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- Table of Contents
1 Citations 2 Q&As
Facts about Heme oxygenase 2.
Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in mind where it may function as a neurotransmitter.
Human | |
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Gene Name: | HMOX2 |
Uniprot: | P30519 |
Entrez: | 3163 |
Belongs to: |
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heme oxygenase family |
heme oxygenase (decycling) 2; heme oxygenase 2; HMOX2; HO2; HO-2; HO-2EC 1.14.99.3
Mass (kDA):
36.033 kDA
Human | |
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Location: | 16p13.3 |
Sequence: | 16; NC_000016.10 (4474697..4510347) |
Microsome. Endoplasmic reticulum.
The HMOX2 marker is a gene for heme oxygenase. In this article, we will discuss the best uses of the HMOX2 marker for research. Boster Bio has partnered with Boster scientists to develop a biomarker for heme oxygenase, and we will review the benefits of this partnership for researchers. We will also cover the application process, which is applicable to scientists all over the world.
Heme oxygenase isozymes, such as the heme oxygenase 2, catalyze the oxidation of heme to ferrous iron and carbon monoxide. Biliverdin reductase is a component of the heme oxygenase system. Its catalytic activity produces equimolar amounts of CO and bilirubin, a signal molecule and an antioxidant.
Researchers identified the gene for heme oxygenase-2 in the rat testis. The protein is induced in the brain when CO or hypoxia is present. Inflammatory changes in heme oxygenase-2 are associated with cardiovascular disease. Inflammatory diseases, especially those involving the gastrointestinal tract, it may lead to cardiac or pulmonary complications.
Heme oxygenase enzymes are responsible for the degradation of heme in the body. They cleave the heme ring to produce bilirubin. Heme oxygenase activity is required for normal tissue repair. It can also be a marker of oxidative stress. The HE-2 enzyme, which is found in heme cells, is highly expressed in various types of tumors and is a potential therapeutic target.
Heme oxygenase-2 is a neuroprotective protein that may protect against cerebral ischemia. It is also known to be a potential promotor of tissue damage. It is also a heme oxygenase 2 marker. However, there are many questions about HO-2. The enzyme is responsible for the anti-inflammatory and redox properties of hemoglobin.
Heme oxygenase is a primary antioxidant enzyme involved in reducing inflammation. The enzyme's expression is modulated by various stimuli, including substrate and cellular stress. Studies have also found that HO-1 induction has anti-inflammatory and anti-microbial effects. There are several natural compounds that can induce HO-1 activity without causing cytotoxic effects. Most of these compounds can be found in food, flavoring, and medicinal plants.
HO-2 cleaves heme to produce equimolar amounts of CO, Fe2+, and BV. The enzyme requires NADPH, Cyt P450, and O2 to catalyze the reaction. HO-2 produces CO and BV, which have antiapoptotic properties and regulate vascular tone. BV is metabolized to BV by NAD(P)H, and Fe2+ is sequestered by ferritin.
Heme oxygenase-1 has been shown to be an important regulator of cGMP-induced endothelial function. In addition, HO-2 is involved in carotid body chemoreception. Heme oxygenase-2 protein and mRNA are regulated by glucocorticoids. When HO-2 is overexpressed, glucocorticoids inhibit relaxation of the NANC.
In patients with intracerebral hemorrhage (ICH), Hpx plays an important role in removing hematomas. It also acts as a scavenger system after blood-heme overload. The heme-Hpx complex is endocytosed by cells that express the CD91 receptor. These cells are vascular cells and activated microglia.
Although the functions of HO-2 are not fully understood, evidence suggests that it is involved in the regulation of blood vessel function. While the gene's role as a sensor of oxygen levels may be unclear, it is known to play a crucial role in cerebrovascular health. The gene is located in the brain and is expressed in neurons, arachnoid trabecular cells, and vascular endothelium. In vivo imaging of HO-2-positive mice showed dilation of arterioles.
HMOX2 is a key enzyme involved in heme catabolism and could play an important role in the production of carbon monoxide. It also plays a role in the conversion of biliverdin to bilirubin. The spleen has the highest activity level of this enzyme. Heme oxygenase activity is induced by nonheme substances. It is present as two isozymes, constitutive and inducible. The enzymes belong to the heme oxygenase family.
The HO system is responsible for the degradation of cellular heme to iron, carbon monoxide, and biliverdin. The two isoforms HO-1 and HO-2 share 45% residue identity and fold and catalyze the same reaction. Although the homologous HO-1 isoform has been studied extensively, isonian HO-2 is less well studied.
PMID: 7890772 by Ishikawa K.; Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2.
PMID: 1575508 by McCoubrey W.K. Jr., et al. Human heme oxygenase-2: characterization and expression of a full- length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal.
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