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Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins.

Samygina VR, Sokolov AV, Bourenkov G, Petoukhov MV, Pulina MO, Zakharova ET, Vasilyev VB, Bartunik H, Svergun DI
PLoS One 8 e67145 (2013)
Cited: 58 times
EuropePMC logo PMID: 23843990

Abstract

Copper-containing ferroxidase ceruloplasmin (Cp) forms binary and ternary complexes with cationic proteins lactoferrin (Lf) and myeloperoxidase (Mpo) during inflammation. We present an X-ray crystal structure of a 2Cp-Mpo complex at 4.7 Å resolution. This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo. Small angle X-ray scattering was employed to construct low-resolution models of the Cp-Lf complex and, for the first time, of the ternary 2Cp-2Lf-Mpo complex in solution. The SAXS-based model of Cp-Lf supports the predicted 1:1 stoichiometry of the complex and demonstrates that both lobes of Lf contact domains 1 and 6 of Cp. The 2Cp-2Lf-Mpo SAXS model reveals the absence of interaction between Mpo and Lf in the ternary complex, so Cp can serve as a mediator of protein interactions in complex architecture. Mpo protects antioxidant properties of Cp by isolating its sensitive loop from proteases. The latter is important for incorporation of Fe(3+) into Lf, which activates ferroxidase activity of Cp and precludes oxidation of Cp substrates. Our models provide the structural basis for possible regulatory role of these complexes in preventing iron-induced oxidative damage.

Reviews - 4ejx mentioned but not cited (1)

  1. Methods for measuring myeloperoxidase activity toward assessing inhibitor efficacy in living systems. Huang J, Milton A, Arnold RD, Huang H, Smith F, Panizzi JR, Panizzi P. J Leukoc Biol 99 541-548 (2016)

Articles - 4ejx mentioned but not cited (4)

  1. Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins. Samygina VR, Sokolov AV, Bourenkov G, Petoukhov MV, Pulina MO, Zakharova ET, Vasilyev VB, Bartunik H, Svergun DI. PLoS One 8 e67145 (2013)
  2. Hyper-truncated Asn355- and Asn391-glycans modulate the activity of neutrophil granule myeloperoxidase. Tjondro HC, Ugonotti J, Kawahara R, Chatterjee S, Loke I, Chen S, Soltermann F, Hinneburg H, Parker BL, Venkatakrishnan V, Dieckmann R, Grant OC, Bylund J, Rodger A, Woods RJ, Karlsson-Bengtsson A, Struwe WB, Thaysen-Andersen M. J Biol Chem 296 100144 (2021)
  3. Identification of Blood Transport Proteins to Carry Temoporfin: A Domino Approach from Virtual Screening to Synthesis and In Vitro PDT Testing. Marconi A, Giugliano G, Di Giosia M, Marforio TD, Trivini M, Turrini E, Fimognari C, Zerbetto F, Mattioli EJ, Calvaresi M. Pharmaceutics 15 919 (2023)
  4. Molecular dynamics analysis of conserved water mediated inter-domain recognition of His667-Trp669 in human ceruloplasmin. Mukhopadhyay BP. Bioinformation 16 209-218 (2020)


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  3. The Dual Role of Myeloperoxidase in Immune Response. Arnhold J. Int J Mol Sci 21 E8057 (2020)
  4. Smoking-induced iron dysregulation in the lung. Zhang WZ, Butler JJ, Cloonan SM. Free Radic Biol Med 133 238-247 (2019)
  5. Regulation of zinc-dependent enzymes by metal carrier proteins. Thompson MW. Biometals 35 187-213 (2022)
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  8. Heme Peroxidases at Unperturbed and Inflamed Mucous Surfaces. Arnhold J. Antioxidants (Basel) 10 1805 (2021)
  9. Molecular Functions of Ceruloplasmin in Metabolic Disease Pathology. Liu Z, Wang M, Zhang C, Zhou S, Ji G. Diabetes Metab Syndr Obes 15 695-711 (2022)
  10. A Current State of Proteomics in Adult and Pediatric Inflammatory Bowel Diseases: A Systematic Search and Review. Fabian O, Bajer L, Drastich P, Harant K, Sticova E, Daskova N, Modos I, Tichanek F, Cahova M. Int J Mol Sci 24 9386 (2023)
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  3. Erythropoietin and Nrf2: key factors in the neuroprotection provided by apo-lactoferrin. Zakharova ET, Sokolov AV, Pavlichenko NN, Kostevich VA, Abdurasulova IN, Chechushkov AV, Voynova IV, Elizarova AY, Kolmakov NN, Bass MG, Semak IV, Budevich AI, Kozhin PM, Zenkov NK, Klimenko VM, Kirik OV, Korzhevskii DE, Menshchikova EB, Vasilyev VB. Biometals 31 425-443 (2018)
  4. A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1. Lai RP, Hock M, Radzimanowski J, Tonks P, Hulsik DL, Effantin G, Seilly DJ, Dreja H, Kliche A, Wagner R, Barnett SW, Tumba N, Morris L, LaBranche CC, Montefiori DC, Seaman MS, Heeney JL, Weissenhorn W. J Biol Chem 289 29912-29926 (2014)
  5. Copper(II)-binding equilibria in human blood. Kirsipuu T, Zadorožnaja A, Smirnova J, Friedemann M, Plitz T, Tõugu V, Palumaa P. Sci Rep 10 5686 (2020)
  6. Proatherogenic modification of LDL by surface-bound myeloperoxidase. Sokolov AV, Kostevich VA, Runova OL, Gorudko IV, Vasilyev VB, Cherenkevich SN, Panasenko OM. Chem Phys Lipids 180 72-80 (2014)
  7. Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties. Sokolov AV, Kostevich VA, Zakharova ET, Samygina VR, Panasenko OM, Vasilyev VB. Free Radic Res 49 800-811 (2015)
  8. Lactoferrin, myeloperoxidase, and ceruloplasmin: complementary gearwheels cranking physiological and pathological processes. Sokolov AV, Zakharova ET, Kostevich VA, Samygina VR, Vasilyev VB. Biometals 27 815-828 (2014)
  9. Thrombin inhibits the anti-myeloperoxidase and ferroxidase functions of ceruloplasmin: relevance in rheumatoid arthritis. Sokolov AV, Acquasaliente L, Kostevich VA, Frasson R, Zakharova ET, Pontarollo G, Vasilyev VB, De Filippis V. Free Radic Biol Med 86 279-294 (2015)
  10. Serum protein profiling of adults and children with Crohn disease. Vaiopoulou A, Gazouli M, Papadopoulou A, Anagnostopoulos AK, Karamanolis G, Theodoropoulos GE, M'Koma A, Tsangaris GT. J Pediatr Gastroenterol Nutr 60 42-47 (2015)
  11. AFM Imaging of Protein Aggregation in Studying the Impact of Knotted Electromagnetic Field on A Peroxidase. Ivanov YD, Pleshakova TO, Shumov ID, Kozlov AF, Ivanova IA, Valueva AA, Tatur VY, Smelov MV, Ivanova ND, Ziborov VS. Sci Rep 10 9022 (2020)
  12. An immunological method to combine the measurement of active and total myeloperoxidase on the same biological fluid, and its application in finding inhibitors which interact directly with the enzyme. Franck T, Minguet G, Delporte C, Derochette S, Zouaoui Boudjeltia K, Van Antwerpen P, Gach O, Deby-Dupont G, Mouithys-Mickalad A, Serteyn D. Free Radic Res 49 790-799 (2015)
  13. Biallelic HEPHL1 variants impair ferroxidase activity and cause an abnormal hair phenotype. Sharma P, Reichert M, Lu Y, Markello TC, Adams DR, Steinbach PJ, Fuqua BK, Parisi X, Kaler SG, Vulpe CD, Anderson GJ, Gahl WA, Malicdan MCV. PLoS Genet 15 e1008143 (2019)
  14. Genetic and Clinical Heterogeneity in Thirteen New Cases with Aceruloplasminemia. Atypical Anemia as a Clue for an Early Diagnosis. Vila Cuenca M, Marchi G, Barqué A, Esteban-Jurado C, Marchetto A, Giorgetti A, Chelban V, Houlden H, Wood NW, Piubelli C, Dorigatti Borges M, Martins de Albuquerque D, Yotsumoto Fertrin K, Jové-Buxeda E, Sanchez-Delgado J, Baena-Díez N, Burnyte B, Utkus A, Busti F, Kaubrys G, Suku E, Kowalczyk K, Karaszewski B, Porter JB, Pollard S, Eleftheriou P, Bignell P, Girelli D, Sanchez M, Sanchez M. Int J Mol Sci 21 E2374 (2020)
  15. Copper chelation and interleukin-6 proinflammatory cytokine effects on expression of different proteins involved in iron metabolism in HepG2 cell line. Di Bella LM, Alampi R, Biundo F, Toscano G, Felice MR. BMC Biochem 18 1 (2017)
  16. Fine Regulation of Neutrophil Oxidative Status and Apoptosis by Ceruloplasmin and Its Derivatives. Golenkina EA, Viryasova GM, Galkina SI, Gaponova TV, Sud'ina GF, Sokolov AV. Cells 7 E8 (2018)
  17. Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. Sokolov AV, Kostevich VA, Kozlov SO, Donskyi IS, Vlasova II, Rudenko AO, Zakharova ET, Vasilyev VB, Panasenko OM. Free Radic Res 49 777-789 (2015)
  18. Comparison of Interaction between Ceruloplasmin and Lactoferrin/Transferrin: to Bind or Not to Bind. Sokolov AV, Voynova IV, Kostevich VA, Vlasenko AY, Zakharova ET, Vasilyev VB. Biochemistry (Mosc) 82 1073-1078 (2017)
  19. Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet. Kostevich VA, Sokolov AV, Kozlov SO, Vlasenko AY, Kolmakov NN, Zakharova ET, Vasilyev VB. Biometals 29 691-704 (2016)
  20. Spectrophotometric Quantification of Peroxidase with p-Phenylene-diamine for Analyzing Peroxidase-Encapsulating Lipid Vesicles. Zhang Y, Schmid YRF, Luginbühl S, Wang Q, Dittrich PS, Walde P. Anal Chem 89 5484-5493 (2017)
  21. Ceruloplasmin decreases respiratory burst reaction during pregnancy. Varfolomeeva EY, Semenova EV, Sokolov AV, Aplin KD, Timofeeva KE, Vasilyev VB, Filatov MV. Free Radic Res 50 909-919 (2016)
  22. Recognition dynamics of trinuclear copper cluster and associated histidine residues through conserved or semi-conserved water molecules in human Ceruloplasmin: The involvement of aspartic and glutamic acid gates. Mukhopadhyay BP. J Biomol Struct Dyn 36 3829-3842 (2018)
  23. Ceruloplasmin and Hypoferremia: Studies in Burn and Non-Burn Trauma Patients. Dubick MA, Barr JL, Keen CL, Atkins JL. Antioxidants (Basel) 4 153-169 (2015)
  24. Association of serum arginase I with L-arginine, 3-nitrotyrosine, and exhaled nitric oxide in healthy Japanese workers. Ogino K, Wang DH, Kubo M, Obase Y, Setiawan H, Yan F, Takahashi H, Zhang R, Tsukiyama Y, Yoshida J, Zou Y. Free Radic Res 48 137-145 (2014)
  25. Computational modelling of the redistribution of copper isotopes by proteins in the liver. Tennant A, Rauk A, Wieser ME. Metallomics 9 1809-1819 (2017)
  26. Inflammatory protein response in CDKL5-Rett syndrome: evidence of a subclinical smouldering inflammation. Cortelazzo A, de Felice C, Leoncini S, Signorini C, Guerranti R, Leoncini R, Armini A, Bini L, Ciccoli L, Hayek J. Inflamm Res 66 269-280 (2017)
  27. Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic. Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB. Metallomics 9 1828-1838 (2017)
  28. Deglycosylation influences the oxidation activity and antigenicity of myeloperoxidase. Wang J, Li JN, Cui Z, Zhao MH. Nephrology (Carlton) 23 46-52 (2018)
  29. Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions. Kostevich VA, Sokolov AV, Grudinina NA, Zakharova ET, Samygina VR, Vasilyev VB. Biometals 28 817-826 (2015)
  30. The Estimation of Blood Paramagnetic Center Changes during Burns Management with Biodegradable Propolis-Nanofiber Dressing. Olczyk P, Komosinska-Vassev K, Krzyminiewski R, Kasperczyk J, Ramos P, Dobosz B, Batoryna O, Stojko J, Stojko M, Ivanova D, Olczyk K, Pilawa B. Oxid Med Cell Longev 2020 3675603 (2020)
  31. Capacity of ceruloplasmin to scavenge products of the respiratory burst of neutrophils is not altered by the products of reactions catalyzed by myeloperoxidase. Sokolov AV, Kostevich VA, Varfolomeeva EY, Grigorieva DV, Gorudko IV, Kozlov SO, Kudryavtsev IV, Mikhalchik EV, Filatov MV, Cherenkevich SN, Panasenko OM, Arnhold J, Vasilyev VB. Biochem Cell Biol 96 457-467 (2018)
  32. Hepatic SEL1L-HRD1 ER-associated degradation regulates systemic iron homeostasis via ceruloplasmin. Thepsuwan P, Bhattacharya A, Song Z, Hippleheuser S, Feng S, Wei X, Das NK, Sierra M, Wei J, Fang D, Huang YM, Zhang K, Shah YM, Sun S. Proc Natl Acad Sci U S A 120 e2212644120 (2023)
  33. Increased DNA damage and oxidative stress among silver jewelry workers. Aktepe N, Aktepe N, Kocyigit A, Yukselten Y, Taskin A, Keskin C, Celik H. Biol Trace Elem Res 164 185-191 (2015)
  34. Molecular mimicry of the receptor-binding domain of the SARS-CoV-2 spike protein: from the interaction of spike-specific antibodies with transferrin and lactoferrin to the antiviral effects of human recombinant lactoferrin. Sokolov AV, Isakova-Sivak IN, Mezhenskaya DA, Kostevich VA, Gorbunov NP, Elizarova AY, Matyushenko VA, Berson YM, Grudinina NA, Kolmakov NN, Zabrodskaya YA, Komlev AS, Semak IV, Budevich AI, Rudenko LG, Vasilyev VB. Biometals 36 437-462 (2023)
  35. Putative role of conserved water molecules in the hydration and inter-domain recognition of mono nuclear copper centers in O2-bound human ceruloplasmin: A comparative study between X-ray and MD simulated structures. Mukhopadhyay BP. Bioinformation 15 402-411 (2019)
  36. Ceruloplasmin-derived peptide is the strongest regulator of oxidative stress and leukotriene synthesis in neutrophils. Golenkina EA, Livenskyi AD, Viryasova GM, Romanova YM, Sud'ina GF, Sokolov AV. Biochem Cell Biol 95 445-449 (2017)
  37. Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines. Mukhopadhyay BP. Bioinformation 15 750-759 (2019)
  38. Letter Relationships between meconium concentrations of acute phase proteins. Lisowska-Myjak B, Skarżyńska E, Płazińska M, Jakimiuk A. Clin Exp Pharmacol Physiol 45 1218-1220 (2018)
  39. Serum Ceruloplasmin Is the Candidate Predictive Biomarker for Acute Aortic Dissection and Is Related to Thrombosed False Lumen: a Propensity Score-Matched Observational Case-Control Study. Ma C, Zhao H, Shi F, Li M, Liu X, Ji C, Han Y. Biol Trace Elem Res 199 895-911 (2021)
  40. Caught red handed: modeling and confirmation of the myeloperoxidase ceruloplasmin alpha-thrombin complex. Zabrodskaya YA, Egorov VV, Sokolov AV, Shvetsov AV, Gorshkova YE, Ivankov OI, Kostevich VA, Gorbunov NP, Ramsay ES, Fedorova ND, Bondarenko AB, Vasilyev VB. Biometals 35 1157-1168 (2022)
  41. Methylglyoxal-Modified Human Serum Albumin Binds to Leukocyte Myeloperoxidase and Inhibits its Enzymatic Activity. Panasenko OM, Ivanov VA, Mikhalchik EV, Gorudko IV, Grigorieva DV, Basyreva LY, Shmeleva EV, Gusev SA, Kostevich VA, Gorbunov NP, Sokolov AV. Antioxidants (Basel) 11 2263 (2022)
  42. The Effect of a Rotating Cone on Horseradish Peroxidase Aggregation on Mica Revealed by Atomic Force Microscopy. Ivanov YD, Tatur VY, Shumov ID, Kozlov AF, Valueva AA, Ivanova IA, Ershova MO, Ivanova ND, Stepanov IN, Lukyanitsa AA, Ziborov VS. Micromachines (Basel) 13 1947 (2022)


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