Heme oxygenase-1 comes back to endoplasmic reticulum

Biochem Biophys Res Commun. 2011 Jan 7;404(1):1-5. doi: 10.1016/j.bbrc.2010.11.067. Epub 2010 Nov 19.


Originally identified as a rate-limiting enzyme for heme catabolism, heme oxygenase-1 (HO-1) has expanded its roles in anti-inflammation, anti-apoptosis and anti-proliferation for the last decade. Regulation of protein activity by location is well appreciated. Even though multiple compartmentalization of HO-1 has been documented, the functional implication of this enzyme at these subcellular organelles is only partially elucidated. In this review we discuss the endoplasmic reticulum (ER)-residing HO-1 and its cytoprotective activity against ER stress.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Endoplasmic Reticulum / enzymology*
  • Heme Oxygenase-1 / genetics
  • Heme Oxygenase-1 / metabolism*
  • Humans
  • Mice
  • Organelles / enzymology
  • Stress, Physiological*
  • Unfolded Protein Response


  • Heme Oxygenase-1