation, the beta subunit of the IκB kinase complex (IKKβ) phosphorylates the inhibitor IκBα, which thereby becomes degraded and liberates NF-κB for translocation in the nucleus, where it can activate the transcription of inflammatory genes as well as of HIF (genes involved in tissue protection and homeostasis are not shown). PHDs and FIH regulate NF-κB activation by controlling the activity of IKKβ. From Eltzschig and Carmeliet (2). Reprinted with permission from the Massachusetts Medical Society.
See this image and copyright information in PMC

Comment on

References

    1. Taylor CT. Interdependent roles for hypoxia inducible factor and nuclear factor-kappaB in hypoxic inflammation. J Physiol. 2008;586(Pt 17):4055–4059. - PMC - PubMed
    1. Eltzschig HK, Carmeliet P. Hypoxia and inflammation. N Engl J Med. 2011;364(7):656–665. - PMC - PubMed
    1. Taylor CT, McElwain JC. Ancient atmospheres and the evolution of oxygen sensing via the hypoxia-inducible factor in metazoans. Physiology (Bethesda) 2010;25(5):272–279. - PubMed
    1. Colgan SP, Eltzschig HK. Adenosine and hypoxia-inducible factor signaling in intestinal injury and recovery. Annu Rev Physiol. 2012;74:153–175. - PMC - PubMed
    1. Karhausen J, et al. Epithelial hypoxia-inducible factor-1 is protective in murine experimental colitis. J Clin Invest. 2004;114(8):1098–1106. - PMC - PubMed

Publication types

MeSH terms

LinkOut - more resources