Artículo

Carrillo, C.; Cejas, S.; Huber, A.; González, N.S.; Algranati, I.D. "Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes" (2003) Journal of Eukaryotic Microbiology. 50(5):312-316
Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

The presence of arginine decarboxylase (ADC) enzymatic activity in Trypanosoma cruzi epimastigotes is still a matter of controversy due to conflicting results published during the last few years. We have investigated whether arginine might indeed be a precursor of putrescine via agmatine in these parasites. We have shown that wild-type T. cruzi epimastigotes cultivated in a medium almost free of polyamines stopped their growth after several repeated passages of cultures in the same medium, and that neither arginine nor ornithine were able to support or reinitiate parasite multiplication. In contrast, normal growth was quickly resumed after adding exogenous putrescine or spermidine. The in vivo labelling of parasites with radioactive arginine showed no conversion of this amino acid into agmatine, and attempts to detect ADC activity measured by the release of CO2 under different conditions in T. cruzi extracts gave negligible values for all strains assayed. The described data clearly indicate that wild-type T. cruzi epimastigotes lack ADC enzymatic activity.

Registro:

Documento: Artículo
Título:Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes
Autor:Carrillo, C.; Cejas, S.; Huber, A.; González, N.S.; Algranati, I.D.
Filiación:Fundación Instituto Leloir, Fac. de Cie. Exactas y Naturales, Univ. de Buenos Aires/CONICET, A. Machado 151, 1405 Buenos Aires, Argentina
Palabras clave:Agmatine; Polyamine biosynthetic pathways; Trypanosomatids; enzyme activity; Animals; Arginine; Carboxy-Lyases; Ornithine; Putrescine; Trypanosoma cruzi; Trypanosoma; Trypanosoma cruzi
Año:2003
Volumen:50
Número:5
Página de inicio:312
Página de fin:316
DOI: http://dx.doi.org/10.1111/j.1550-7408.2003.tb00141.x
Título revista:Journal of Eukaryotic Microbiology
Título revista abreviado:J. Eukaryotic Microbiol.
ISSN:10665234
CODEN:JEMIE
CAS:arginine decarboxylase, EC 4.1.1.19; Arginine, 74-79-3; Carboxy-Lyases, EC 4.1.1.-; Ornithine, 7006-33-9; Putrescine, 110-60-1
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v50_n5_p312_Carrillo

Referencias:

  • 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. , Goldemberg, S. H. & Algranati, I. D. (ed.). Oxford University Press, Oxford
  • 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
  • Bacchi, C.J., Braunstein, V.L., Rattendi, D., Yarlett, N., Wittner, M., Tanowitz, H.B., Stage-specific polyamine metabolism in Trypanosoma cruzi (2001) J. Eukaryot. Microbiol., 49, pp. 201S-202S
  • 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
  • Bera, T., The γ-guanidinobutyramide pathway of L-arginine catabolism in Leishmania donovani promastigotes (1987) Mol. Biochem. Parasitol., 23, pp. 183-192
  • 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
  • Brenner, Z., Chiari, E., Morphological variations observed in different samples of Trypanosoma cruzi (1963) Rev. Inst. Med. Trop. Sao Paulo, 5, pp. 220-224
  • Brun, R., Schonenberger, M., Cultivation and in vitro cloning of procyclic culture forms of Trypanosoma brucei in a semi-defined medium (1979) Acta Trop., 36, pp. 289-292
  • 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
  • Cataldi, A.A., Algranati, I.D., Polyamines and regulation of ornithine biosynthesis in E. coli (1989) J. Bacteriol., 171, pp. 1998-2002
  • 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
  • Coffino, P., Molecular biology of eukaryotic ornithine decarboxylase (1989) Ornithine Decarboxylase: Biology, Enzymology, and Molecular Genetics, pp. 135-144. , Hayashi S. (ed.). Pergamon Press, New York
  • Cohen, S.S., Pathways of polyamine metabolism in animals (1998) A Guide to the Plyamines, pp. 208-230. , Cohen, S. S. (ed.). Oxford University Press, New York
  • 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 (Buenos Aires), 41, pp. 549-555
  • 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
  • Hernández, S., Schwarcz De Tarlovsky, M., Arginine decarboxylase in Trypanosoma cruzi. Characteristics and kinetic properties (1999) Cell. Mol. Biol., 45, pp. 383-391
  • Hunter, K.J., Le Quesne, S.A., Fairlamb, A.H., Identification and biosynthesis of N1, N 9-bis(glutathionyl)aminopropyl-cadaverine (homotrypanothione) in Trypanosoma cruzi (1994) Eur. J. Biochem., 226, pp. 1019-1027
  • Kallio, A., Mc Cann, P.P., Bey, P., DL-α (Difluoromethyl)arginine: A potent enzyme-activated irreversible inhibitor of bacterial arginine decarboxylases (1981) Biochemistry, 20, pp. 3163-3166
  • Keithly, J.S., Zhu, G., Upton, S.J., Woods, K.M., Martínez, M.P., Yarlett, N., Polyamine biosynthesis in Cryptosporidium parvum and its implications for chemotherapy (1997) Mol. Biochem. Parasitol., 88, pp. 35-42
  • Kierszenbaum, F., Wirth, J.J., Mc Cann, P.P., Sjoerdsma, A., Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 4278-4282
  • Li, G., Regunathan, S., Reis, D.J., Agmatine is synthesized by a mitochondrial arginine decarboxylase in rat brain (1995) Ann. N. Y. Acad. Sci., 763, pp. 325-329
  • 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
  • Malmberg, R.L., Cellino, M.L., Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides (1994) J. Biol. Chem., 269, pp. 2703-2706
  • Martínez-Calvillo, S., López, I., Hernández, R., pRIBOTEX expression vector: A pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants (1997) Gene, 199, pp. 71-76
  • Müller, S., Coombs, G.H., Walter, R.D., Targeting polyamines of parasitic protozoa in chemotherapy (2001) Trends Parasitol., 17, pp. 242-249
  • 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. USA, 98, pp. 7301-7306
  • Raasch, W., Regunathan, S., Li, G., Reis, D.J., Agmatine, the bacterial amine, is widely distributed in mammalian tissues (1995) Life Sci., 56, pp. 2319-2330
  • Regunathan, S., Reis, D.J., Characterization of arginine decarboxylase in rat brain and liver: Distinction from ornithine decarboxylase (2000) J. Neurochem., 74, pp. 2201-2208
  • 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 promastigote cultures (1997) Biochem. J., 324, pp. 847-853
  • Schwarcz De Tarlovsky, M.N., Hernández, S.M., Bedoya, A.M., Lammel, E.M., Isola, E.L.D., Polyamines in Trypanosoma cruzi (1993) Biochem. Mol. Biol. Int., 30, pp. 547-558
  • 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 (Buenos Aires), 40, pp. 97-102
  • Smith, T.A., Marshall, J.H.A., The oxidative decarboxylation of ornithine by extracts of higher plants (1988) Phytochemistry, 27, pp. 703-710
  • Wu, W.H., Morris, D.R., Biosynthetic arginine decarboyxlase from Escherichia coli: Purification and properties (1973) J. Biol. Chem., 248, pp. 1687-1695
  • Yakubu, M.A., Basso, B., Kierszenbaum, F., DL-αdifluoromethylarginine inhibits intracellular Trypanosoma cruzi multiplication by affecting cell division but not trypomastigote-amastigote transformation (1992) J. Parasitol., 78, pp. 414-419

Citas:

---------- APA ----------
Carrillo, C., Cejas, S., Huber, A., González, N.S. & Algranati, I.D. (2003) . Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes. Journal of Eukaryotic Microbiology, 50(5), 312-316.
http://dx.doi.org/10.1111/j.1550-7408.2003.tb00141.x
---------- CHICAGO ----------
Carrillo, C., Cejas, S., Huber, A., González, N.S., Algranati, I.D. "Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes" . Journal of Eukaryotic Microbiology 50, no. 5 (2003) : 312-316.
http://dx.doi.org/10.1111/j.1550-7408.2003.tb00141.x
---------- MLA ----------
Carrillo, C., Cejas, S., Huber, A., González, N.S., Algranati, I.D. "Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes" . Journal of Eukaryotic Microbiology, vol. 50, no. 5, 2003, pp. 312-316.
http://dx.doi.org/10.1111/j.1550-7408.2003.tb00141.x
---------- VANCOUVER ----------
Carrillo, C., Cejas, S., Huber, A., González, N.S., Algranati, I.D. Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes. J. Eukaryotic Microbiol. 2003;50(5):312-316.
http://dx.doi.org/10.1111/j.1550-7408.2003.tb00141.x