Cross-linking of nuclear proteins to DNA by platinum compounds

• Autorzy: Walter Z. , Wozniak K. , Kowalik J.
• Języki publikacji: EN

Abstrakty

EN

In this work we investigated the lymphocyte nuclear proteins which participated in DNA-protein cross-links induced by three platinum compounds: cis-DDP, trans-DDP and carboplatin. Our studies indicated that many proteins were cross- linked to DNA in the intact cell. Trans-DDP was the most effective cross-linker. The cross-linking process depended on time of the cells incubation with aforementioned compounds. Carboplatin produced the DNA-protein cross-links more slowly and less effectively than cis-DDP. After incubation of the cells with cis-DDP, trans- DDP and carboplatin a similar protein pattern was obtained. In case of all compounds studied 34.5 kDa protein was abundantly represented.

Słowa kluczowe

EN

nuclear protein; carboplatin; cis-diamminedichloroplatinum; lymphocyte; cross-linking; platinum compound; DNA

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1997
• Tom: 02
• Numer: 4
• Opis fizyczny: p.371-378,fig.

Twórcy

autor

Walter Z.

• University of Lodz, Banacha 12-16, 90-237 Lodz, Poland

autor

Wozniak K.

autor

Kowalik J.

Bibliografia

• 1. Podlewski, J. K., and Chwalibogowska-Podlewska, A. Leki współczesnej terapii, 11 th edition, Split Trading, Buchner Fundation, 1993, 211-212.
• 2. Terheggen, P. M. A. B. Pharmaceutisch Weekblad Scientific edition 3 (1990) 119-120.
• 3. Guchelaar, H-J., de Vries, E. G. E., Meijer, C., Esselink, M. T., Vellenga, E., Uges, D. R. A. and Mulder, N. H. Pharmaceutical Res. 9 (1994) 1265-1269.
• 4. Fichtinger-Schepman, A. M. J., van der Veer, J. L., de Hartog, J. H. J., Lohman, P. H. M. and Reedijk, J. Biochemistry 24 (1985) 707-713.
• 5. Pinto, L. A. and Lippard, S. J. Biochim. Biophys. Acta 780 (1985) 167-180.
• 6. Caradonna, J. P. and Lippard, S. J. Adv. Chem. Ser. 209 (1983) 14-16.
• 7. Kasparkova, J. and Brabec, V. Biochemistry 34 (1995) 12379-12387.
• 8. Donahue, B. A., Augot, M., Bellon, S. F., Treiber, D. K., Toney, J. H., Lippard, S. J. and Essigmann, J. M. Biochemistry 29 (1990) 5872-5880.
• 9. Banjar, Z. M., Hnilica, L. S., Briggs, R. C., Stein, J. and Stein, G. Biochemistry 23 (1984) 1921-1926.
• 10. Oliński, R., Wedrychowski, A., Schmidt, W. N., Briggs, R. C. and Hnilica, L. S. Cancer Res. 47 (1987) 201-205.
• 11. Miller, Ch. A., Cohen, M. D. and Costa, M. Carcinogenesis 12 (1991) 269-276.
• 12. Ferraro, A., Grandi, P., Eufemi, M., Altieri, F. and Turano, C. FEBS Letters 307 (1992) 383-385.
• 13. Marples, B., Adomat, H., Billings, P. C., Farrell, N. P., Koch, C. J. and Skov, K. A. Anti-Cancer Drug Design 9 (1994) 389-399.
• 14. Boyum, A. Nature 204 (1964) 794.
• 15. Lowry, J. O. H., Rosenbrough, N. J., Farr, A. L. and Randall, R. J. J. Biol. Chem. 193 (1951) 265-275.
• 16. Laemmli, U. K. Nature 227 (1970) 680-685.
• 17. Wray, W., Boulikas, T., Wray, V. P. and Hancock, R. Anal. Biochem. 118 (1981) 197-203.
• 18. Oleinick, N. L, Chiu, S., Ramakrishnan, N. and Xue, L. Br. J. Cancer (Suppl. 8) 55 (1987) 135-140.
• 19. Plooy, A. C. M., Van Dijk, M. and Lohman, P. H. M. Cancer Res. 44 (1984) 2043-2051.
• 20. Hughes, E. N., Engelsberg, B. N. and Billings, P. C. J. Biol. Chem. 267 (1992) 13520-13527.
• 21. Locker, D., Decoville, M., Maurizot, J. C., Bianchi, M. E. and Leng, M. J. Mol, Biol. 246 (1995) 243-247.