4.6 Review

Heme oxygenase-1: from biology to therapeutic potential

Journal

TRENDS IN MOLECULAR MEDICINE
Volume 15, Issue 2, Pages 50-58

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.molmed.2008.12.004

Keywords

-

Funding

  1. 'Fundacao para Ciencia e Tecnologia', Portugal [POCTI/BIA-BCM/56829/2004, POCTI/SAU-MNO/56066/2004, POCTI/SAU-MNO/56066/2007]
  2. European Commission's Sixth Framework Programme, Xenome [LSHB-CT-2006-037377]
  3. GEMI fund (Linde Health care)
  4. National Institutes of Health [HL77721, HL58688]
  5. Julie Henry Fund of the Department of Surgery, Beth Israel Deaconess Medical Center, Boston, MA, USA

Ask authors/readers for more resources

Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Over the past few years it has become apparent that these 'arms' of the HO-1 system can act protectively in a variety of experimental models of disease; there is also evidence that HO-1 and bilirubin have protective actions in humans. Here, we present a model for the beneficial actions of the products of heme degradation, and we discuss the potential clinical applications of enhancing the HO-1 system.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available