Иммунотоксины, полученные на основе моно-и поликлональных антител и А-цепи рицина
Диссертация
Существует два основных способа получения активных высокоспецифических конъюгатов. В одном случае AT конъюгируют с целым токсином, в другой — с его ферментативной частью. Цитотоксичес-кая активность конъюгатов, содержащих целый токсин, как правило, выше (см. Табл. 4). Но для достижения специфичности действия таких конъюгатов в среду необходимо добавлять, например, в случае рицина, лактозу или… Читать ещё >
Содержание
- ВВЕДЕНИЕ
- ГЛАВА I. ШШЮТОКСИШ. Обзор литературы
- 1. 1. Использование антител в качестве векторов иммунотоксинов
- 1. 1. 1. Особенности использования поликлональных антител, их F (ab)2- и Раь-фрагментов. I0-II
- 1. 1. 2. Новые возможности, связанные с применением моноклональных антител
- 1. 2. Токсины, использующиеся для конъюгации с антителами
- 1. 2. 1. Преимущества токсинов белковой природы
- 1. 2. 2. Структура белковых токсинов
- 1. 2. 3. Механизм действия токсинов
- 1. 3. Методы конъюгации белковых токсинов и антител
- 1. 3. 1. Методы конъюгирования целых токсинов и антител
- 1. 3. 2. Методы получения конъюгатов, содержащих А-цепь токсинов
- 1. 3. 3. Другие способы получения иммунотоксинов
- 1. 4. Механизм проникновения внутрь клетки А-цепи
- 1. 5. Изучение действия иммунотоксинов в культуре клеток
- I. 5. I. Действие ИТ, содержащих антитела к целым клеткам
- 1. 5. 2. Цитотоксические свойства ИТ, содержащих поликлональные антитела к антигенам клеточной поверхности
- 1. 5. 3. Ингибирующая активность ИТ, содержащих моноклональные антитела к отдельным цепям ig и искусственным антигенам, расположенным на поверхности клеток-мишеней
- 1. 5. 4. Действие ИТ, содержащих моноклональные антитела к опухолево-специфическим, диф-ференцировочным и другим антигенам
- 1. 6. Использование иммунотоксинов для ингибиро-вания опухолевого роста
- 1. 6. 1. Удаление опухолевых клеток из смеси обработкой ИТ с последующим возвращением донору
- 1. 6. 2. Действие ИТ на раковые клетки у безтимусных мышей
- 1. 6. 3. Применение ИТ при прямом подавлении роста опухоли
- 1. 7. Модуляция специфического иммунного ответа с помощью иммунотоксина
- 1. 8. Что ограничивает эффективность действия иммунотоксинов
- 1. 1. Использование антител в качестве векторов иммунотоксинов
Список литературы
- Raso V., Griffin T. Specific cytotoxicity of a human immunoglobulin directed Fab'-ricin A chain conjugate. J. Immunol. 1980, v. 125, pp 2610−2616.
- Vitteta E.S., Krolick K.A., Miyama-Inaba M., Cushley W., Uhr J.W. Immunotoxins: A new approach to cancer therapy. Science, 1983, v. 219, pp. 644−650.
- Masuho Y., Нага T. Target-cell cytotoxicity of a hybrid of Fab' of immunoglobulin and A-chain of ricin. Gann: Jap. J. Cancer Res., 1980, v. 71, pp. 759−765.
- Raso V. Antibody mediated delivery of toxic molecules to antigen bearing target cells. Immunol. Rev., 1982, v. 62, pp. 93−117.
- Youle R.J., Neville D.M. Jr. Anti-Thy 1.2 monoclonal antibody linked to ricin is a potent cell-type specific toxin. -Proc. Natl. Acad. Sci. USA, 1980, v. 77, pp. 5483−5486.
- Krolick K.A., Villemez C., Isakson P., Uhr J. WVetteta E.S. Selective killing of normal or neoplastic В cells L antibodies coupled to the A-chain of ricin. Proc. Natl. Acad. Sci. USA, v. 77, pp. 5419−5423.
- Trowbridge I.S., Domingo D.L. Anti-transferrin receptor monoclonal antibody and toxin-antibody conjugates affect, v growth of human tumour cells. Nature, 1981, v. 294, p.171−173.
- Youle R.J., Neville D.M.Jr. Kinetics of protein synthesis inactivation by ricin-anti-Thy 1.1 monoclonal antibody hybrids. J. Biol. Chem., 1982, v. 257, pp. 1598−1601.
- Ghose Т., Blair A.H. Antibody-linked cytotoxic agents in the treatment of cancer: current status and future prospects.
- J. Natl. Cancer Inst., 1978, v. 61, pp. 657−676.
- Arnon R., Sela M. Targeted chemotherapy: drugs conjugated to anti-tumor antibodies. Cancer Surveys, 1982, v. 1, pp. 429−449.
- Moolten F.L., Schreiber B.M., Zajdel S.H. Antibodies cun-jugated to potent cytotoxins as specific antitumor agents. Immunol. Rev., 1982, v. 62, pp. 47−73.
- Yamaizumi M., Mekada E., Uchida Т., Okada Y. One molecule of diphteria toxin fragment A introduced into a cell can kill the cell. Cell, 1978, v. 15, pp. 245−250.
- Eiklid K., Olsnes S., Pikl A. Entry of lethal doses of abrin, ricin and modeccin into the cytosol of HeLa cells. Exp. Cell Res., 1980, v. 126, pp. 321−326.
- Thorpe P.E., Ross W.C.J., Brown A.N.F., Myers C.D., Cumber A.J., Foxwell B.M.J., Forrester J.T. Blockade of the galactose-binding sites of ricin by its lankage to antibody. Eur. J. Biochem., v. 140, pp. 63−71.
- Pappenheiraer A.M.Jr. Diphteria toxin. Ann. Rev. Biochem., 1977, v. 46, pp. 69−94.
- Roberts W.K., Stewart T.S. Purification and properties a translation inhibitor from wheat germ. Biochemistry, 1979, v. 18, pp. 2615−2621.
- Stirpe F., Pession-Brizzi A., Lozenroni E., Strocchi P., Montanaro L., Sperti S. Studies on the proteins from the seeds of Croton tiglium and of Jatropha Curcas. Biochem. J., 1976, v. 156, pp. 1−6.
- Gasperi-Campani A., Barbieri L., Morelli P., Stirpe F. Seed extracts inhibiting protein synthesis in vitro. Biochem. J., 1980, v. 186, pp. 439−441.
- Van Ness B.G., Howard J.В., Bodley J.W. ADP-ribosylation of elongation factor 2 by diphteria toxin. NMR spectra and proposed structured of ribosyldiphthamide and its hybrolysis products. J. Biol. Chem., 1980, v. 255, pp 10 710−10 716.
- Moolten F.L., Cooperband S.R. Selective destruction of target cells by diphtheria toxin conjugated to antibody directed against antigens on the cells. Science, 1970, v. 169, pp. 68−70.
- Moolten F.L., Zajdel S., Cooperband S. Immunotherapy of experimental animal tumors with antitumor antibodies conjugated to diphteria toxin or ricin. Ann. N.Y. Acad. Sci., 1976, v. 277, p. 690.
- Moolten F.L., Capparell N.J., Cooperband S.R. Antitumor effects of antibody-diphteria toxin conjugates: use of hapten-coated tumor cells as an antigenic target. J. Natl. Cancer Inst., 1972, v. 49, pp. 1057−1062.
- Thorpe P.E., Ross W.C.J., Cumber A.J., Hinson C.A., Edwards D.C., Davies A.J.S. Toxicity of diphtheria toxin for lymphoblastoid cells is increased by conjugation to antilymphocytic globulin. Nature, 1978, v. 271, pp. 752−755.
- Edwards D.C., Smith A., Ross W.C.J., Cumber A.J., Thorpe P.E. Davies A.J.S. The effect of abrin, anti-lymphocyte globulin and their conjugates on the immune response of mice to sheep red blood cells. Experientia, 1981, v. 37, pp. 256−259.
- Thorpe P.E., Ross W.C.J. The preparation and cytotoxic properties of antibody-toxin conjugates. Immunol. Rev., 1982, v. 62, pp. 119−158.
- Neville D.M., Youle R.J., Monoclonal antibody ricin or ricin A-chain hybrids: kinetic analysis of cell killing for tumor therapy. Immunol. Rev., 1982, v. 62, pp. 75−91.
- Sandvig K., Olsnes S., Pihl A. Chemical modifications of the toxic lectins abrin and ricin. Eur. J. Biochem., 1978, v. 84, pp. 323−331.
- Miyazaki H., Beppu M., Terao Т., Osawa T. Preparation of antibody (JgG)-ricin A chain conjugate and its biological activity. Gann: Jap. j. Cancer Res., 1980, pp. 766−774.
- Gilliland G.D., Collier J, R. A model system involving anti-concanavalin A for antibody targeting of diphtheria toxin fragment A. Cancer Res., 1980, v. 40, pp. 3564−3569.
- Masuho Y., Нага Т., Noguchi T. Preparation of hybrid of fragment Fab' of antibody and fragment A of diphtheria toxin and its cytotoxicity. Biochem. Biophys. Res. Commun., 1979, v. 90, p. 320−326.
- Martinez 0., Wallace E.F., Wofsy L. Preparation of disulfide- linked conjugates of fragment A of diphtheria toxin with biotin, avidin and antibodies. Fed. Proc. Fed. Amer. Soc. Exp. Biol., 1980, v. 39, p. 719.
- Martinez 0., Kimura J., Gottfried T.D., Seicher M., Wofsy L. Variance in cytotoxic effectiveness of antibody-toxin A hybrids. Cancer Surveys, 1982, v. 1, pp. 373−388.
- Raso V., Griffin T. Hybrid antibodies with dual specificity for the delivery of ricin to immunoglobulin-bearing target cells. Cancer Res., 1981, v. 41, pp. 2073−2078.
- Nisonoff A., Rivers Mi.M. Recombination of mixture of un-valent antibody fragments of different specificity. Arch. Biochem. Biophys., 1961, v. 93, pp. 460−467.
- Delfini C., Amici C., Belardelli F., Oberholtzez G., Sorrentino M. Concanavalin A induced inhibition of abrin and ricin activity parallel with a decrease of the number of toxin-binding uptake-elution cycles. Exp. Cell Res., 1982, v. 142, pp. 427−435.
- Sargiacomo M., Hughes R.C. A cytotoxic, photolabile cross-linking derivative of ricin. Exp. Cell Res., 1982, v. 142, pp. 283−292.
- Olsnes S., Pihl A. Abrin, ricin and their associated agglutinins. In: The specificity and Action of Animal, Bacterial and Plant Toxins. Receptors and Recognition, series B. ed. Cuatrecasas P., Chapman and Hall. London, 1976, v. 1, pp. 129−161.
- Raso V., Lawrence J. Carboxylic ionophores enhance the cytotoxic potency of ligand and antibody-delivered ricin A chain. J. Exp. Med., 1984, v. 160, pp. 1234−1240.
- Vitetta E.S., Cushley W., Uhr J.W. Synergy of ricin A chain containing immunotoxins and ricin В chain-containing immunotoxins in vitro, killing of neoplastic human В cells. Proc. Natl. Acad. Sci. USA, v. 80, pp. 6332−6335.
- Vitetta E.S., Fulton J.R., Uhr J.W. Cytotoxicity of a cell-reactive immunotoxin containing ricin A chain is potentiated by an anti-immunotoxin containing ricin В chain. J. Exp. Med., 1984, v. 160, pp. 341−346.
- Fu S.M., Winchester R.J., Kunkel H.G. Occurence of surface IgM, IgD and free light chains on human lymphocytes. J. Exp. Med., 1974, v. 139, pp. 451−458.
- Filippa D.A., Lieberman P.H., Erlandson R.A., Koziner В., Siegel F.P., Turnbull A., Zimring A., Good R.A. A study of malignant lymphomas using light and ultramicroscopic, cytochemical and immunologic tehnics. Amer. J. Med., 1978, v. 64, pp. 259−266.
- De Petris S., Faff M.C. Normal distribution, patching and capping of lymphocyte surface immunoglobulin studies by electron microscopy. Nature, New Biol., 1973, v. 241, pp. 257−259.
- Uhr J.W., Vitetta E.S. The use of ricin A-chain-containing immunotoxins to kill neoplastic В cells. In: Progress in immunology, Academic Press, 1983, v. 5, pp. 1409−1416.
- Casellas P., Carriere D., Gros 0., Laurent J.C., Poncelet P. Jansen F.K. Properties of antibody-ricin A chain conjugates (immunotoxins) in specific cell killing. In: Bacterial Protein Toxins. Academic Press, 1983, pp. 28−36.
- Blythman H.E., Casellas P., Gros 0., Gros P., Jansen F.K., Paolucci F., Pau В., Vidal H. Immunotoxins: hybrid molecules of monoclonal antibodies and toxin subunit specifically kill tumor cells. Nature, 1981, v. 290, pp. 145−146.
- Thorpe P.E., Mason D.W., Brown A.N.F., Simmonds S.J., Ross W.C.J., Cumber A.J., Forrester J.A. Selective killing of malignant cells in a leukaemic rat bone marrow using an antibody-ricin conjugate. Nature, 1982, v. 297, pp.594−596.
- Raso V., Ritz J., Basala M., Schlossman S.F. Monoclonal antibody-ricin A chain conjugate selectively cytotoxic for cells bearing the common acute lymphoblastic leukemia antigen. Cancer Res., 1982, v. 42, pp. 457−464.
- Krolick K.A., Yuan D., Vitetta E.S. Specific killing of a human breast carcinoma cell line by a monoclonal antibody coupled to the A-chain of ricin. Cancer Immunol. Immunother., 1981, v. 12, pp. 39−41.
- Osawa Т., Watanabe Y., Yamaguchi Т., Miyazaki H. Preparation and cytotixic properties of concanavalin A- and anti-car cinoembryonic antigen antibody-ricin A chain conjugates. Cancer Surveys, 1982, v. 1, pp. 353−372.
- Bumol T.F., Wang Q.C., Reisfeld R.A., Kaplan N.O. Monoclonal antibody and an antibody-toxin conjugate to a cell surface proteoglycan of melanoma cells suppress in vivo tumor growth. Proc. Natl. Acad. Sci. USA, 1983, v. 80, pp. 529−533.
- Mason D.W., Thorpe P.E., Ross W.C.J. Elimination of leukemic cells from rodent bone marrow in vitro with antibo-dy-ricin conjugates: implications for autologous marrow transplantation in man. Cancer Surveys, 1982, v. 1, pp. 389−415.
- Volkman D.J., Atteg Ahmad, Fauci A.S., Neville D.M.Jr. Selective abrogation of antigen-specific human B-cell responses by antigen-ricin conjugates. J. Exp. Med., 1982, v. 156, pp. 634−639.
- Moolten F.L., Capparell N.J., Zajdel S.H. Antitumor effects of antibody-diphtheria toxin conjugates. III. Cyclophos-phamide-induced immune unresponsiveness to conjugates.
- J. Natl. Cancer Inst., 1975, v. 55, pp. 709−712.
- Nicolson V.E., Blaustein J. The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces. Biochem. biophys. acta, 1972, v. 266, pp. 543−547.
- Olsnes S., Pihl A. Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis. Biochemistry, 19 83, v. 12, pp. 3121−3126.
- Anderson C.W., Baum P.R., Gesteland R.F. SDS-gel-electro-phoresis of proteins. J. Virol., 1973, v. 12, pp. 241−254.
- Ramakrishnan S., Eagle M.R., Honston L.L. Radioimmunoassay of ricin A- and B-chains applied to samples of ricin A-chain prepared by chromatofocusing and by DEAE Bio-Gel A chromatography. Bioch. Biophys. Acta, 1982, v. 719, pp. 341−348.
- Jones V.E. Isolation of pure normal IgG from mouse serum. Immunology, 1969, v. 16, pp. 589−592.
- Bale W.F., Helkamp R.W., Izzo M.J., Contreras M.A., Spar131
- L. High specific activity labeling of protein with I by the iodine monochloride method. Proc. Soc. Exp. Biol. Med., 1966, v. 122, pp. 407−414.
- Рохлин O.B., Незлин P.С. Определение антигенов с помощью фиксированных на целлюлозе чистых антител. Вопросы мед. хим., 1969, т. 15, W k, стр. 439-^1.
- Carlsson J., Drebin Н., Axen R. Protein thiolation and reversible protein-protein conjugation. Biochem. J., 1978, v. 173, pp. 723−737.
- Till G.E., McCullach E.A. A direct measurement of radiation sensivity of mouse bone marrow cells. Radiat. Res., 1961, v. 14, pp. 213−217.
- Gray J.W., Coffino P. Cell cycle analysis by flow cytometry. In: Methods in Enzymology. Cell Culture. Eds. Jakoby В., Pastan I.H. N.Y. etc: Academic Press, 1979, v. 58, pp. 233−248.
- Bradford M.M. A rapid and sensitive method for quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 1976, v. 72, pp. 248−254.-!Тзб1
- Towbin Н., Staehelin Т., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some application. Proc. Natl. Acad. Sci. USA, 1979, v. 76, pp. 4350−4354.
- Kearney J.F., Radbrush A. Liesegang В., Rajewsky K.
- A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol., 1979, v. 123, p. 1548.
- Ирлин И. С, Тихонова З. Н. Розинова Э.Н., Макарова Г. Ф., Колобков С. Л., Иевлева Е. С. Получение и свойства самоподдерживающейся суспензионной культуры мышиных эритробластов. Пробл. гематол., 1977, т. 9, стр. k2-k6.
- Ievleva E.S., Engelhardt N.V., Abelev G.I., Specific antigen of murine erythroblast. Int. J. Cancer, 1976, v. 17, pp. 798−805.
- Иевлева E.C., Энгельгардт H.B., Абелев Г. И. Эритроидный антиген у мышей с вирусными лейкозами. Бюлл. Экс. Биол. Мед., 197^, т. 6, стр. 82−84.
- Мечетнер Е.Б., Розинова Э. Н., Ирлин И. С. Свойства клоногенн генных клеток самоподдерживающихся штаммов эритробластов Раушера. Пробл. гематол., 1978, т. 10, стр. 26−28.
- Розинова Э.Н., Ирлин И. С. Получение самоподдерживающихся линий эритробластоза у мышей AKR. Пробл. гематол., 1977, т. 9, стр. hG-kS.
- Мечетнер Е.Б., Иевлева Е. С., Розинова Э. Н., Ирлин И. С., Чижевская М. А. Свойства и идентификация клоногенных клеток лейкоза Раушера. Пробл. гематол., 1979, т. 9, стр. 51−59.