Ontology highlight
ABSTRACT:
SUBMITTER: Gottlieb Y
PROVIDER: S-EPMC3487549 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Gottlieb Yehonatan Y Truman Marianna M Cohen Lyora A LA Leichtmann-Bardoogo Yael Y Meyron-Holtz Esther G EG
Haematologica 20120314 10
Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin. Heme is a hydrophobic co-factor in many proteins, including hemoglobin. Free heme is highly cytotoxic and, therefore, both heme synthesis and breakdown are tightly regulated. During turnover of heme proteins, heme is released in the phago-lysosomal compartment or the cytosol. The subcellular location of the heme-oxygenase 1 active site has not been clarified. Using constr ...[more]