Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family. Note: This description may include information from UniProtKB.
Protein type: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 18.104.22.168; Oxidoreductase
Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; extracellular space; membrane; nucleus; perinuclear region of cytoplasm
Molecular Function: enzyme binding; heme binding; heme oxygenase (decyclizing) activity; protein binding; protein homodimerization activity; signal transducer activity
Biological Process: angiogenesis; cell death; cellular iron ion homeostasis; endothelial cell proliferation; erythrocyte homeostasis; excretion; healing during inflammatory response; heme catabolic process; heme oxidation; iron ion homeostasis; negative regulation of leukocyte migration; negative regulation of smooth muscle cell proliferation; positive regulation of chemokine biosynthetic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of smooth muscle cell proliferation; protein homooligomerization; regulation of angiogenesis; regulation of transcription factor activity; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to hydrogen peroxide; response to nicotine; response to oxidative stress; smooth muscle hyperplasia