Heme oxygenase-1 comes back to endoplasmic reticulum

Hong Pyo Kim; Hyun-Ock Pae; Sung Hun Back; Su Wol Chung; Je Moon Woo; Yong Son; Hun-Taeg Chung

doi:10.1016/j.bbrc.2010.11.067

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.

Authors

Hong Pyo Kim¹, Hyun-Ock Pae, Sung Hun Back, Su Wol Chung, Je Moon Woo, Yong Son, Hun-Taeg Chung

Affiliation

¹ School of Biological Sciences, Ulsan University, Republic of Korea.

PMID: 21094129
DOI: 10.1016/j.bbrc.2010.11.067

Abstract

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

Substances

Heme Oxygenase-1