好酸球ペルオキシダーゼ EPO
WordNet
- any of a group of enzymes (occurring especially in plant cells) that catalyze the oxidation of a compound by a peroxide
- a leukocyte readily stained with eosin (同)eosinophile
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/05/31 08:14:24」(JST)
[Wiki en表示]
Eosinophil peroxidase is a haloperoxidase enzyme that in humans is encoded by the EPX gene.[1][2] The enzyme is a heterodimeric 71-77 kD peroxidase consisting of a heavier glycosylated chain and a lighter nonglycosylated chain. This enzyme prefers bromide over chloride as a substrate, converting it to toxic hypobromite.
Eosinophil peroxidase |
Identifiers |
Symbols |
EPX ; EPO; EPP; EPX-PEN |
External IDs |
OMIM: 131399 MGI: 107569 HomoloGene: 20144 ChEMBL: 2438 GeneCards: EPX Gene |
EC number |
1.11.1.7 |
Gene ontology |
Molecular function |
• peroxidase activity
• heme binding
• metal ion binding
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Biological process |
• defense response to nematode
• negative regulation of interleukin-10 production
• negative regulation of interleukin-5 production
• positive regulation of interleukin-4 production
• hydrogen peroxide catabolic process
• eosinophil migration
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Sources: Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
8288 |
13861 |
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Ensembl |
ENSG00000121053 |
ENSMUSG00000052234 |
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UniProt |
P11678 |
P49290 |
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RefSeq (mRNA) |
NM_000502 |
NM_007946 |
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RefSeq (protein) |
NP_000493 |
NP_031972 |
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Location (UCSC) |
Chr 17:
56.27 – 56.28 Mb |
Chr 11:
87.86 – 87.88 Mb |
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PubMed search |
[1] |
[2] |
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Contents
- 1 Function
- 2 Role in pathology
- 3 See also
- 4 References
- 5 Further reading
- 6 External links
Function
In the presence of H2O2 formed by the eosinophil, and either chloride or bromide ions, eosinophil peroxidase provides a potent mechanism by which eosinophils kill multicellular parasites (such as, for example, the nematode worms involved in filariasis); and also certain bacteria (such as tuberculosis bacteria). Eosinophil peroxidase is a haloperoxidase that preferentially uses bromide over chloride for this purpose, generating hypobromite (hypobromous acid).[3] The enzyme is also capable of oxidizing thiocyanate (SCN-) and uses it as a co-substrate, with optimal concentrations occurring at about normal plasma levels.[4]
Eosinophil peroxidase is also partly responsible for tissue remodeling.
Role in pathology
The oxidizing compounds produced by eosinophil peroxidase have been implicated in the inflammatory pathology of several disease states, including asthma.[5]
See also
- Eosinophil
- Major basic protein
References
- ^ Sakamaki K, Tomonaga M, Tsukui K, Nagata S (October 1989). "Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase". J. Biol. Chem. 264 (28): 16828–36. PMID 2550461.
- ^ Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ (May 1989). "Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family". J. Exp. Med. 169 (5): 1757–69. doi:10.1084/jem.169.5.1757. PMC 2189302. PMID 2541222.
- ^ Mayeno AN, Curran AJ, Roberts RL, Foote CS (April 1989). "Eosinophils preferentially use bromide to generate halogenating agents". J. Biol. Chem. 264 (10): 5660–8. PMID 2538427.
- ^ Tahboub YR, Galijasevic S, Diamond MP, Abu-Soud HM (2005). "Thiocyanate modulates the catalytic activity of mammalian peroxidases". J. Biol. Chem. 280 (28): 26129–36. doi:10.1074/jbc.M503027200. PMID 15894800.
- ^ van Dalen CJ, Kettle AJ (August 2001). "Substrates and products of eosinophil peroxidase". Biochem. J. 358 (Pt 1): 233–9. doi:10.1042/0264-6021:3580233. PMC 1222052. PMID 11485572.
Further reading
- Romano M, Patriarca P, Melo C, et al. (1994). "Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12496–500. doi:10.1073/pnas.91.26.12496. PMC 45465. PMID 7809065.
- Ten RM, Pease LR, McKean DJ, et al. (1989). "Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family". J. Exp. Med. 169 (5): 1757–69. doi:10.1084/jem.169.5.1757. PMC 2189302. PMID 2541222.
- Ulrich M, Petre A, Youhnovski N, et al. (2008). "Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase". J. Biol. Chem. 283 (42): 28629–40. doi:10.1074/jbc.M801196200. PMC 2661412. PMID 18694936.
- van Dalen CJ, Winterbourn CC, Kettle AJ (2006). "Mechanism of nitrite oxidation by eosinophil peroxidase: implications for oxidant production and nitration by eosinophils". Biochem. J. 394 (Pt 3): 707–13. doi:10.1042/BJ20051470. PMC 1383721. PMID 16336215.
- Parwez Q, Stemmler S, Epplen JT, Hoffjan S (2008). "Variation in genes encoding eosinophil granule proteins in atopic dermatitis patients from Germany". Journal of negative results in biomedicine 7: 9. doi:10.1186/1477-5751-7-9. PMC 2596079. PMID 19014520.
- Yamaguchi E, Nishihira J, Shimizu T, et al. (2000). "Macrophage migration inhibitory factor (MIF) in bronchial asthma". Clin. Exp. Allergy 30 (9): 1244–9. doi:10.1046/j.1365-2222.2000.00888.x. PMID 10971470.
- Sakamaki K, Tomonaga M, Tsukui K, Nagata S (1989). "Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase". J. Biol. Chem. 264 (28): 16828–36. PMID 2550461.
- Nakamura H, Miyagawa K, Ogino K, et al. (2003). "High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis". J. Allergy Clin. Immunol. 112 (6): 1127–31. doi:10.1016/j.jaci.2003.08.051. PMID 14657871.
- Hrdlickova B, Izakovicova-Holla L (2009). "Association of single nucleotide polymorphisms in the eosinophil peroxidase gene with allergic rhinitis in the Czech population". Int. Arch. Allergy Immunol. 150 (2): 184–91. doi:10.1159/000218122. PMID 19439985.
- Nakamura H, Higashikawa F, Miyagawa K, et al. (2004). "Association of single nucleotide polymorphisms in the eosinophil peroxidase gene with Japanese cedar pollinosis". Int. Arch. Allergy Immunol. 135 (1): 40–3. doi:10.1159/000080222. PMID 15316147.
- Keyhani E, Zarei MA, Lashgarblooki-Livani T (1999). "Kinetics of peroxidases in guinea pig bone marrow under immunostimulation". FEBS Lett. 452 (3): 233–6. doi:10.1016/S0014-5793(99)00665-1. PMID 10386597.
- Hartley JL, Temple GF, Brasch MA (2000). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Sakamaki K, Kanda N, Ueda T, et al. (2000). "The eosinophil peroxidase gene forms a cluster with the genes for myeloperoxidase and lactoperoxidase on human chromosome 17". Cytogenet. Cell Genet. 88 (3–4): 246–8. doi:10.1159/000015529. PMID 10828600.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Borelli V, Vita F, Shankar S, et al. (2003). "Human Eosinophil Peroxidase Induces Surface Alteration, Killing, and Lysis of Mycobacterium tuberculosis". Infect. Immun. 71 (2): 605–13. doi:10.1128/IAI.71.2.605-613.2003. PMC 145361. PMID 12540536.
- Wu C, Ma MH, Brown KR, et al. (2007). "Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening". Proteomics 7 (11): 1775–85. doi:10.1002/pmic.200601006. PMID 17474147.
- Oxvig C, Thomsen AR, Overgaard MT, et al. (1999). "Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo". J. Biol. Chem. 274 (24): 16953–8. doi:10.1074/jbc.274.24.16953. PMID 10358043.
External links
- Eosinophil peroxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
Oxidoreductases: peroxidases (EC 1.11)
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1.11.1.1-14 |
- Catalase
- Cytochrome c peroxidase
- Eosinophil peroxidase
- Glutathione peroxidase
- Horseradish peroxidase
- Lactoperoxidase
- Myeloperoxidase
- Thyroid peroxidase
- Deiodinase
- Iodothyronine deiodinase
- Iodotyrosine deiodinase
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1.11.1.15 (peroxiredoxin) |
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Antimicrobial peptides: Granulocyte granule contents
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Azurophilic granules (1°) |
- Myeloperoxidase
- Defensins
- neutral serine proteases (Proteinase 3)
- Lysozyme
- Bactericidal/permeability increasing protein
- Collagenase
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Specific granules (2°) |
Neutrophil
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- Alkaline phosphatase
- Lactoferrin
- Lysozyme
- NADPH oxidase
- Collagenase
- Cathelicidin
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Eosinophil
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- Cathepsin
- Major basic protein
- Eosinophil cationic protein
- Eosinophil peroxidase
- Eosinophil-derived neurotoxin
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Basophil
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see also platelet alpha-granule, dense granule
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cell/phys (coag, heme, immu, gran), csfs
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rbmg/mogr/tumr/hist, sysi/epon, btst
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drug (B1/2/3+5+6), btst, trns
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From JC Segen Dictionary of Modern Medicine database
UpToDate Contents
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English Journal
- Indigenous enteric eosinophils control DCs to initiate a primary Th2 immune response in vivo.
- Chu DK1, Jimenez-Saiz R1, Verschoor CP1, Walker TD1, Goncharova S1, Llop-Guevara A1, Shen P1, Gordon ME1, Barra NG1, Bassett JD1, Kong J1, Fattouh R2, McCoy KD3, Bowdish DM1, Erjefält JS4, Pabst O5, Humbles AA6, Kolbeck R6, Waserman S1, Jordana M7.
- The Journal of experimental medicine.J Exp Med.2014 Jul 28;211(8):1657-72. doi: 10.1084/jem.20131800.
- Eosinophils natively inhabit the small intestine, but a functional role for them there has remained elusive. Here, we show that eosinophil-deficient mice were protected from induction of Th2-mediated peanut food allergy and anaphylaxis, and Th2 priming was restored by reconstitution with il4(+/+) or
- PMID 25071163
- Sex-response differences of immunological and histopathological biomarkers in gill of Prochilodus argenteus from a polluted river in southeast Brazil.
- Procópio MS1, Ribeiro HJ1, Pereira LA2, Oliveira Lopes GA3, Castro AC1, Rizzo E1, Sato Y4, Russo RC3, Corrêa JD Jr5.
- Fish & shellfish immunology.Fish Shellfish Immunol.2014 Jul;39(1):108-17. doi: 10.1016/j.fsi.2014.04.010. Epub 2014 May 2.
- The fish gill is in direct and standing contact with the immediate external environment and, therefore, is highly vulnerable to aquatic pollutants. In this study, Prochilodus argenteus were caught at two different points in São Francisco river. The first point is located near Três Marias dam, whil
- PMID 24795082
- Eosinophil Granule Proteins: Form and Function.
- Acharya KR1, Ackerman SJ2.
- The Journal of biological chemistry.J Biol Chem.2014 Jun 20;289(25):17406-17415. Epub 2014 May 6.
- Experimental and clinical data strongly support a role for the eosinophil in the pathogenesis of asthma, allergic and parasitic diseases, and hypereosinophilic syndromes, in addition to more recently identified immunomodulatory roles in shaping innate host defense, adaptive immunity, tissue repair/r
- PMID 24802755
Japanese Journal
- マイクロウェーブ固定で観察した鼻アレルギー鼻粘膜中の好酸球
- 廣瀬 壮
- Dokkyo journal of medical sciences 37(2), 97-101, 2010-07-25
- 好酸球顆粒内蛋白は組織障害性物質であることが知られている.しかし,これらの蛋白がどのように細胞外へ放出されるかの報告は非常に少ない.今回,我々はタンニンを含んだ固定液を用いてマイクロウェーブ照射(MWI)を試みた.タンニンは蛋白の固定力が強く,蛋白を高電子物質として可視化する.好酸球顆粒内蛋白がどのように顆粒外に出てくるかを検討した.MWIを施して, そしてこの結果が既に報告されているDAB 法に …
- NAID 110007616516
- Chromatographic methods for the analyses of 2-halofatty aldehydes and chlorohydrin molecular species of lysophosphatidylcholine
- ALBERT Carolyn J.,ANBUKUMAR Dhanalakshmi S.,MESSNER Maria C.,FORD David A.
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 877(26), 2768-2777, 2009-09-15
- NAID 10028023497
- Efficient assay for total antioxidant capacity in human plasma using a 96-well microplte
- Kambayashi Yasuhiro,Ogino Keiki,Takemoto Kei,Imagama Takashi,Takigawa Tomoko,Kimura Shingo,Hibino Yuri,Hitomi Yoshiaki,Nakamura Hiroyuki
- Journal of Clinical Biochemistry and Nutrition 44(1), 95-103, 2009-01
- … (Di)bromotyrosine is formed by the specific reaction of eosinophil peroxidase and can be used as an eosinophil activation marker. … In the present study, an antibody for (di)bromotyrosine in proteins was prepared to investigate the pathogenesis of eosinophil-related diseases such as allergic responses. …
- NAID 120001170065
Related Links
- TEXT Description Human eosinophil peroxidase (EC 1.11.1.7) is a heme-containing glycoprotein that is present in lysosomes of eosinophilic granulocytes.
- Lee Bio produces ultra pure Eosinophil Peroxidase (EPO) from human eosinophils for diagnostic manufacturing, control, calibrator and research uses - Inquire for details. ... Lee Biosolutions is the leading supplier of Human Eosinophil ...
★リンクテーブル★
[★]
- 関
- EPP erythropoietic protoporphyria 赤血球生成性プロトポルフィリン症
[★]
- 英
- eosinophil peroxidase, EPO
- 関
- 好酸球
[★]
ペルオキシダーゼ、過酸化酵素
- 関
- myeloperoxidase