Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties

References

• Panasenko OM, Gorudko IV, Sokolov AV. Hypochlorous acid as a precursor of free radicals in living systems. Biochemistry (Mosc) 2013;78:1466–1489.
   PubMed Web of Science ®Google Scholar
• Sakamaki K, Tomonaga M, Tsukui K, Nagata S. Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem 1989;264: 16828–16836.
   PubMed Web of Science ®Google Scholar
• Furtmüller PG, Burner U, Obinger C. Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 1998;37:17923–17930.
   PubMed Web of Science ®Google Scholar
• Furtmüller PG, Jantschko W, Zederbauer M, Jakopitsch C, Arnhold J, Obinger C. Kinetics of interconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase. Jpn J Infect Dis 2004;57:S30–S31.
   Web of Science ®Google Scholar
• Arnhold J, Furtmüller PG, Regelsberger G, Obinger C. Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase. Eur J Biochem 2001;268:5142–5148.
   PubMedGoogle Scholar
• Hawkins CL, Davies MJ. The role of reactive N-bromo species and radical intermediates in hypobromous acid-induced protein oxidation. Free Radic Biol Med 2005;39:900–912.
   PubMed Web of Science ®Google Scholar
• Segelmark M, Persson B, Hellmark T, Wieslander J. Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin? Clin Exp Immunol 1997;108: 167–174.
   PubMed Web of Science ®Google Scholar
• Gitlin JD. Transcriptional regulation of ceruloplasmin gene expression during inflammation. J Biol Chem 1988;263: 6281–6287.
   PubMed Web of Science ®Google Scholar
• Osaki S. Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin). J Biol Chem 1966;241:5053–5059.
   PubMed Web of Science ®Google Scholar
• Stoj C, Kosman DJ. Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function. FEBS Lett 2003;554:422–426.
   PubMed Web of Science ®Google Scholar
• Vasil'ev VB, Kachurin AM, Soroka NV. Dismutation of superoxide radicals by ceruloplasmin–details of the mechanism. Biokhimiia 1988;53:2051–2058.
   PubMedGoogle Scholar
• Shiva S, Wang X, Ringwood LA, Xu X, Yuditskaya S, Annavajjhala V, et al. Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis. Nat Chem Biol 2006;2:486–493.
   PubMed Web of Science ®Google Scholar
• Kim IG, Park SY. Requirement of intact human ceruloplasmin for the glutathione-linked peroxidase activity. FEBS Lett 1998;437:293–296.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Ageeva KV, Pulina MO, Tcherkalina OS, Samygina VR, Vlasova II, et al. Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other. Free Radic Res 2008;42:989–998.
   PubMed Web of Science ®Google Scholar
• Panasenko OM, Chekanov AV, Vlasova II, Sokolov AV, Ageeva KV, Pulina MO, et al. A study of the effect of ceruloplasmin and lactoferrin on the chlorination activity of leukocytic myeloperoxidase using the chemiluminescence method. Biofizika 2008;53:573–581.
   PubMedGoogle Scholar
• Sokolov AV, Golenkina EA, Kostevich VA, Vasilyev VB, Sud'ina GF. Interaction of ceruloplasmin and 5-lipoxygenase. Biochemistry (Mosc) 2010;75:1464–1469.
   PubMed Web of Science ®Google Scholar
• Samygina VR, Sokolov AV, Bourenkov G, Petoukhov MV, Pulina MO, Zakharova ET, et al. Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins. PLoS One 2013;8:e67145.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Zakahrova ET, Kostevich VA, Samygina VR, Vasilyev VB. Lactoferrin, myeloperoxidase, and ceruloplasmin: complementary gearwheels cranking physiological and pathological processes. Biometals 2014; 27:815–828.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Kostevich VA, Runova OL, Gorudko IV, Vasilyev VB, Cherenkevich SN, Panasenko OM. Proatherogenic modification of LDL by surface-bound myeloperoxidase. Chem Phys Lipids 2014;180:72–80.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Zakharova ET, Shavlovskiĭ MM, Vasil'ev VB. Isolation of stable human ceruloplasmin and its interaction with salmon protamine. Bioorg Khim 2005;31:269–279.
   PubMedGoogle Scholar
• Sokolov AV, Kostevich VA, Romanico DN, Zakharova ET, Vasilyev VB. Two-stage method for purification of ceruloplasmin based on its interaction with neomycin. Biochemistry (Mosc) 2012;77:631–638.
   PubMed Web of Science ®Google Scholar
• Noyer M, Dwulet FE, Hao YL, Putnam FW. Purification and characterization of undegraded human ceruloplasmin. Anal Biochem 1980;102:450–458.
   PubMed Web of Science ®Google Scholar
• Bolscher BG, Plat H, Wever R. Some properties of human eosinophil peroxidase, a comparison with other peroxidases. Biochim Biophys Acta 1984;784:177–186.
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–686.
   PubMed Web of Science ®Google Scholar
• Davis BJ. Disc electrophoresis. II. Method and application to human serum proteins. Ann N Y Acad Sci 1964;121: 404–427.
   PubMed Web of Science ®Google Scholar
• Owen CA, Smith H. Detection of ceruloplasmin after zone electrophoresis. Clin Chim Acta 1961;6:441–444.
   Web of Science ®Google Scholar
• Sokolov AV, Ageeva KV, Cherkalina OS, Pulina MO, Zakharova ET, Prozorovskii VN, et al. Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin. Chem Phys Lipids 2010;163: 347–355.
   PubMed Web of Science ®Google Scholar
• Eyer P, Worek F, Kiderlen D, Sinko G, Stuglin A, Simeon-Rudolf V, Reiner E. Molar absorption coefficients for the reduced Ellman reagent: reassessment. Anal Biochem 2003;312:224–227.
   PubMed Web of Science ®Google Scholar
• Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008;9:40
   PubMed Web of Science ®Google Scholar
• Weiler JM, Edens RE, Gleich GJ. Eosinophil granule cationic proteins regulate complement. I. Activity on the alternative pathway. J Immunol 1992;149:643–648.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Pulina MO, Ageeva KV, Ayrapetov MI, Berlov MN, Volgin GN, etal. Interaction of ceruloplasmin, lactoferrin, and myeloperoxidase. Biochemistry (Mosc) 2007; 72:409–415.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Ageeva KV, Kostevich VA, Berlov MN, Runova OL, Zakharova ET, Vasilyev VB. Study of interaction of ceruloplasmin with serprocidins. Biochemistry (Mosc) 2010;75:1361–1367.
   PubMed Web of Science ®Google Scholar
• Furtmüller PG, Zederbauer M, Jantschko W, Helm J, Bogner M, Jakopitsch C, Obinger C. Active site structure and catalytic mechanisms of human peroxidases. Arch Biochem Biophys 2006;445:199–213.
   PubMed Web of Science ®Google Scholar
• van Dalen CJ, Kettle AJ. Substrates and products of eosinophil peroxidase. Biochem J 2001;358:233–239.
   PubMed Web of Science ®Google Scholar
• van Dalen CJ, Whitehouse MW, Winterbourn CC, Kettle AJ. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J 1997;327:487–492.
   PubMed Web of Science ®Google Scholar
• Chandler JD, Day BJ. Thiocyanate: a potentially useful therapeutic agent with host defense and antioxidant properties. Biochem Pharmacol 2012;84:1381–1387.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Ageeva KV, Pulina MO, Zakharova ET, Vasilyev VB. Effect of lactoferrin on oxidative features of ceruloplasmin. Biometals 2009;22:521–529.
   PubMed Web of Science ®Google Scholar
• Chapman AL, Mocatta TJ, Shiva S, Seidel A, Chen B, Khalilova I, et al. Ceruloplasmin is an endogenous inhibitor of myeloperoxidase. J Biol Chem 2013;288:6465–6477.
   PubMed Web of Science ®Google Scholar
• De Filippis V, Vassiliev VB, Beltramini M, Fontana A, Salvato B, Gaitskhoki VS. Evidence for the molten globule state of human apo-ceruloplasmin. Biochim Biophys Acta 1996;1297:119–123.
   PubMedGoogle Scholar
• Vachette P, Dainese E, Vasyliev VB, Di Muro P, Beltramini M, Svergun DI, De Filippis V, Salvato B. A key structural role for active site type 3 copper ions in human ceruloplasmin. J Biol Chem 2002;277:40823–40831.
   PubMed Web of Science ®Google Scholar
• Saude EJ, Lacy P, Musat-Marcu S, Mayes DC, Bagu J, Man SF, Sykes BD, Moqbel R. NMR analysis of neutrophil activation in sputum samples from patients with cystic fibrosis. Magn Reson Med 2004;52:807–814.
   PubMed Web of Science ®Google Scholar
• MacPherson JC, Comhair SA, Erzurum SC, Klein DF, Lipscomb MF, Kavuru MS, Samoszuk MK, Hazen SL. Eosinophils are a major source of nitric oxide-derived oxidants in severe asthma: characterization of pathways available to eosinophils for generating reactive nitrogen species. J Immunol 2001;166:5763–5772.
   PubMed Web of Science ®Google Scholar
• Higashi N, Mita H, Taniguchi M, Turikisawa N, Higashi A, Ozawa Y, et al. Urinary eicosanoid and tyrosine derivative concentrations in patients with vasculitides. J Allergy Clin Immunol 2004;114:1353–1358.
   PubMed Web of Science ®Google Scholar
• Pattison DI, Davies MJ. Kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and use of 3-bromotyrosine as a marker of oxidative stress. Biochemistry 2004;43:4799–4809.
   PubMed Web of Science ®Google Scholar
• Panasenko OM, Vakhrusheva T, Tretyakov V, Spalteholz H, Arnhold J. Influence of chloride on modification of unsaturated phosphatidylcholines by the myeloperoxidase/hydrogen peroxide/bromide system. Chem Phys Lipids 2007;149: 40–51.
   PubMed Web of Science ®Google Scholar
• Senthilmohan R, Kettle AJ. Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch Biochem Biophys 2006;445: 235–244.
   PubMed Web of Science ®Google Scholar
• Squitti R, Quattrocchi CC, Salustri C, Rossini PM. Ceruloplasmin fragmentation is implicated in ‘free’ copper deregulation of Alzheimer's disease. Prion 2008;2:23–27.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Pulina MO, Ageeva KV, Tcherkalina OS, Zakharova ET, Vasilyev VB. Identification of complexes formed by ceruloplasmin with matrix metalloproteinases 2 and 12. Biochemistry (Mosc) 2009; 74:1388–1392.
   PubMed Web of Science ®Google Scholar
• Sokolov AV, Pulina MO, Ageeva KV, Runova OL, Zakharova ET, Vasil'ev VB. Identification of leukocyte cationic proteins that interact with ceruloplasmin. Biochemistry (Mosc) 2007;72:872–877.
   PubMed Web of Science ®Google Scholar