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Enhancement of potency and stability of human extracellular superoxide dismutase

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초록

Cells express several antioxidant enzymes to scavenge reactiveoxygen species (ROS) responsible for oxidative damages andvarious human diseases. Therefore, antioxidant enzymes areconsidered biomedicine candidates. Among them, extracellularsuperoxide dismutase (SOD3) had showed prominent efficacyagainst asthma and inflammation. Despite its advantages as abiomedicine, the difficulty in obtaining large quantity of activerecombinant human SOD3 (rhSOD3) has limited its clinicalapplications. We found that a significant fraction of overexpressedrhSOD3 was composed of the inactive apo-enzymeand its potency against inflammation depended on the rate ofmetal incorporation. Also, purified rhSOD3 was unstable andlost its activity very quickly. Here, we suggest an idealpreparative method to express, purify, and store highly activerhSOD3. The enzymatic activity of rhSOD3 was maximizedby incorporating metal ions into rhSOD3 after purification. Also, albumin or polyethylene glycol prevented rapidinactivation or degradation of rhSOD3 during preparativeprocedures and long-term storage.

Abstract

Cells express several antioxidant enzymes to scavenge reactiveoxygen species (ROS) responsible for oxidative damages andvarious human diseases. Therefore, antioxidant enzymes areconsidered biomedicine candidates. Among them, extracellularsuperoxide dismutase (SOD3) had showed prominent efficacyagainst asthma and inflammation. Despite its advantages as abiomedicine, the difficulty in obtaining large quantity of activerecombinant human SOD3 (rhSOD3) has limited its clinicalapplications. We found that a significant fraction of overexpressedrhSOD3 was composed of the inactive apo-enzymeand its potency against inflammation depended on the rate ofmetal incorporation. Also, purified rhSOD3 was unstable andlost its activity very quickly. Here, we suggest an idealpreparative method to express, purify, and store highly activerhSOD3. The enzymatic activity of rhSOD3 was maximizedby incorporating metal ions into rhSOD3 after purification. Also, albumin or polyethylene glycol prevented rapidinactivation or degradation of rhSOD3 during preparativeprocedures and long-term storage.

참고문헌 (34)

  1. Finkel T, "Radical medicine: treating ageing to cure disease", Nat Rev Mol Cell Biol, 6, pp.971~976 (2005)
  2. Rosanna DP, "Reactive oxygen species, inflammation, and lung diseases", Curr Pharm Des, 18, pp.3889~3900 (2012)
  3. Niwa Y, "Lipid peroxides and superoxide dismutase(SOD)induction in skin inflammatory diseases, and treatment with SOD preparations", Dermatologica, 179(1), pp.101~106 (1989)
  4. Kim BH, "Kurarinone regulates immune responses through regulation of the JAK", STAT and TCR-mediated signaling pathways, 2013, pp.85, 1134~1144
  5. Sunitha K, "N-Acetylcysteine amide: a derivative to fulfill the promises of N-Acetylcysteine", Free Radic Res, 47, pp.357~367 (2013)
  6. Traber MG, "Vitamins C and E: beneficial effects from a mechanistic perspective", Free Radic Biol Med, 51, pp.1000~1013 (2011)
  7. Yamakura F, "Post-translational modifications of superoxide dismutase", Biochim Biophys Acta, 1804, pp.318~325 (2010)
  8. Fridovich I, "Superoxide radical and superoxide dismutases", Annu Rev Biochem, 64, pp.97~112 (1995)
  9. Zelko IN, "Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression", Free Radic Biol Med, 33, pp.337~349 (2002)
  10. Lee YS, "Loss of Extracellular Superoxide Dismutase Induces Severe IL-23-Mediated Skin Inflammation in Mice", J Invest Dermatol, 133, pp.732~741 (2013)
  11. Asikainen TM, "Increased sensitivity of homozygous Sod2 mutant mice to oxygen toxicity", Free Radic Biol Med, 32, pp.175~186 (2002)
  12. Kwon MJ, "Superoxide dismutase 3 controls adaptive immune responses and contributes to the inhibition of ovalbumin-induced allergic airway inflammation in mice", Antioxid Redox Signal, 17, pp.1376~1392 (2012)
  13. Kwon MJ, "Superoxide dismutase 3 suppresses hyaluronic acid fragments mediated skin inflammation by inhibition of toll-like receptor 4 signaling pathway: superoxide dismutase 3 inhibits reactive oxygen species-induced trafficking of toll-like receptor 4 to lipid rafts", Antioxid Redox Signal, 16, pp.297~313 (2012)
  14. Tominaga T, "Exogenously-added copper", zinc superoxide dismutase rescues damage of endothelial cells from lethal irradiation, 2012, pp.50, 78~83
  15. 김대원, "Effect of silk fibroin peptide derived from silkworm Bombyx mori on the anti-inflammatory effect of Tat-SOD in a mice edema model", BMB Reports, 44(12), pp.787~792 (2011), 생화학분자생물학회
  16. Na K, "EC-SOD suppresses contact hypersensitivity in mouse skin by impairing Langerhans cell migration", J Invest Dermatol, 127, pp.1930~1937 (2007)
  17. Kim Y, "Regulation of skin inflammation and angiogenesis by EC-SOD via HIF-1alpha and NF-kappaB pathways", Free Radic Biol Med, 51, pp.1985~1995 (2011)
  18. Jaarsma D, "Human Cu", Zn superoxide dismutase(SOD1)overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1, 2000, pp.7, 623~643
  19. Uematsu T, "Pharmacokinetics and safety of intravenous recombinant human superoxide dismutase(NK341)in healthy subjects", Int J Clin Pharmacol Ther, 32, pp.638~641 (1994)
  20. Karlsson K, "Pharmacokinetics of extracellular-superoxide dismutase in the vascular system", Free Radic Biol Med, 14, pp.185~190 (1993)
  21. Bowler RP, "Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase", J Biol Chem, 277, pp.16505~16511 (2002)
  22. Enghild JJ, "The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis", J Biol Chem, 274, pp.14818~14822 (1999)
  23. Petersen SV, "The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis", Free Radic Biol Med, 49, pp.894~899 (2010)
  24. Jeney V, "Role of antioxidant-1 in extracellular superoxide dismutase function and expression", Circ Res, 96, pp.723~729 (2005)
  25. Ahl IM, "Coexpression of yeast copper chaperone(yCCS)and CuZn-superoxide dismutases in Escherichia coli yields protein with high copper contents", Protein Expr Purif, 37, pp.311~319 (2004)
  26. 김지인, "Endotoxin-induced renal tolerance against ischemia and reperfusion injury is removed by iNOS, but not eNOS, gene-deletion", BMB Reports, 43(9), pp.629~634 (2010), 생화학분자생물학회
  27. Adachi T, "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro", Free Radic Biol Med, 13, pp.205~210 (1992)
  28. Arai K, "Glycation and inactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites", J Biol Chem, 262, pp.16969~16972 (1987)
  29. Petersen SV, "The high concentration of Arg213-->Gly extracellular superoxide dismutase(EC-SOD)in plasma is caused by a reduction of both heparin and collagen affinities", Biochem J, 385, pp.427~432 (2005)
  30. Petersen SV, "The dual nature of human extracellular superoxide dismutase: one sequence and two structures", Proc Natl Acad Sci U S A, 100, pp.13875~13880 (2003)
  31. Tibell L, "Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product", Proc Natl Acad Sci U S A, 84, pp.6634~6638 (1987)
  32. Son YJ, "Expression, high cell density culture and purification of recombinant EC-SOD in Escherichia coli", Appl Biochem Biotechnol, 162, pp.1585~1598 (2010)
  33. Chen HL, "Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris", J Agric Food Chem, 54, pp.8041~8047 (2006)
  34. Bae JY, "Cu", Zn incorporation during purification of soluble human EC-SOD from E. coli stabilizes proper disulfide bond formation, 2013, pp.169, 1633~1647

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