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ORGANELLE MARKERS - Endoplasmic Reticulum - Membrane

 

Heme oxygenase-1

 

Heme oxygenase-1 (HO-1) or HSP32 is the inducible isoform of heme oxygenase which catalyzes the NADPH, O2 and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, iron and biliverdin that is immediately reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator; biliverdin and its product bilirubin are potent antioxidants; .free. iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferrin receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5.- or 3.-UTRs of the mRNAs. To date, three heme oxygenase isoforms HO-1, HO-2 and HO-3 have been identified. HO-1, also known as Hsp32, a major heat shock/stress response protein, is ubiquitous and its mRNA as well as its activity can be increased several-fold by heme, other metalloporphyrins, transition metals and stimuli that induce cellular stress. The 5.-untranslated region (UTR) of HO-1 has several consensus regulatory elements which include sites for activator protein 1 (AP-1), metal responsive element (MRE), oncogene c-myc/max heterodimer binding site (Myc/Max), antioxidant response element (ARE) and GC box binding (Sp1). HO-1 expression has been shown to increase in benign postatic hyperplasia (BPH) and malignant prostate tissue suggesting a role for this stress protein in the pathogenesis of BPH and prostate cancer. There is recent data which indicates the ability of peroxynitrite (ONOO-) to modulate the expression of HO-1 and suggest that the heme oxygenase pathway contributes to protection against the cytotoxic action of ONOO- which is a potent oxidizing agent generated by the interaction of nitric oxide (NO) and the superoxide anion. ONOO- rapidly decomposes to a highly reactive hydroxyl radical and nitrogen dioxide, both of which cause oxidative damage.

 

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