Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi
Wild-type Trypanosoma cruzi epimastigotes lack arginine decarboxylase (ADC) enzymatic activity. However, the transformation of these parasites with a recombinant plasmid containing the oat ADC cDNA coding region gave rise to the transient heterologous expression of the enzyme, suggesting the absence...
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2004
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| 008 | 190411s2004 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-7944222074 | |
| 024 | 7 | |2 cas |a alpha difluoromethylarginine, 69955-43-7; Carboxy-Lyases, 4.1.1.-; DNA Primers; DNA, Complementary; Enzyme Inhibitors; Recombinant Proteins; arginine decarboxylase, 4.1.1.19 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BBGSB | ||
| 100 | 1 | |a Carrillo, C. | |
| 245 | 1 | 0 | |a Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| 260 | |c 2004 | ||
| 270 | 1 | 0 | |m Fundación Instituto Leloir, Fac. de Ciencias Exactas Y Naturales, Univ. Buenos Aires CONICET, A. M.Argentina; email: ialgranati@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Bacchi, C.J., Nathan, H.C., Hutner, S.H., Mc Cann, P.P., Sjoerdsma, A., Polyamine metabolism: A potential therapeutic target in trypanosomes (1980) Science, 210, pp. 332-334 | ||
| 504 | |a Bacchi, C.J., Mc Cann, P.P., Parasitic protozoa and polyamines (1987) Inhibition of Polyamine Metabolism. Biological Significance and Bases for New Therapies, pp. 317-344. , P.P. Mc Cann A.E. Pegg A. Sjoerdsma Academic Press, Inc. Orlando, Fl | ||
| 504 | |a Van Nieuwenhove, S., Schechter, P.J., Declercq, J., Boné, 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 Fairlamb, A.H., Cerami, A., Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids (1985) Mol. Biochem. Parasitol., 14, pp. 187-198 | ||
| 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 Fairlamb, A.H., Cerami, A., Metabolism and functions of trypanothione in the Kinetoplastida (1992) Annu. Rev. Microbiol., 46, pp. 695-729 | ||
| 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 (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 decarboxylase 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 Assaraf, Y.G., Kahana, C., Spira, D.T., Bachrach, U., Plasmodium falciparum: Purification, properties and immunochemical study of ornithine decarboxylase, the key enzyme in polyamine biosynthesis (1988) Exp. Parasitol., 67, pp. 20-30 | ||
| 504 | |a Hayashi, S., Murakami, Y., Rapid and regulated degradation of ornithine decarboxylase (1995) Biochem. J., 306, pp. 1-10 | ||
| 504 | |a Carrillo, C., Cejas, S., Cortés, M., Ceriani, C., Huber, 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 Algranati, I.D., Sánchez, C., González, N.S., Polyamines in Trypanosoma cruzi and Leishmania mexicana (1990) The Biology and Chemistry of Polyamines, pp. 137-146. , S.H. Goldemberg I.D. Algranati Oxford Univ. Press Oxford | ||
| 504 | |a Hunter, K.J., Le Quesne, S.A., Fairlamb, A.H., Identification and biosynthesis of N 1-N 9-bis (glutathionyl) aminopropyl-cadaverine (homotrypanothione) in Trypanosoma cruzi (1994) Eur. J. Biochem., 226, pp. 1019-1027 | ||
| 504 | |a Ariyanayagam, M.R., Fairlamb, A.H., Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes (1997) Mol. Biochem. Parasitol., 84, pp. 111-121 | ||
| 504 | |a Müller, S., Coombs, G.H., Walter, R.D., Targeting polyamines of parasitic protozoa in chemotherapy (2001) Trends Parasitol., 17, pp. 242-249 | ||
| 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 Kierszenbaum, F., Wirth, J.J., Sjoerdsma, A., Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells (1987) Proc. Natl. Acad. Sci. U. S. A., 84, pp. 4278-4282 | ||
| 504 | |a Majumder, S., Wirth, J.J., Bitonti, A.J., Mc Cann, P.P., Kierszenbaum, F., Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi (1992) J. Parasitol., 78, pp. 371-374 | ||
| 504 | |a Hernández, S., Schwarcz De Tarlovsky, M., Arginine decarboxylase in Trypanosoma cruzi. Characteristics and kinetic properties (1999) Cell. Mol. Biol., 45, pp. 383-391 | ||
| 504 | |a Piacenza, L., Peluffo, G., Radi, R., L-Arginine-dependent suppression of apoptosis in Trypanosoma cruzi: Contribution of the nitric oxide and polyamine pathways (2001) Proc. Natl. Acad. Sci. U. S. A., 98, pp. 7301-7306 | ||
| 504 | |a Cohen, S.S., Pathways of polyamine metabolism in animals (1998) A Guide to the Polyamines, pp. 208-230. , S.S. Cohen Oxford Univ. Press New York | ||
| 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 Carrillo, C., Cejas, S., Huber, A., González, N.S., Algranati, I.D., Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes (2003) J. Eukaryot. Microbiol., 50, pp. 312-316 | ||
| 504 | |a Segura, E.L., Subias, E., Esteva, M., Cabeza Meckert, P., Brozina, A., Laguens, R.P., Características de infectividad de tres poblaciones de cultivo de Trypanosoma cruzi (1980) Medicina (B. Aires), 40, pp. 97-102 | ||
| 504 | |a González Cappa, S.M., Katzin, A.M., Añasco, N., Lajmanovich, S., Comparative studies on infectivity and surface carbohydrates of several strains of Trypanosoma cruzi (1981) Medicina (B. Aires), 41, pp. 549-555 | ||
| 504 | |a Cazzulo, J.J., Franke De Cazzulo, B.M., Engel, J.C., Cannata, J.J.B., End products and enzyme levels of aerobic glucose fermentation in trypanosomatids (1985) Mol. Biochem. Parasitol., 16, pp. 329-343 | ||
| 504 | |a Brun, R., Schonenberger, M., Cultivation and in vivo cloning of procyclic culture forms of Trypanosoma brucei in a semi-defined medium (1979) Acta Trop., 36, pp. 289-292 | ||
| 504 | |a Cataldi, A.A., Algranati, I.D., Polyamines and regulation of ornithine decarboxylase biosynthesis in Escherichia coli (1989) J. Bacteriol., 171, pp. 1998-2002 | ||
| 504 | |a Bell, E., Malmberg, R.L., Analysis of a cDNA-encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing (1990) Mol. Gen. Genet., 224, pp. 431-436 | ||
| 504 | |a Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254 | ||
| 504 | |a Martínez-Calvillo, S., López, I., Hernández, R., P-RIBOTEX expression vector: PTEX derivative for a rapid selection of Trypanosoma cruzi transfectans (1997) Gene, 199, pp. 71-76 | ||
| 504 | |a Hariharan, S., Ajioka, J., Swindle, J., Stable transformation of Trypanosoma cruzi: Inactivation of the PUB12,5 polyubiquitin gene by targeted gene disruption (1993) Mol. Biochem. Parasitol., 57, pp. 15-30 | ||
| 504 | |a 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. 327-330 | ||
| 504 | |a Malmberg, R.L., Cellino, M.L., Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptdies (1994) J. Biol. Chem., 269, pp. 2703-2706 | ||
| 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 Bass, K.E., Sommer, J.M., Cheng, Q.L., Wang, C.C., Mouse ornithine decarboxylase is stable in Trypanosoma brucei (1992) J. Biol. Chem., 267, pp. 11034-11037 | ||
| 504 | |a Zhu, M.J., Iyo, A., Piletz, J.E., Regunathan, S., Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine (2004) Biochim. Biophys. Acta, 1670, pp. 156-164 | ||
| 504 | |a Coleman, C.S., Hu, G., Pegg, A.E., Putrescine biosynthesis in mammalian tissues Biochem. J., , (in press) | ||
| 520 | 3 | |a Wild-type Trypanosoma cruzi epimastigotes lack arginine decarboxylase (ADC) enzymatic activity. However, the transformation of these parasites with a recombinant plasmid containing the oat ADC cDNA coding region gave rise to the transient heterologous expression of the enzyme, suggesting the absence of endogenous mechanisms that could inhibit the expression of a hypothetical own ADC gene or the assay used to measure its enzymatic activity. The foreign ADC enzyme expressed in the transgenic T. cruzi was characterized by identification of the products, the stoichiometry of the catalysed reaction, the specific inhibition by α-difluoromethylarginine (DFMA) and the study of its metabolic turnover. The half-life of the heterologous ADC activity in T. cruzi was about 150 min. Bioinformatics studies and polymerase chain reaction (PCR) analyses seem to indicate the absence of ADC-like DNA sequences in the wild-type T. cruzi genome. © 2004 Published by Elsevier B.V. |l eng | |
| 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: Fundación Antorchas | ||
| 536 | |a Detalles de la financiación: National Institutes of Health, A145061, A145039, A145038 | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: We thank Dr. Sara H. Goldemberg for helpful discussions. This work was partially supported by grants from Agencia Nacional de Promoción Científica y Tecnológica (Argentina), The National Research Council (CONICET), Fundación Antorchas (Argentina) and the International Centre for Genetic Engineering and Biotechnology Collaborative Research Programme (Trieste, Italy). Preliminary genomic data were accessed via http://TcruziDB.org and/or http://www.tigr.org/tdb/tcruzi/ . Most of the genomic data were provided by the TIGR-SBRI-KI Sequencing Consortium (TSK-TSC) supported by NIH grants A145038, A145061 and A145039. | ||
| 593 | |a Fundación Instituto Leloir, Fac. de Ciencias Exactas Y Naturales, Univ. Buenos Aires CONICET, A. M., Argentina | ||
| 593 | |a Inst. Invest. Medicas Alfredo Lanari, UBA and CONICET, Combatientes Malvinas 3150, 1427 B., Argentina | ||
| 690 | 1 | 0 | |a AGMATINE |
| 690 | 1 | 0 | |a ARGININE DECARBOXYLASE |
| 690 | 1 | 0 | |a POLYAMINE BIOSYNTHESIS |
| 690 | 1 | 0 | |a TRANSGENIC PARASITE |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI EPIMASTIGOTE |
| 690 | 1 | 0 | |a ALPHA DIFLUOROMETHYLARGININE |
| 690 | 1 | 0 | |a ARGININE DECARBOXYLASE GENE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BIOINFORMATICS |
| 690 | 1 | 0 | |a BIOLISTIC TRANSFORMATION |
| 690 | 1 | 0 | |a CATALYSIS |
| 690 | 1 | 0 | |a CATALYST |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a DNA SEQUENCE |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a ENZYME ASSAY |
| 690 | 1 | 0 | |a ENZYME INHIBITION |
| 690 | 1 | 0 | |a GENE EXPRESSION |
| 690 | 1 | 0 | |a GENETIC CODE |
| 690 | 1 | 0 | |a GENETIC RECOMBINATION |
| 690 | 1 | 0 | |a GENOME |
| 690 | 1 | 0 | |a HALF LIFE TIME |
| 690 | 1 | 0 | |a HETEROLOGOUS EXPRESSION |
| 690 | 1 | 0 | |a INTERMETHOD COMPARISON |
| 690 | 1 | 0 | |a METABOLIC REGULATION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PLANT |
| 690 | 1 | 0 | |a POLYMERASE CHAIN REACTION |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a REACTION ANALYSIS |
| 690 | 1 | 0 | |a SEQUENCE ANALYSIS |
| 690 | 1 | 0 | |a STOICHIOMETRY |
| 690 | 1 | 0 | |a TRANSGENE |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a WILD TYPE |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a ANIMALS, GENETICALLY MODIFIED |
| 690 | 1 | 0 | |a AVENA SATIVA |
| 690 | 1 | 0 | |a BASE SEQUENCE |
| 690 | 1 | 0 | |a CARBOXY-LYASES |
| 690 | 1 | 0 | |a DNA PRIMERS |
| 690 | 1 | 0 | |a DNA, COMPLEMENTARY |
| 690 | 1 | 0 | |a ENZYME INHIBITORS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a OPEN READING FRAMES |
| 690 | 1 | 0 | |a RECOMBINANT PROTEINS |
| 690 | 1 | 0 | |a TRANSFECTION |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a TRYPANOSOMA |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 700 | 1 | |a Serra, M.P. | |
| 700 | 1 | |a Pereira, C.A. | |
| 700 | 1 | |a Huber, A. | |
| 700 | 1 | |a González, N.S. | |
| 700 | 1 | |a Algranati, I.D. | |
| 773 | 0 | |d 2004 |g v. 1674 |h pp. 223-230 |k n. 3 |p Biochim. Biophys. Acta Gen. Subj. |x 03044165 |w (AR-BaUEN)CENRE-2260 |t Biochimica et Biophysica Acta - General Subjects | |
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