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. 1996 Jun;73(11):1323–1327. doi: 10.1038/bjc.1996.253

Altered biodistribution of an antibody--enzyme conjugate modified with polyethylene glycol.

E A Eno-Amooquaye 1, F Searle 1, J A Boden 1, S K Sharma 1, P J Burke 1
PMCID: PMC2074478  PMID: 8645574

Abstract

Polyethylene glycol modification of the antibody--enzyme conjugate, F(ab')2-A5B7-CPG2, extends its duration in the circulation of nude mice bearing human colonic cancer xenografts (LS174T). Increased concentration of modified conjugate is achieved in the tumour, but residual non-specific enzyme concentrations in normal tissue and blood demonstrate the fundamental requirement to remove or inactivate non-specifically held enzyme in this system.

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Selected References

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  1. Abuchowski A., van Es T., Palczuk N. C., Davis F. F. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J Biol Chem. 1977 Jun 10;252(11):3578–3581. [PubMed] [Google Scholar]
  2. Bagshawe K. D., Sharma S. K., Springer C. J., Rogers G. T. Antibody directed enzyme prodrug therapy (ADEPT). A review of some theoretical, experimental and clinical aspects. Ann Oncol. 1994 Dec;5(10):879–891. doi: 10.1093/oxfordjournals.annonc.a058725. [DOI] [PubMed] [Google Scholar]
  3. Berger H., Jr, Pizzo S. V. Preparation of polyethylene glycol-tissue plasminogen activator adducts that retain functional activity: characteristics and behavior in three animal species. Blood. 1988 Jun;71(6):1641–1647. [PubMed] [Google Scholar]
  4. Chen R. H., Abuchowski A., Van Es T., Palczuk N. C., Davis F. F. Properties of two urate oxidases modified by the covalent attachment of poly(ethylene glycol). Biochim Biophys Acta. 1981 Aug 13;660(2):293–298. doi: 10.1016/0005-2744(81)90173-x. [DOI] [PubMed] [Google Scholar]
  5. Fraker P. J., Speck J. C., Jr Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem Biophys Res Commun. 1978 Feb 28;80(4):849–857. doi: 10.1016/0006-291x(78)91322-0. [DOI] [PubMed] [Google Scholar]
  6. Habeeb A. F. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal Biochem. 1966 Mar;14(3):328–336. doi: 10.1016/0003-2697(66)90275-2. [DOI] [PubMed] [Google Scholar]
  7. Katre N. V., Knauf M. J., Laird W. J. Chemical modification of recombinant interleukin 2 by polyethylene glycol increases its potency in the murine Meth A sarcoma model. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1487–1491. doi: 10.1073/pnas.84.6.1487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Melton R. G., Boyle J. M., Rogers G. T., Burke P., Bagshawe K. D., Sherwood R. F. Optimisation of small-scale coupling of A5B7 monoclonal antibody to carboxypeptidase G2. J Immunol Methods. 1993 Jan 14;158(1):49–56. doi: 10.1016/0022-1759(93)90257-8. [DOI] [PubMed] [Google Scholar]
  9. Melton R. G., Wiblin C. N., Baskerville A., Foster R. L., Sherwood R. F. Covalent linkage of carboxypeptidase G2 to soluble dextrans--II. In vivo distribution and fate of conjugates. Biochem Pharmacol. 1987 Jan 1;36(1):113–121. doi: 10.1016/0006-2952(87)90388-1. [DOI] [PubMed] [Google Scholar]
  10. Pedley R. B., Boden J. A., Boden R., Begent R. H., Turner A., Haines A. M., King D. J. The potential for enhanced tumour localisation by poly(ethylene glycol) modification of anti-CEA antibody. Br J Cancer. 1994 Dec;70(6):1126–1130. doi: 10.1038/bjc.1994.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rogers G. T., Burke P. J., Sharma S. K., Koodie R., Boden J. A. Plasma clearance of an antibody--enzyme conjugate in ADEPT by monoclonal anti-enzyme: its effect on prodrug activation in vivo. Br J Cancer. 1995 Dec;72(6):1357–1363. doi: 10.1038/bjc.1995.515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Sharma S. K., Bagshawe K. D., Burke P. J., Boden J. A., Rogers G. T., Springer C. J., Melton R. G., Sherwood R. F. Galactosylated antibodies and antibody-enzyme conjugates in antibody-directed enzyme prodrug therapy. Cancer. 1994 Feb 1;73(3 Suppl):1114–1120. doi: 10.1002/1097-0142(19940201)73:3+<1114::aid-cncr2820731352>3.0.co;2-l. [DOI] [PubMed] [Google Scholar]
  13. Sharma S. K., Bagshawe K. D., Springer C. J., Burke P. J., Rogers G. T., Boden J. A., Antoniw P., Melton R. G., Sherwood R. F. Antibody directed enzyme prodrug therapy (ADEPT): a three phase system. Dis Markers. 1991 May-Aug;9(3-4):225–231. [PubMed] [Google Scholar]
  14. Sherwood R. F., Melton R. G., Alwan S. M., Hughes P. Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method. Eur J Biochem. 1985 May 2;148(3):447–453. doi: 10.1111/j.1432-1033.1985.tb08860.x. [DOI] [PubMed] [Google Scholar]
  15. Sung C., Youle R. J., Dedrick R. L. Pharmacokinetic analysis of immunotoxin uptake in solid tumors: role of plasma kinetics, capillary permeability, and binding. Cancer Res. 1990 Nov 15;50(22):7382–7392. [PubMed] [Google Scholar]
  16. Veronese F. M., Largajolli R., Boccù E., Benassi C. A., Schiavon O. Surface modification of proteins. Activation of monomethoxy-polyethylene glycols by phenylchloroformates and modification of ribonuclease and superoxide dismutase. Appl Biochem Biotechnol. 1985 Apr;11(2):141–152. doi: 10.1007/BF02798546. [DOI] [PubMed] [Google Scholar]
  17. Wagener C., Clark B. R., Rickard K. J., Shively J. E. Monoclonal antibodies for carcinoembryonic antigen and related antigens as a model system: determination of affinities and specificities of monoclonal antibodies by using biotin-labeled antibodies and avidin as precipitating agent in a solution phase immunoassay. J Immunol. 1983 May;130(5):2302–2307. [PubMed] [Google Scholar]

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