heme oxygenase-1

ヘムオキシゲナーゼ1、ヘムオキシゲナーゼ-1

WordNet

1. utter `hem or `ahem
2. the edge of a piece of cloth; especially the finished edge that has been doubled under and stitched down; "the hem of her dress was stained"; "let down the hem"; "he stitched weights into the curtains hem"; "it seeped along the hem of his jacket"
3. the utterance of a sound similar to clearing the throat; intended to get attention, express hesitancy, fill a pause, hide embarrassment, warn a friend, etc. (同)ahem
4. fold over and sew together to provide with a hem; "hem my skirt"
5. the 5th letter of the Hebrew alphabet
6. a complex red organic pigment containing iron and other atoms to which oxygen binds (同)haem, hematin, haemitin, protoheme
7. an oxidoreductase that catalyzes the incorporation of molecular oxygen

PrepTutorEJDIC

1. (折り返して縫った衣類や布の)へり,縁 / (一般に)へり,縁 / 〈布・着物〉‘の'へりを折り返して縫う;…‘の'縁どりをする
2. へん!えへん!(注意・疑い・ちゅうちょ・当惑などを表するための発声) / へん(えへん)と言う,せき払いをする
3. 彼は,彼が / 《指す人の性別が分からないか,または分かる必要のない場合に》その人,あの人,自分 / 《he who(that)の形で》《文》…するものはだれでも / (動物の)おす(雄)
4. 鬼ごっこ(tag,tick,tig)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/08/01 01:44:51」(JST)

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heme oxygenase
Identifiers
EC number	1.14.99.3
CAS number	9059-22-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

Heme oxygenase
crystal structures of ferrous and ferrous-no forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
Identifiers
Symbol	Heme_oxygenase
Pfam	PF01126
Pfam clan	CL0230
InterPro	IPR016053
PROSITE	PDOC00512
SCOP	1qq8
SUPERFAMILY	1qq8
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, ferrous iron, and carbon monoxide. There is limited evidence that levels of heme oxygenase are positive predictors of metabolic disease, insulin resistance, and metaflammation.

Reaction

Heme oxygenase cleaves the heme ring at the alpha-methene bridge to form either biliverdin or, if the heme is still attached to a globin, verdoglobin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase.

The reaction occurs as follows:

Heme b + 3O₂ + 3½NADPH + 3½H⁺ → biliverdin + Fe²⁺ + CO + 3½NADP⁺ + 3H₂O

Heme b  Biliverdin

This reaction can occur in virtually every cell; the classic example is the formation of a bruise, which goes through different colors as it gradually heals: red heme to green biliverdin to yellow bilirubin. Under normal physiological conditions, the activity of heme oxygenase is highest in the spleen, where old erythrocytes are sequestrated and destroyed. In terms of molecular mechanisms, the enzyme facilitates the intramolecular hydroxylation of one meso carbon centre in the heme.

Isoforms

Three isoforms of heme oxygenase are known. Heme oxygenase 1 (HO-1) is an inducible isoform in response to stress such as oxidative stress, hypoxia, heavy metals, cytokines, etc. Heme oxygenase 2 (HO-2) is a constitutive isoform that is expressed under homeostatic conditions. Both HO-1 and HO-2 are ubiquitously expressed and catalytically active.

A third heme oxygenase (HO-3) is not catalytically active, but is thought to work in oxygen sensing.

Roles in physiology

Heme oxygenase expression is induced by oxidative stress, and in animal models increasing this expression seems to be protective. Carbon monoxide released from heme oxygenase reactions can influence vascular tone independently or influence the function of nitric oxide synthase. Carbon monoxide released from the reaction of free heme in the bloodstream of someone with the sickle-cell trait is believed to lessen the effects of cerebral malaria.

References

External links

• Heme Oxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
• EC 1.14.99.3

UpToDate Contents

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• 1. 初期肺移植片機能不全 primary lung graft dysfunction
• 2. 酸素毒性 oxygen toxicity
• 3. ビリルビン代謝 bilirubin metabolism
• 4. ポルフィリン症：概要 porphyrias an overview
• 5. 急性間欠性ポルフィリン症のマネージメントおよび予後 management and prognosis of acute intermittent porphyria

English Journal

• Styrene-maleic acid-copolymer conjugated zinc protoporphyrin as a candidate drug for tumor-targeted therapy and imaging.

• Fang J1,2, Tsukigawa K1,2, Liao L1,3, Yin H1, Eguchi K2, Maeda H1.
• Journal of drug targeting.J Drug Target.2016 Jun;24(5):399-407. doi: 10.3109/1061186X.2015.1077851. Epub 2015 Aug 24.
• Previous studies indicated the potential of zinc protoporphyrin (ZnPP) as an antitumor agent targeting to the tumor survival factor heme oxygenase-1, and/or for photodynamic therapy (PDT). In this study, to achieve tumor-targeted delivery, styrene-maleic acid-copolymer conjugated ZnPP (SMA-ZnPP) was
• PMID 26302870

• Protective effects of monomethyl fumarate at the inflamed blood-brain barrier.

• Lim JL1, van der Pol SM2, Di Dio F3, van Het Hof B4, Kooij G5, de Vries HE6, van Horssen J7.
• Microvascular research.Microvasc Res.2016 May;105:61-9. doi: 10.1016/j.mvr.2015.12.003. Epub 2015 Dec 8.
• BACKGROUND: Reactive oxygen species play a key role in the pathogenesis of multiple sclerosis as they induce blood-brain barrier disruption and enhance transendothelial leukocyte migration. Thus, therapeutic compounds with antioxidant and anti-inflammatory potential could have clinical value in mult
• PMID 26679389

• Targeting of heme oxygenase-1 as a novel immune regulator of neuroblastoma.

• Fest S1,2, Soldati R1,3, Christiansen NM2, Zenclussen ML3, Kilz J1,3, Berger E1,3, Starke S2, Lode HN4, Engel C5, Zenclussen AC3, Christiansen H2.
• International journal of cancer.Int J Cancer.2016 Apr 15;138(8):2030-42. doi: 10.1002/ijc.29933. Epub 2015 Dec 12.
• Heme oxygenase (HO)-1 catalyzes the degradation of cytotoxic heme into biliverdin and blocks antitumor immune responses, thus protecting cancer against host defense. Whether this scenario also applies to neuroblastoma (NB), the most common extracranial solid childhood tumor, is not known. Here, we d
• PMID 26595750

Japanese Journal

• Protection of Cultured Cortical Neurons by Luteolin against Oxidative Damage through Inhibition of Apoptosis and Induction of Heme Oxygenase-1

• Ｂｉｏｌｏｇｉｃａｌ　＆　Ｐｈａｒｍａｃｅｕｔｉｃａｌ　Ｂｕｌｌｅｔｉｎ 40(3), 256-265, 2017
• NAID 130005398472

• Protective effects of tyrosol against LPS-induced acute lung injury via inhibiting NF-κB and AP-1 activation and activating the HO-1/Nrf2 Pathways

• Ｂｉｏｌｏｇｉｃａｌ　＆　Ｐｈａｒｍａｃｅｕｔｉｃａｌ　Ｂｕｌｌｅｔｉｎ, 2017
• NAID 130005317148

• Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers

• Ｂｉｏｌｏｇｉｃａｌ　＆　Ｐｈａｒｍａｃｅｕｔｉｃａｌ　Ｂｕｌｌｅｔｉｎ 40(2), 128-134, 2017
• NAID 130005308413

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「hem」

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