Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase
α-Difluoromethylornithine (DFMO), the specific and irreversible inhibitor of ornithine decarboxylase (ODC), was able to induce the arrest of proliferation in Leishmania mexicana and ODC-transformed Trypanosoma cruzi cultures grown in a semi-defined medium essentially free of polyamines. Conversely,...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
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Academic Press Inc.
2000
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 12832caa a22011417a 4500 | ||
|---|---|---|---|
| 001 | PAPER-2125 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203131.0 | ||
| 008 | 190411s2000 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0034694943 | |
| 024 | 7 | |2 cas |a eflornithine, 67037-37-0, 70052-12-9; ornithine decarboxylase, 9024-60-6; spermidine, 124-20-9, 334-50-9; trypanothione, 96304-42-6 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BBRCA | ||
| 100 | 1 | |a Carrillo, C. | |
| 245 | 1 | 0 | |a Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase |
| 260 | |b Academic Press Inc. |c 2000 | ||
| 270 | 1 | 0 | |m Algranati, I.D.; Instituto de Invest. Bioquím., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires/CONICET, A. Machado 151, 1405 Buenos Aires, Argentina; email: algra@iib.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Coons, T., Hanson, S., Bitonti, A.J., McCann, P.P., Ullman, B., α-Difluoromethylornithine resistance in Leishmania donovani is associated with increased ornithine decarboxylase activity (1990) Mol. Biochem. Parasitol., 39, pp. 77-90 | ||
| 504 | |a González, N.S., Sánchez, C.P., Sferco, L., Algranati, I.D., Control of Leishmania mexicana proliferation by modulation of polyamine intracellular levels (1991) Biochem. Biophys. Res. Commun., 180, pp. 797-804 | ||
| 504 | |a Li, F., Hua, S., Wang, C.C., Gottesdiener, K.M., Procyclic Trypanosoma brucei cell lines deficient in ornithine decarboxylase activity (1996) Mol. Biochem. Parasitol., 78, pp. 227-236 | ||
| 504 | |a Algranati, I.D., Sánchez, C.P., González, N.S., (1990), pp. 137-146. , The Biology and Chemistry of Polyamines (Goldemberg, S. H., and Algranati, I. D., Eds.), IRL Press, Oxford; Hunter, K.J., Le Quesne, S.A., Fairlamb, A.H., Identification and biosynthesis of N1,N9-bis(glutathionyl) amino-propilcadaverine (homotrypano-thione) in Trypanosoma cruzi (1994) Eur. J. Biochem., 226, pp. 1019-1027 | ||
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| 504 | |a González, N.S., Ceriani, C., Algranati, I.D., Differential regulation of putrescine uptake in Trypanosoma cruzi and other trypanosomatids (1992) Biochem. Biophys. Res. Commun., 188, pp. 120-128 | ||
| 504 | |a Le Quesne, S.A., Fairlamb, A.H., Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes (1996) Biochem. J., 316, pp. 481-486 | ||
| 504 | |a Pegg, A.E., (1989), pp. 21-34. , Ornithine Decarboxylase: Biology, Enzymology, and Molecular Genetics (Hayashi, S., Ed.), Pergamon Press, New York; Hayashi, S., Murakami, Y., Rapid and regulated degradation of ornithine decarboxylase (1995) Biochem. J., 306, pp. 1-10 | ||
| 504 | |a Phillips, M.A., Coffino, P., Wang, C.C., Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei (1987) J. Biol. Chem., 262, pp. 8721-8727 | ||
| 504 | |a Sánchez, C.P., González, N.S., Algranati, I.D., Stable ornithine decarboxylase in promastigotes of Leishmania mexicana mexicana (1989) Biochem. Biophys. Res. Commun., 161, pp. 754-761 | ||
| 504 | |a Hanson, S., Adelman, J., Ullman, B., Amplification and molecular cloning of the ornithine decarboxylase gene of Leishmania donovani (1992) J. Biol. Chem., 267, pp. 2350-2359 | ||
| 504 | |a Ghoda, L., Phillips, M.A., Bass, K.E., Wang, C.C., Coffino, P., Trypanosome ornithine decarboyxlase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation (1990) J. Biol. Chem., 265, pp. 11823-11826 | ||
| 504 | |a Ghoda, L., Sidney, D., Macrae, M., Coffino, P., Structural elements of ornithine decarboxylase required for intracellular degradation and polyamine-dependent regulation (1992) Mol. Cell. Biol., 12, pp. 2178-2185 | ||
| 504 | |a Bacchi, C.J., Nathan, H.C., Hutner, S.H., McCann, P.P., Sjoerdsma, A., Polyamine metabolism: A potential therapeutic target in trypanosomes (1980) Science, 210, pp. 332-334 | ||
| 504 | |a Van Nieuwenhove, S., Schechter, P.J., Declercq, J., Bone, G., Burke, J., Sjoerdsma, A., Treatment of Gambiense sleeping sickness in the Sudan with oral DFMO, an inhibitor of ornithine decarboxylase: First field trial (1985) Trans. R. Soc. Trop. Med. Hyg., 79, pp. 692-698 | ||
| 504 | |a Heby, O., Persson, L., Molecular genetics of polyamine synthesis in eukaryotic cells (1990) Trends Biochem. Sci., 15, pp. 153-158 | ||
| 504 | |a Iten, M., Mett, H., Evans, A., Enyaru, J.C.K., Brun, R., Kaminsky, R., Alterations in ornithine decarboxylase characteristics account for tolerance of Trypanosoma brucei rhodesiense to DL-α-difluoromethylornithine (1997) Antimicrob. Agents Chemother., 41, pp. 1922-1925 | ||
| 504 | |a Ceriani, C., González, N.S., Algranati, I.D., Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation (1992) FEBS Lett., 301, pp. 261-264 | ||
| 504 | |a Svensson, F., Ceriani, C., Wallström, E.L., Kockum, I., Algranati, I.D., Heby, O., Persson, L., Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain (1997) Proc. Natl. Acad. Sci. USA, 74, pp. 397-402 | ||
| 504 | |a Ceriani, C., (1997) Polyamine Metabolism in Crithidia fasciculata, , Ph.D. thesis, University of Buenos Aires | ||
| 504 | |a Carrillo, C., Cejas, S., González, N.S., Algranati, I.D., Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme (1999) FEBS Lett., 454, pp. 192-196 | ||
| 504 | |a Sánchez, C.P., Sidrauski, C., Menezes Freire, S., González, N.S., Algranati, I.D., Ornithine decarboxylase from Leishmania mexicana promastigotes: Interaction with pyridoxal-5′-phosphate and α-difluoromethylornithine (1995) Biochem. Biophys. Res. Commun., 212, pp. 396-403 | ||
| 504 | |a Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein - dye binding (1976) Anal Biochem., 72, pp. 248-254 | ||
| 504 | |a Morgan, D.M.L., (1998), pp. 111-1118. , Polyamine Protocols (Morgan, D. M. L., Ed.), Humana Press, Totowa, NJ; Medina-Acosta, E., Cross, G.A.M., Rapid isolation of DNA from trypanosomatid protozoa using a simple "mini-prep" procedure (1993) Mol. Biochem. Parasitol., 59, pp. 327-329 | ||
| 504 | |a Sánchez, C.P., Mucci, J., González, N.S., Ochoa, A., Zakin, M.M., Algranati, I.D., α-Difluoromethylornithine-resistant cell lines obtained after one-step selection of Leishmania mexicana promastigotes cultures (1997) Biochem. J., 324, pp. 847-853 | ||
| 504 | |a Byers, T.L., Bush, T.L., McCann, P.P., Bitonti, A.J., Antitrypanosomal effects of polyamine biosynthesis inhibitors correlate with increases in Trypanosoma brucei brucei S-adenosyl-L-methionine (1991) Biochem. J., 274, pp. 527-533 | ||
| 504 | |a Bacchi, C.J., Garofalo, J., Ciminelli, M., Rattendi, D., Goldberg, B., McCann, P.P., Yarlett, N., Resistance to DL-α-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense. Role of S-adenosylmethionine (1993) Biochem. Pharmacol., 46, pp. 471-481 | ||
| 520 | 3 | |a α-Difluoromethylornithine (DFMO), the specific and irreversible inhibitor of ornithine decarboxylase (ODC), was able to induce the arrest of proliferation in Leishmania mexicana and ODC-transformed Trypanosoma cruzi cultures grown in a semi-defined medium essentially free of polyamines. Conversely, Crithidia fasciculata and Phytomonas 274 were not affected by the inhibitor. The drug-resistance of Crithidia and Phytomonas was neither caused by an impairment of DFMO uptake nor by a decrease of the enzyme affinity for the inhibitor. We were also able to rule out the possibility of ODC overexpression in the drug-tolerant parasites. The measurements of ODC metabolic turnover indicated that the enzymes from Crithidia and Phytomonas have a short half-life of 20-40 min, while ODC from Leishmania and transgenic Trypanosoma cruzi are rather stable with a half-life longer than 6 hours. Analyses of polyamine internal pools under different growth conditions have shown that DFMO was able to markedly decrease the levels of putrescine and spermidine in all parasites, but the depletion of spermidine was higher in trypanosomatids containing an ODC with slow turnover. Our results suggest that in these parasites cultivated in the presence of the drug, spermidine might decrease below critical levels needed to maintain trypanothione concentrations or other conditions essential for normal proliferation. © 2000 Academic Press. |l eng | |
| 536 | |a Detalles de la financiación: SAREC | ||
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: National Research Council | ||
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Comisión de Investigaciones Científicas | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: We are grateful to Ms. Marta Bravo for HPLC determinations and Dr. S. H. Goldemberg for helpful discussions. This study was supported by grants from Agencia Nacional de Promoción Científica y Tecnológica (Argentina), the National Research Council (CONICET, Argentina), the University of Buenos Aires, the Swedish Agency for Research Cooperation with Developing Countries (SAREC) and the United Nations Industrial Development Organization (UNIDO). C. Carrillo and S. Cejas are fellows of the FOMEC Program and the Buenos Aires Research Council (CIC), respectively; C. Ceriani is at the University of Tandil (Argentina) and N. S. González and I. D. Algranati are career investigators of the Consejo Nacional de Inves-tigaciones Científicas y Técnicas (Argentina). | ||
| 593 | |a Instituto de Invest. Bioquím., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires/CONICET, A. Machado 151, 1405 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a CRITHIDIA FASCICULATA |
| 690 | 1 | 0 | |a DFMO-RESISTANCE |
| 690 | 1 | 0 | |a LEISHMANIA MEXICANA |
| 690 | 1 | 0 | |a ORNITHINE DECARBOXYLASE |
| 690 | 1 | 0 | |a PHYTOMONAS |
| 690 | 1 | 0 | |a POLYAMINES |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a TRYPANOSOMATIDS PROLIFERATION |
| 690 | 1 | 0 | |a EFLORNITHINE |
| 690 | 1 | 0 | |a ORNITHINE DECARBOXYLASE |
| 690 | 1 | 0 | |a SPERMIDINE |
| 690 | 1 | 0 | |a TRYPANOTHIONE |
| 690 | 1 | 0 | |a ANTIPROTOZOAL ACTIVITY |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CRITHIDIA FASCICULATA |
| 690 | 1 | 0 | |a DRUG EFFECT |
| 690 | 1 | 0 | |a DRUG SCREENING |
| 690 | 1 | 0 | |a ENZYME INHIBITION |
| 690 | 1 | 0 | |a ENZYME METABOLISM |
| 690 | 1 | 0 | |a LEISHMANIA MEXICANA |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PHYTOMONAS |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 700 | 1 | |a Cejas, S. | |
| 700 | 1 | |a Cortés, M. | |
| 700 | 1 | |a Ceriani, C. | |
| 700 | 1 | |a Huber, A. | |
| 700 | 1 | |a González, N.S. | |
| 700 | 1 | |a Algranati, I.D. | |
| 773 | 0 | |d Academic Press Inc., 2000 |g v. 279 |h pp. 663-668 |k n. 2 |p Biochem. Biophys. Res. Commun. |x 0006291X |w (AR-BaUEN)CENRE-905 |t Biochemical and Biophysical Research Communications | |
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