Hème oxygénase 1

HMOX1
Structures disponibles
PDB	Recherche d'orthologue: PDBe RCSB
Identifiants PDB
	1N3U, 1N45, 1NI6, 1OYK, 1OYL, 1OZE, 1OZL, 1OZR, 1OZW, 1S13, 1S8C, 1T5P, 1TWN, 1TWR, 1XJZ, 1XK0, 1XK1, 1XK2, 1XK3, 3CZY, 3HOK, 3K4F, 3TGM, 4WD4, 5BTQ
Identifiants
Aliases	HMOX1
IDs externes	OMIM: 141250 MGI: 96163 HomoloGene: 31075 GeneCards: HMOX1
Position du gène (Homme)
Chr.	Chromosome 22 humain
Fin	35,394,214 bp
Position du gène (Souris)
Chr.	Chromosome 8 (souris)
Fin	75,827,217 bp
Expression génétique
	Fortement exprimé dans
	rate; ; monocyte; ; îlot de Langerhans; ; vésicule biliaire; ; upper lobe of left lung; ; os spongieux; ; duodénum; ; right lobe of liver; ; left adrenal gland; ; skin of abdomen;
	Fortement exprimé dans
	rate; ; cristallin; ; lèvre; ; œsophage; ; placenta; ; calvaria; ; Vésicule vitelline; ; glande surrénale; ; Cortex entorhinal; ; proximal tubule;
	Plus de données d'expression de référence
	Plus de données d'expression de référence
Gene Ontology
Fonction moléculaire	phospholipase D activity; protein homodimerization activity; heme oxygenase (decyclizing) activity; liaison ion métal; signal transducer activity; heme binding; liaison protéique; liaison enzymatique; activité d'oxydoréductase;
Composant cellulaire	cytosol; membrane du réticulum endoplasmique; membrane; intracellular membrane-bounded organelle; nucléole; réticulum endoplasmique; Cavéole; perinuclear region of cytoplasm; noyau; milieu extracellulaire;
Processus biologique	negative regulation of neuron apoptotic process; apoptose; cellular iron ion homeostasis; negative regulation of smooth muscle cell proliferation; cellular response to heat; intracellular signal transduction; negative regulation of mast cell cytokine production; response to hypoxia; excrétion; low-density lipoprotein particle clearance; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; small GTPase mediated signal transduction; negative regulation of DNA binding; response to nicotine; iron ion homeostasis; mort cellulaire; heme oxidation; negative regulation of mast cell degranulation; cellular response to cadmium ion; regulation of angiogenesis; negative regulation of muscle cell apoptotic process; response to oxidative stress; negative regulation of DNA-binding transcription factor activity; cellular response to nutrient; positive regulation of angiogenesis; réaction à l'œstrogène; wound healing involved in inflammatory response; regulation of blood pressure; heme catabolic process; erythrocyte homeostasis; regulation of DNA-binding transcription factor activity; cellular response to arsenic-containing substance; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; angiogenèse; intrinsic apoptotic signaling pathway in response to DNA damage; endothelial cell proliferation; positive regulation of I-kappaB kinase/NF-kappaB signaling; smooth muscle hyperplasia; protein homooligomerization; negative regulation of leukocyte migration; cellular response to hypoxia; response to hydrogen peroxide; negative regulation of cell population proliferation; heme metabolic process; positive regulation of smooth muscle cell proliferation; regulation of transcription from RNA polymerase II promoter in response to iron; positive regulation of apoptotic process; cellular response to cisplatin; positive regulation of macroautophagy; negative regulation of vascular associated smooth muscle cell proliferation; negative regulation of epithelial cell apoptotic process; régénération du foie; negative regulation of macroautophagy;
	Sources:Amigo / QuickGO
Orthologues
	3162
	15368
	ENSG00000100292
	ENSMUSG00000005413
	P09601
	P14901
	NM_002133
	NM_010442
	NP_002124
	NP_034572
	Wikidata
Voir/Editer Humain	Voir/Editer Souris

L'hème oxygénase 1 est l'une des trois isoformes de l'hème oxygénase. Son gène est le HMOX1 situé sur le chromosome 22 humain.

Rôles[modifier | modifier le code]

Elle permet le catabolisme de l'hème en biliverdine, monoxyde de carbone et ion fer^[5].

Elle a un effet protecteur sur divers organes contre différents types de stress : foie^[6], rein^[7], cœur^[8], rétine^[9] ou cerveau^[10]. Il inhibe l'activité pro-inflammatoire des monocytes, jouant ainsi sur la fonction endothéliale des patients hypertendus^[11].

un déficit congénital en hème oxygénase 1 provoque un syndrome comportant une hémolyse, une absence de rate, une insuffisance rénale^[12]. Il peut être responsable d'une fausse-couche^[13].

Notes et références[modifier | modifier le code]

↑ ^{a b et c} GRCh38: Ensembl release 89: ENSG00000100292 - Ensembl, May 2017
↑ ^{a b et c} GRCm38: Ensembl release 89: ENSMUSG00000005413 - Ensembl, May 2017
↑ « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ Wegiel B, Nemeth Z, Correa-Costa M, Bulmer AC, Otterbein LE, Heme oxygenase-1: a metabolic nike, Antioxid Redox Signal, 2014;20:1709–1722
↑ Zuckerbraun BS, Billiar TR, Otterbein SL, Kim PK, Liu F, Choi AM, Bach FH, Otterbein LE, Carbon monoxide protects against liver failure through nitric oxide-induced heme oxygenase 1, J Exp Med, 2003;198:1707–1716
↑ Tayem Y, Green CJ, Motterlini R, Foresti R, Isothiocyanate-cysteine conjugates protect renal tissue against cisplatin-induced apoptosis via induction of heme oxygenase-1, Pharmacol Res, 2014;81:1–9
↑ Clark JE, Foresti R, Sarathchandra P, Kaur H, Green CJ, Motterlini R, Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardial dysfunction, Am J Physiol Heart Circ Physiol, 2000;278:H643–H651
↑ Sun MH, Pang JH, Chen SL et al. Retinal protection from acute glaucoma-induced ischemia-reperfusion injury through pharmacologic induction of heme oxygenase-1, Invest Ophthalmol Vis Sci, 2010;51:4798–4808
↑ Zhang F, Wang S, Zhang M et al. Pharmacological induction of heme oxygenase-1 by a triterpenoid protects neurons against ischemic injury, Stroke, 2012;43:1390–1397.
↑ Wenzel P, Rossmann H, Müller C et al. Heme oxygenase-1 suppresses a pro-inflammatory phenotype in monocytes and determines endothelial function and arterial hypertension in mice and humans, Eur Heart J, 2015;36:3437-3446
↑ Radhakrishnan N, Yadav SP, Sachdeva A et al. Human heme oxygenase-1 deficiency presenting with hemolysis, nephritis, and asplenia, J Pediatr Hematol Oncol, 2011;33:74–78
↑ Schumacher A, Zenclussen AC, Effects of heme oxygenase-1 on innate and adaptive immune responses promoting pregnancy success and allograft tolerance, Front Pharmacol, 2014;5:288

[refGRCh38Ensembl-1] {a b et c} GRCh38: Ensembl release 89: ENSG00000100292 - Ensembl, May 2017

[refGRCm38Ensembl-2] {a b et c} GRCm38: Ensembl release 89: ENSMUSG00000005413 - Ensembl, May 2017

[3] « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[4] « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[Wegiel_2014-5] Wegiel B, Nemeth Z, Correa-Costa M, Bulmer AC, Otterbein LE, Heme oxygenase-1: a metabolic nike, Antioxid Redox Signal, 2014;20:1709–1722

[Zuckerbraun_2003-6] Zuckerbraun BS, Billiar TR, Otterbein SL, Kim PK, Liu F, Choi AM, Bach FH, Otterbein LE, Carbon monoxide protects against liver failure through nitric oxide-induced heme oxygenase 1, J Exp Med, 2003;198:1707–1716

[Tayem_2014-7] Tayem Y, Green CJ, Motterlini R, Foresti R, Isothiocyanate-cysteine conjugates protect renal tissue against cisplatin-induced apoptosis via induction of heme oxygenase-1, Pharmacol Res, 2014;81:1–9

[Clark_2000-8] Clark JE, Foresti R, Sarathchandra P, Kaur H, Green CJ, Motterlini R, Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardial dysfunction, Am J Physiol Heart Circ Physiol, 2000;278:H643–H651

[Sun_2010-9] Sun MH, Pang JH, Chen SL et al. Retinal protection from acute glaucoma-induced ischemia-reperfusion injury through pharmacologic induction of heme oxygenase-1, Invest Ophthalmol Vis Sci, 2010;51:4798–4808

[Zhang_2012-10] Zhang F, Wang S, Zhang M et al. Pharmacological induction of heme oxygenase-1 by a triterpenoid protects neurons against ischemic injury, Stroke, 2012;43:1390–1397.

[Wenzel_2015-11] Wenzel P, Rossmann H, Müller C et al. Heme oxygenase-1 suppresses a pro-inflammatory phenotype in monocytes and determines endothelial function and arterial hypertension in mice and humans, Eur Heart J, 2015;36:3437-3446

[Radhakrishnan_2011-12] Radhakrishnan N, Yadav SP, Sachdeva A et al. Human heme oxygenase-1 deficiency presenting with hemolysis, nephritis, and asplenia, J Pediatr Hematol Oncol, 2011;33:74–78

[Schumacher_2014-13] Schumacher A, Zenclussen AC, Effects of heme oxygenase-1 on innate and adaptive immune responses promoting pregnancy success and allograft tolerance, Front Pharmacol, 2014;5:288

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