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Oxidative Medicine and Cellular Longevity
Volume 2016 (2016), Article ID 3075695, 9 pages
http://dx.doi.org/10.1155/2016/3075695
Review Article

Widening and Elaboration of Consecutive Research into Therapeutic Antioxidant Enzyme Derivatives

Institute of Experimental Cardiology, Russian Cardiology Research-and-Production Complex, Ministry of Health Care of Russian Federation, 15a 3rd Cherepkovskaya Street, Moscow 121552, Russia

Received 22 December 2015; Revised 16 February 2016; Accepted 16 March 2016

Academic Editor: Tanea T. Reed

Copyright © 2016 Alexander V. Maksimenko. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. E. Sobel, “Coronary thrombolysis and the new biology,” Journal of the American College of Cardiology, vol. 14, no. 4, pp. 850–860, 1989. View at Publisher · View at Google Scholar · View at Scopus
  2. A. V. Maksimenko and E. G. Tischenko, “New thrombolytic strategy: bolus administration of tPA and urokinase-fibrinogen conjugate,” Journal of Thrombosis and Thrombolysis, vol. 7, no. 3, pp. 307–312, 1999. View at Publisher · View at Google Scholar · View at Scopus
  3. A. V. Maksimenko, “Development and application of targeted therapeutic protein conjugates,” Russian Journal of General Chemistry, vol. 84, no. 2, pp. 357–363, 2014. View at Publisher · View at Google Scholar · View at Scopus
  4. A. V. Maksimenko, “Cardiological biopharmaceuticals in the conception of drug targeting delivery: practical results and research perspectives,” Acta Naturae, vol. 4, no. 3, pp. 72–81, 2012. View at Google Scholar
  5. Z. L. Wu, “Time of molecular glycobiology,” Glycobiology Journal, vol. 1, no. 2, article e106, 2012. View at Publisher · View at Google Scholar
  6. C. M. West, “Latest advances in glycobiology highlighted and old challenges revisited at the 2013 annual conference of the society for glycobiology,” Glycobiology, vol. 24, no. 3, pp. 218–219, 2014. View at Publisher · View at Google Scholar · View at Scopus
  7. E. D. Hood, M. Chorny, C. F. Greineder, I. Alferiev, R. J. Levy, and V. R. Muzykantov, “Endothelial targeting of nanocarriers loaded with antioxidant enzymes for protection against vascular oxidative stress and inflammation,” Biomaterials, vol. 35, no. 11, pp. 3708–3715, 2014. View at Publisher · View at Google Scholar · View at Scopus
  8. P. U. Richard, J. T. Duskey, S. Stolarov, M. Spulber, and C. G. Palivan, “New concepts to fight oxidative stress: nanosized three-dimensional supramolecular antioxidant assemblies,” Expert Opinion on Drug Delivery, vol. 12, no. 9, pp. 1527–1545, 2015. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Sandhir, A. Yadav, A. Sunkaria, and N. Singhal, “Nano-antioxidants: an emerging strategy for intervention against neurodegenerative conditions,” Neurochemistry International, vol. 89, pp. 209–226, 2015. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Kim, J.-H. Kim, O. Jeon, I. C. Kwon, and K. Park, “Engineered polymers for advanced drug delivery,” European Journal of Pharmaceutics and Biopharmaceutics, vol. 71, no. 3, pp. 420–430, 2009. View at Publisher · View at Google Scholar · View at Scopus
  11. H. W. Zhang, F. S. Wang, W. Shao et al., “Characterization and stability investigation of Cu,Zn-superoxide dismutase covalently modified by low molecular weight heparin,” Biochemistry (Moscow), vol. 71, supplement 1, pp. S96–S100, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. J. Soucek, P. Poucková, J. Strohalm et al., “Poly[N-(2-hydroxypropyl)methacrylamide] conjugates of bovine pancreatic ribonuclease (RNase A) inhibit growth of human melanoma in nude mice,” Journal of Drug Targeting, vol. 10, no. 3, pp. 175–183, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Nakamura and A. Kato, “Multi-functional biopolymer prepared by covalent attachment of galactomannan to egg-white proteins through naturally occurring Maillard reaction,” Nahrung, vol. 44, no. 3, pp. 201–206, 2000. View at Google Scholar · View at Scopus
  14. D. Xie, C. Yao, L. Wang et al., “An albumin-conjugated peptide exhibits potent anti-HIV activity and long in vivo half-life,” Antimicrobial Agents and Chemotherapy, vol. 54, no. 1, pp. 191–196, 2010. View at Publisher · View at Google Scholar
  15. A. Kultti, C. Zhao, N. C. Singha et al., “Accumulation of extracellular hyaluronan by hyaluronan synthase 3 promotes tumor growth and modulates the pancreatic cancer microenvironment,” BioMed Research International, vol. 2014, Article ID 817613, 15 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. D. da Silva Freitas and J. Abrahão-Neto, “Biochemical and biophysical characterization of lysozyme modified by PEGylation,” International Journal of Pharmaceutics, vol. 392, no. 1-2, pp. 111–117, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Mero, M. Schiavon, F. M. Veronese, and G. Pasut, “A new method to increase selectivity of transglutaminase mediated PEGylation of salmon calcitonin and human growth hormone,” Journal of Controlled Release, vol. 154, no. 1, pp. 27–34, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. O. Schiavon, P. Caliceti, P. Ferruti, and F. M. Veronese, “Therapeutic proteins: a comparison of chemical and biological properties of uricase conjugated to linear or branched poly(ethylene glycol) and poly(N-acryloylmorpholine),” II Farmaco, vol. 55, no. 4, pp. 264–269, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Werle and A. Bernkop-Schnürch, “Strategies to improve plasma half life time of peptide and protein drugs,” Amino Acids, vol. 30, no. 4, pp. 351–367, 2006. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Schlapschy, U. Binder, C. Börger et al., “PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins,” Protein Engineering, Design and Selection, vol. 26, no. 8, pp. 489–501, 2013. View at Publisher · View at Google Scholar · View at Scopus
  21. J. Wu, “New stories on protein modification,” Journal of Molecular Cell Biology, vol. 8, no. 1, pp. 1–1, 2016. View at Publisher · View at Google Scholar
  22. A. Mire-Sluis, D. French, J. Mercer, G. Kleemann, and J. Dougherty, “Drug products for biological medicines: novel delivery devices, challenging formulations, and combination products, part 1,” BioProcess International, vol. 11, no. 4, pp. 48–62, 2013. View at Google Scholar · View at Scopus
  23. Working Group on the Summit on Combination Therapy for Cardiovascular Diseases, “Combination pharmacotherapy to prevent cardiovascular disease: present status and challenges,” European Heart Journal, vol. 35, no. 6, pp. 353–364, 2014. View at Publisher · View at Google Scholar
  24. T. Muller-Spath, N. Ulmar, L. Aumann et al., “Purifying common light-chain bispecific antibodies. A twin-column, countercurrent chromatography platform process,” BioProcess International, vol. 11, no. 5, pp. 36–44, 2013. View at Google Scholar
  25. Z. Wei, E. Shacter, M. Schenerman, J. Dougherty, and L. D. McLeod, “The role of higher-order structure in defining biopharmaceutical quality,” BioProcess International, vol. 9, no. 4, pp. 58–66, 2011. View at Google Scholar · View at Scopus
  26. I. F. Cooper and M. S. Siadaty, “Amino acids, peptides, or proteins associated with glycosaminoglycans binding,” BioMedLib Review, vol. 705, pp. 864–909, 2014. View at Google Scholar
  27. I. F. Cooper and M. S. Siadaty, “Therapeutic or preventive procedures associated with prourokinase,” BioMedLib Review, vol. 705, pp. 305–490, 2014. View at Google Scholar
  28. I. F. Cooper and M. S. Siadaty, “Enzymes associated with cell coat,” BioMedLib Review, vol. 705, pp. 371–894, 2014. View at Google Scholar
  29. A. V. Maksimenko, “Extracellular oxidative damage of vascular walls and their protection using antioxidant enzymes,” Pharmaceutical Chemistry Journal, vol. 41, no. 5, pp. 235–243, 2007. View at Publisher · View at Google Scholar · View at Scopus
  30. A. V. Maksimenko and A. V. Vavaev, “Antioxidant enzymes as potential targets in cardioprotection and treatment of cardiovascular diseases. Enzyme antioxidants: the next stage of pharmacological counterwork to the oxidative stress,” Heart International, vol. 7, no. 1, pp. 14–19, 2012. View at Publisher · View at Google Scholar · View at Scopus
  31. H. N. Siti, Y. Kamisah, and J. Kamsiah, “The role of oxidative stress, antioxidants and vascular inflammation in cardiovascular disease (a review),” Vascular Pharmacology, vol. 71, pp. 40–56, 2015. View at Publisher · View at Google Scholar · View at Scopus
  32. A. V. Maksimenko, “Experimental antioxidant biotherapy for protection of the vascular wall by modified forms of superoxide dismutase and catalase,” Current Pharmaceutical Design, vol. 11, no. 16, pp. 2007–2016, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. J. Carillon, J.-M. Rouanet, J.-P. Cristol, and R. Brion, “Superoxide dismutase administration, a potential therapy against oxidative stress related diseases: several routes of supplementation and proposal of an original mechanism of action,” Pharmaceutical Research, vol. 30, no. 11, pp. 2718–2728, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. S. Ekelof, S. E. Jensen, J. Rosenberg, and I. Gogenur, “Reduced oxidative stress in STEMI patients treated by primary percutaneous coronary intervention and with antioxidant therapy: a systematic review,” Cardiovascular Drugs and Therapy, vol. 28, no. 2, pp. 173–181, 2014. View at Publisher · View at Google Scholar · View at Scopus
  35. A. V. Maksimenko and E. G. Tischenko, “Covalent modification of superoxide dismutase subunits by chondroitin sulfate,” Biochemistry (Moscow), vol. 62, no. 10, pp. 1163–1166, 1997. View at Google Scholar · View at Scopus
  36. A. V. Maksimenko and E. G. Tischenko, “Modification of catalase by chondroitin sulfate,” Biochemistry (Moscow), vol. 62, no. 10, pp. 1167–1170, 1997. View at Google Scholar · View at Scopus
  37. A. V. Maksimenko, V. L. Golubykh, and E. G. Tischenko, “The combination of modified antioxidant enzymes for anti-thrombotic protection of the vascular wall: the significance of covalent connection of superoxide dismutase and catalase activities,” Journal of Pharmacy and Pharmacology, vol. 56, no. 11, pp. 1463–1468, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. A. V. Vavaev, E. G. Tischenko, V. P. Mokh, and A. V. Maksimenko, “Effect of hydrogen peroxide on the tone of rat arterial fragment and its antioxidant protection with derivatives of catalase and superoxide dismutase,” Technol Living Systems, vol. 6, no. 3, pp. 26–32, 2009 (Russian). View at Google Scholar
  39. A. V. Maksimenko, A. V. Vavaev, L. I. Bouryachkovskaya et al., “Biopharmacology of enzyme conjugates: vasoprotective activity of supramolecular superoxide dismutase-chondroitin sulfate-catalase derivative,” Acta Naturae, vol. 2, no. 4, pp. 82–94, 2010. View at Google Scholar
  40. A. V. Maksimenko, A. V. Vavaeva, A. A. Abramov, A. V. Vavaev, and V. L. Lakomkin, “Medicative and preventive action of bienzyme superoxide dismutase-chondroitin sulfate-catalase conjugate at endotoxic shock,” Living Systems Technology, vol. 11, no. 2, pp. 35–44, 2014 (Russian). View at Google Scholar
  41. M. S. Yilmaz, W. R. Millington, and C. Feleder, “The preoptic anterior hypothalamic area mediates initiation of the hypotensive response induced by LPS in male rats,” Shock, vol. 29, no. 2, pp. 232–237, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. T. Münzel, T. Gori, R. M. Bruno, and S. Taddei, “Is oxidative stress a therapeutic target in cardiovascular disease?” European Heart Journal, vol. 31, no. 22, pp. 2741–2749, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. G. P. van Hout, S. J. Jansen of Lorkeers, K. E. Wever et al., “Translational failure of anti-inflammatory compounds for myocardial infarction: a meta-analysis of large animal models,” Cardiovascular Research, vol. 109, no. 2, pp. 240–248, 2016. View at Publisher · View at Google Scholar
  44. J. S. Bice, Y. Keim, J.-P. Stasch, and G. F. Baxter, “NO-independent stimulation or activation of soluble guanylyl cyclase during early reperfusion limits infarct size,” Cardiovascular Research, vol. 101, no. 2, pp. 220–228, 2014. View at Publisher · View at Google Scholar · View at Scopus
  45. S. Kimura, G.-X. Zhang, and Y. Abe, “Malfunction of vascular control in lifestyle-related diseases: oxidative stress of angiotensin II-induced hypertension: mitogen-activated protein kinases and blood pressure regulation,” Journal of Pharmacological Sciences, vol. 96, no. 4, pp. 406–410, 2004. View at Publisher · View at Google Scholar · View at Scopus
  46. V. G. Barauna, L. C. G. Campos, A. A. Miyakawa, and J. E. Krieger, “ACE as a mechanosensor to shear stress influences the control of its own regulation via phosphorylation of cytoplasmic ser1270,” PLoS ONE, vol. 6, no. 8, Article ID e22803, 2011. View at Publisher · View at Google Scholar · View at Scopus
  47. I. Fleming, K. Kohlstedt, and R. Busse, “New fACEs to the renin-angiotensin system,” Physiology, vol. 20, no. 2, pp. 91–95, 2005. View at Publisher · View at Google Scholar · View at Scopus
  48. C. Scott, “Speeding development and lowering costs while enhancing quality: a BPI theater roundtable at the 2015 BIO convention,” BioProcess International, vol. 13, supplement 4, pp. 23–25, 2015. View at Google Scholar · View at Scopus