Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase

The metabolism of polyamines as well as their functions as growth regulators in plants have been extensively studied for many years. However, almost nothing is known about the biosynthesis and roles of these substances in Phytomonas spp., parasites of several plants. We have used HPLC and electropho...

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Autor principal: Marcora, M.S
Otros Autores: Cejas, S., González, N.S, Carrillo, C., Algranati, I.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2010
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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024 7 |2 scopus  |a 2-s2.0-84755161369 
024 7 |2 cas  |a agmatine, 306-60-5; arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; benzyloxycarbonylleucylleucylleucinal, 133407-82-6; eflornithine, 67037-37-0, 70052-12-9; ornithine, 70-26-8, 7006-33-9; ornithine decarboxylase, 9024-60-6; proteasome, 140879-24-9; putrescine, 110-60-1, 333-93-7; pyridoxal 5 phosphate, 54-47-7; spermidine, 124-20-9, 334-50-9; spermidine synthase, 37277-82-0, 67016-02-8; spermine, 306-67-2, 71-44-3; Ornithine Decarboxylase, 4.1.1.17; Polyamines; Protozoan Proteins; Putrescine, 110-60-1; Spermidine, 124-20-9; Spermine, 71-44-3 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a IJPYB 
100 1 |a Marcora, M.S. 
245 1 0 |a Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase 
260 |c 2010 
270 1 0 |m Carrillo, C.; Fundación Instituto Leloir, IIBBA - CONICET, Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina; email: ccarrillo@leloir.org.ar 
506 |2 openaire  |e Política editorial 
504 |a Algranati, I.D., Sánchez, C.P., González, N.S., Polyamines in Trypanosoma cruzi and Leishmania mexicana (1990) The Biology and Chemistry of Polyamines, pp. 137-146. , Oxford University Press, Oxford, S.H. Goldemberg, I.D. Algranati (Eds.) 
504 |a Ariyanayagam, M.R., Fairlamb, A.H., Ovothiol and trypanothione as antioxidants in trypanosomatids (2001) Mol. Biochem. Parasitol., 115, pp. 189-198 
504 |a Arteaga-Nieto, P., Villagomez-Castro, J.C., Calvo-Méndez, C.C., López-Romero, E., Partial purification and characterization of ornithine decarboxylase from Entamoeba histolytica (1996) Int. J. Parasitol., 26, pp. 253-260 
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 Berlin, C.M., Schimke, R.T., Influence of turnover rates on the responses of enzymes to cortisone (1965) Mol. Pharmacol., 1, pp. 149-156 
504 |a Calvo-Mendez, C., Villagomez-Castro, J.C., López-Romero, E., Ornithine decarboxylase activity in Entamoeba invadens (1993) Int. J. Parasitol., 23, pp. 847-852 
504 |a Canellakis, E.S., Kyriakidis, D.A., Rinehart, C.A., Huang, S.C., Panagiotidis, C., Fong, W.F., Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Review (1985) Biosci. Rep., 5, pp. 189-204 
504 |a Cánepa, G.E., Carrillo, C., Armesto, A.R., Bouvier, L.A., Miranda, M.R., Pereira, C.A., Phytomonas: transport of amino acids, hexoses and polyamines (2007) Exp. Parasitol., 117, pp. 106-110 
504 |a Carrillo, C., Cejas, S., Gonzalez, 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 Carrillo, C., Cejas, S., Cortés, M.M., Ceriani, C., Huber, M.A., González, N.S., Algranati, I.D., Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase (2000) Biochem. Biophys. Res. Commun., 279, pp. 663-668 
504 |a Carrillo, C., González, N.S., Algranati, I.D., Trypanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites (2007) Biochim. Biophys. Acta, 1770, pp. 1605-1611 
504 |a Cataldi, A.A., Algranati, I.D., Polyamines and regulation of ornithine biosynthesis in Escherichia coli (1989) J. Bacteriol., 171, pp. 1998-2002 
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 (1998) A Guide to the Polyamines, , University Press, Oxford, S.S. Cohen (Ed.) 
504 |a Dollet, M., Plant diseases caused by flagellate protozoa (Phytomonas) (1984) Annu. Rev. Phytopathol., 22, pp. 115-132 
504 |a Dollet, M., Phloem-restricted trypanosomatids form a clearly characterised monophyletic group among trypanosomatids isolated from plants (2001) Int. J. Parasitol., 31, pp. 459-467 
504 |a Eichler, W., Properties of purified l-ornithine decarboxylase (EC 4.1.1.17) from Tetrahymena thermophila (1989) J. Protozool., 36, pp. 577-582 
504 |a Fairlamb, A.H., Cerami, A., Metabolism and functions of trypanothione in the Kinetoplastida (1992) Annu. Rev. Microbiol., 46, pp. 695-729 
504 |a Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T., Cerami, A., Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids (1985) Science, 227, pp. 1485-1487 
504 |a Gillin, F.D., Reiner, D.S., McCann, P.P., Inhibition of growth of Giardia lamblia by difluoromethylornithine, a specific inhibitor of polyamine biosynthesis (1984) J. Protozool., 31, pp. 161-163 
504 |a González, N.S., Algranati, I.D., Regulation of putrescine uptake in Leishmania mexicana promastigotes (1994) Cell. Mol. Biol., 40, pp. 907-914 
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 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 González, N.S., Huber, M.A., Algranati, I.D., Spermidine is essential for normal proliferation of trypanosomatid protozoa (2001) FEBS Lett., 508, pp. 323-326 
504 |a Hanfrey, C., Sommer, S., Mayer, M.J., Burtin, D., Michael, A.J., Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity (2001) Plant J., 27, pp. 551-560 
504 |a Hayashi, S., Murakami, Y., Rapid and regulated degradation of ornithine decarboxylase (1995) Biochem. J., 306, pp. 1-10 
504 |a Heby, O., Polyamines and cell cycle (1980) Polyamines in Biomedical Research, pp. 17-34. , Wiley and Sons, New York, J.M. Gaugas (Ed.) 
504 |a Heby, O., Luk, G.D., Schindler, J., Polyamine synthesis inhibitors act as both inducers and suppressors of cell differentiation (1987) Inhibition of Polyamine Metabolism. Biological Significance and Basis for New Therapies, pp. 156-186. , Academic Press, Orlando, Florida, P.P. McCann, A.E. Pegg, A. Sjoerdsma (Eds.) 
504 |a Heby, O., Persson, L., Rentala, M., Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis (2007) Amino Acids, 33, pp. 359-366 
504 |a Hunter, K.J., Strobos, C.A., Fairlamb, A.H., Inhibition of polyamine biosynthesis in Crithidia fasciculata by d,l-alpha-difluoromethylornithine and d,l-alpha-difluoromethylarginine (1991) Mol. Biochem. Parasitol., 46, pp. 35-43 
504 |a Igarashi, K., Kashiwagi, K., Polyamines: mysterious modulators of cellular functions (2000) Biochem. Biophys. Res. Commun., 271, pp. 559-564 
504 |a Jankevicius, J.V., Jankevicius, S.I., Campaner, M., Conchon, I., Maeda, L.A., Teixeira, M.M.G., Freymuller, E., Camargo, E.P., Life cycle and culturing of Phytomonas serpens (Gibbs), a trypanosomatid parasite of tomatoes (1989) J. Protozool., 36, pp. 265-271 
504 |a Lee, D.H., Goldberg, A.L., Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae (1996) J. Biol. Chem., 271, pp. 27280-27284 
504 |a Lee, D.H., Goldberg, A.L., Proteasome inhibitors: valuable new tools for cell biologists (1998) Trends Cell Biol., 8, pp. 397-403 
504 |a Li, F., Hua, S.B., 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 Matsufuji, S., Matsufuji, T., Miyazaki, Y., Murakami, Y., Atkins, J.F., Gesteland, R.F., Hayashi, S., Autoregulatory frame shifting in decoding mammalian ornithine decarboxylase antizyme (1995) Cell, 80, pp. 51-60 
504 |a Metcalf, B.W., Bey, P., Danzin, C., Jung, M.J., Casara, P., Velvet, J.P., Catalytic irreversible inhibition of mammalian ornithine decarboxylase (1978) J. Am. Chem. Soc., 100, pp. 2551-2553 
504 |a (1998) Polyamine Protocols, , Humana Press, Totowa, New Jersey, D.M.L. Morgan (Ed.) 
504 |a Morris, D.R., Pardee, A.B., Multiple pathways of putrescine biosynthesis in Escherichia coli (1966) J. Biol. Chem., 241, pp. 3129-3135 
504 |a Mûller, S., Coombs, G.H., Walter, R.D., Targeting polyamines of parasitic protozoa in chemotherapy (2001) Trends Parasitol., 17, pp. 242-249 
504 |a Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., Ichihara, A., Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination (1992) Nature, 360, pp. 597-599 
504 |a Pegg, A.E., Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy (1988) Cancer Res., 48, pp. 759-774 
504 |a Poulin, R., Lu, L., Ackermann, B., Bey, P., Pegg, A.E., Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites (1992) J. Biol. Chem., 267, pp. 150-158 
504 |a Satishchandran, C., Boyle, S.M., Antagonistic transcriptional regulation of the putrescine biosynthetic enzyme agmatine ureohydrolase by cyclic AMP and agmatine in Escherichia coli (1984) J. Bacteriol., 157, pp. 552-559 
504 |a Smith, T.A., Recent advances in the biochemistry of plant amines (1975) Phytochemistry, 14, pp. 865-890 
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 Wilkinson, S.R., Meyer, D.J., Kelly, J.M., Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity (2000) Biochem. J., 352, pp. 755-761 
504 |a Yanagisawa, H., Suzuki, Y., Corn agmatine iminohydrolase: purification and properties (1981) Plant Physiol., 67, pp. 697-700 
520 3 |a The metabolism of polyamines as well as their functions as growth regulators in plants have been extensively studied for many years. However, almost nothing is known about the biosynthesis and roles of these substances in Phytomonas spp., parasites of several plants. We have used HPLC and electrophoretic analyses to investigate the presence and metabolism of polyamines in Phytomonas Jma strain, detecting both putrescine and spermidine but not spermine. Experiments carried out by incubation of intact parasites with labelled ornithine or putrescine showed the formation of radioactive putrescine or spermidine, respectively. These results indicated that Phytomonas Jma can synthesise these polyamines through the action of ornithine decarboxylase (ODC) and spermidine synthase. On the other hand, we could not detect the conversion of arginine to agmatine, suggesting the absence of arginine decarboxylase (ADC) in Phytomonas. However, we cannot ensure the complete absence of this enzymatic activity in the parasite. Phytomonas ODC required pyridoxal 5'-phosphate for maximum activity and was specifically inhibited by α-difluoromethylornithine. The metabolic turnover of the enzyme was very high, with a half-life of 10-15 min, one of the shortest found among all ODC enzymes studied to date. The parasite proteasome seems to be involved in degradation of the enzyme, since Phytomonas ODC can be markedly stabilized by MG-132, a well known proteasome inhibitor. The addition of polyamines to Phytomonas cultures did not decrease ODC activity, strongly suggesting the possible absence of antizyme in this parasite. © 2010 Australian Society for Parasitology Inc.  |l eng 
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: We wish to thank Dr. S.H. Goldemberg for helpful discussions and C. Zadikian for technical assistance. This work was partially supported by the National Research Council (Argentina) and the University of Buenos Aires. 
593 |a Fundación Instituto Leloir, IIBBA - CONICET, Buenos Aires, Argentina 
593 |a Departamento de Química Biológica - FCEN, Universidad de Buenos Aires (UBA), Buenos Aires, Argentina 
690 1 0 |a METABOLIC TURNOVER 
690 1 0 |a MG-132 
690 1 0 |a ORNITHINE DECARBOXYLASE 
690 1 0 |a PHYTOMONAS JMA 
690 1 0 |a PROTEASOME 
690 1 0 |a AGMATINE 
690 1 0 |a ARGININE 
690 1 0 |a BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL 
690 1 0 |a EFLORNITHINE 
690 1 0 |a ORNITHINE 
690 1 0 |a ORNITHINE DECARBOXYLASE 
690 1 0 |a POLYAMINE 
690 1 0 |a PROTEASOME 
690 1 0 |a PUTRESCINE 
690 1 0 |a PYRIDOXAL 5 PHOSPHATE 
690 1 0 |a SPERMIDINE 
690 1 0 |a SPERMIDINE SYNTHASE 
690 1 0 |a SPERMINE 
690 1 0 |a BIOCHEMISTRY 
690 1 0 |a BIODEGRADATION 
690 1 0 |a ELECTROKINESIS 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a EXPERIMENTAL STUDY 
690 1 0 |a GROWTH REGULATOR 
690 1 0 |a INHIBITION 
690 1 0 |a METABOLISM 
690 1 0 |a PARASITE 
690 1 0 |a PLANT 
690 1 0 |a ARTICLE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ELECTROPHORESIS 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME ANALYSIS 
690 1 0 |a ENZYME DEGRADATION 
690 1 0 |a ENZYME STABILITY 
690 1 0 |a HALF LIFE TIME 
690 1 0 |a HIGH PERFORMANCE LIQUID CHROMATOGRAPHY 
690 1 0 |a NONHUMAN 
690 1 0 |a PHYTOMONAS 
690 1 0 |a PHYTOMONAS JMA 
690 1 0 |a POLYAMINE SYNTHESIS 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a ENZYME STABILITY 
690 1 0 |a ORNITHINE DECARBOXYLASE 
690 1 0 |a POLYAMINES 
690 1 0 |a PROTOZOAN PROTEINS 
690 1 0 |a PUTRESCINE 
690 1 0 |a SPERMIDINE 
690 1 0 |a SPERMINE 
690 1 0 |a TRYPANOSOMATINA 
690 1 0 |a PHYTOMONAS 
700 1 |a Cejas, S. 
700 1 |a González, N.S. 
700 1 |a Carrillo, C. 
700 1 |a Algranati, I.D. 
773 0 |d 2010  |g v. 40  |h pp. 1389-1394  |k n. 12  |p Int. J. Parasitol.  |x 00207519  |w (AR-BaUEN)CENRE-5208  |t International Journal for Parasitology 
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