title: Heme oxygenase-1 comes back to endoplasmic reticulum.
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.
authors.affiliation: School of Biological Sciences, Ulsan University, Republic of Korea.
authors.forename: Hong Pyo
authors.initials: HP
authors.lastname: Kim
authors.forename: Hyun-Ock
authors.initials: HO
authors.lastname: Pae
authors.forename: Sung Hun
authors.initials: SH
authors.lastname: Back
authors.forename: Su Wol
authors.initials: SW
authors.lastname: Chung
authors.forename: Je Moon
authors.initials: JM
authors.lastname: Woo
authors.forename: Yong
authors.initials: Y
authors.lastname: Son
authors.forename: Hun-Taeg
authors.initials: HT
authors.lastname: Chung
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D051547:Heme Oxygenase-1 / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051379:Mice; D015388:Organelles / Q000201:enzymology; D013312:Stress, Physiological; D056811:Unfolded Protein Response
chemical_list: D051547:Heme Oxygenase-1