350 rub
Journal №1 for 2013 г.
Article in number:
Investigation of basic pharmacokinetic properties of L-lysine-α-oxidase
Authors:
E.V. Lukasheva, А.N. Lukashev, V.S. Pokrovsky, H.М. Treshalina, Е.Yu. Shumilina, А.Yu. Arinbasarova, А.G.Medentsev, Т.Т. Berezov
Abstract:
ELISA assay was developed for quantitative definition of antitumor enzyme L-lysine-α-oxidase (LO) in mouse serum. After intravenous administration of LO in single doses of 1.0-3.0 mg/kg (95-285 U/kg) the pharmacokinetic profile was nonlinear with two evident phases. LO basic pharmacokinetic parameters: Cl - 0.05-0.1 ml/min; T1/2 - 1.05-1.55 h were comparable with those of E. coli L-asparaginase, which is presently used in clinical cancer therapy. The pharmacokinetic profile of LO after multiple administrations (five doses with 48 h interval) was similar to the pharmacokinetic parameters upon a single injection.
Pages: 57-62
References
  1. TreshalinaH.M., LukashevaE.V., SedakovaL.A., etal.Anticancer enzyme L-lysine α-oxidase. Properties and application perspectives // Appl. Biochem. Biotechnol. 2000. № 84. Р. 267-273.
  2. Kusakabe H., Kodama K.,Kuninaka A. et al. A new antitumor enzyme, L-lysine-alpha-oxydase from Trichoderma viride // J. Biol Chem. 1980. № 255(3). Р. 976-981.
  3. Лукашева Е.В., Березов Т.Т. L-лизин-альфа-оксидаза: физико-химические и биологические свойства // Биохимия. 2002. Т. 67. № 10. С. 1394-1402.
  4. Трещалина Е.М. Противоопухолевая активность веществ природного происхождения. М. 2005. 270 с.
  5. Березов Т.Т.Молекулярные и биохимические основы энзимотерапии опухолей // Биомедицинская химия. 2005. № 51. С. 235-247.
  6. Жукова О.С., Хадуев С.Х., Добрынин Я.В. и др. Влияние L-лизин-aоксидазы на кинетику клеточного цикла культивируемых клеток лимфомы Беркитта // Экспериментальная онкология. 1985. Т. 7. № 6. С. 42-44.
  7. Dedrick R.L. Animal scale-up // J. Pharmacokinet. Biopharm. 1973. № 1. Р. 435-461.
  8. Asselin B.L., Whitin J.C., Coppola D.J., et al. Comparative pharmacokinetic studies of three asparaginase preparations // J. Clin. Oncol. 1993. V. 11. № 9. Р. 1780-1786.
  9. Lewis G.D., Figari I., Fendly B., et al.Differential responses of human tumor cell lines to anti-p185HER2 monoclonal antibodies // Cancer Immunol. Immunother. 1993. № 37. Р. 255-263.
  10. Keshishian H., Addona T., Burgess M., et al. Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution // Mol. Cell Proteomics. 2007. № 6. Р. 2212-2229.
  11. Chen Z., Liu R., Che J., et al.Qualitative and quantitative studies on human B7.1-Fc fusion protein and the application  in pharmacokinetic study in rhesus monkeys // J. Pharm. Biomed. Anal. 2011. V. 54. № 1. Р. 133-140.
  12. Wang W., Prueksaritanont T. Prediction of human clearance of therapeutic proteins: simple allometric scaling method revisited // Biopharm. Drug Dispos. 2010. V. 31. № 4. Р. 253-263.
  13. Puetter J., Flenker I. Investigations on Distribution and Elimination of administered L-Asparaginase. // Eur. J. Drug Metab. Pharmacokinet. 1976. V. 1. № 3. Р. 149-154.
  14. Kotzia G.A., Lappa K., Labrou N.E. Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage // Biochem. J. 2007. V. 404. № 2. Р. 337-343.