Perossidasi eosinofila

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Perossidasi eosinofila
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Numero EC 1.11.1.7
Classe Ossidoreduttasi
Banche dati BRENDA, EXPASY, GTD, KEGG, PDB
Fonte: IUBMB

La perossidasi eosinofila o EPO (dall'inglese eosinophil peroxidase) è un enzima perossidasi (aloperossidasi) codificato negli esseri umani dal gene EPX.[1][2] È un eterodimero 71-77 kD composto da una catena più pesante glicosilata e una più leggera non glicosilata.

Indice

Funzione[modifica]

In presenza di H2O2, formata dall'eosinofilo, e ioni cloruro o bromuro, la perossidasi eosinofila innesca un potente meccanismo con il quale l'eosinofilo uccide parassiti multicellulari (come, per esempio, il verme nematode che causa filariasi); e anche alcuni batteri (come ad esempio quello della tubercolosi). Questo enzima usa preferenzialmente come substrato il bromuro piuttosto che il cloruro, generando ipobromito (acido ipobromoso).[3]

L'enzima è anche in grado di ossidare il tiocianato e usarlo come co-substrato.[4]

Ruolo nelle patologie[modifica]

I composti ossidanti prodotti dalla perossidasi eosinofila sono implicati in stati infiammatorie di diverse patologie, incluso l'asma.[5]

Voci correlate[modifica]

Note[modifica]

  1. ^ Sakamaki K, Tomonaga M, Tsukui K, Nagata S (ottobre 1989). Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J. Biol. Chem. 264 (28): 16828–36. PMID 2550461.
  2. ^ Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ (maggio 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. PMID 2541222.
  3. ^ Mayeno AN, Curran AJ, Roberts RL, Foote CS (aprile 1989). Eosinophils preferentially use bromide to generate halogenating agents. J. Biol. Chem. 264 (10): 5660–8. PMID 2538427.
  4. ^ 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.
  5. ^ van Dalen CJ, Kettle AJ (agosto 2001). Substrates and products of eosinophil peroxidase. Biochem. J. 358 (Pt 1): 233–9. DOI:10.1042/0264-6021:3580233. PMID 11485572.

Bibliografia[modifica]

  • 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. 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. 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. 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. 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. 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. 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. 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. 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.
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