Hème oxygénase 1

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.

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[1] Locus 22q12.3 Début 35,380,361 bp[1] Fin 35,394,214 bp[1]
Position du gène (Souris) Chr. Chromosome 8 (souris)[2] Locus 8 35.59 cM|8 C1 Début 75,820,249 bp[2] Fin 75,827,217 bp[2]
Expression génétique Bgee Humain Souris (orthologue) Fortement exprimé dans cartilage tissue rate monocyte granulocyte îlot de Langerhans left ovary mucosa of transverse colon skin of leg vésicule biliaire right ovary Fortement exprimé dans stroma of bone marrow rate tibiofemoral joint cristallin granulocyte lèvre œsophage placenta calvaria Vésicule vitelline Plus de données d'expression de référence BioGPS 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 Espèces Homme Souris Entrez 3162 15368 Ensembl ENSG00000100292 ENSMUSG00000005413 UniProt P09601 P14901 RefSeq (mRNA) NM_002133 NM_010442 RefSeq (protéine) NP_002124 NP_034572 Localisation (UCSC) Chr 22: 35.38 – 35.39 Mb Chr 8: 75.82 – 75.83 Mb Publication PubMed [3] [4]
Wikidata
Voir/Editer Humain Voir/Editer Souris

Rôles

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

1. GRCh38: Ensembl release 89: ENSG00000100292 - Ensembl, May 2017
2. 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
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
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
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
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
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
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.
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
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
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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