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Energy Metabolism in Trypanosoma cruzi

  • Chapter
Intracellular Parasites

Part of the book series: Subcellular Biochemistry ((SCBI,volume 18))

Abstract

The American trypanosomiasis, Chagas’ disease, affects about 20 million people in Central and South America. The causative agent is a parasitic flagellate, Trypanosoma cruzi, which has a complex life cycle, involving a replicative form, the amastigote, and a nonreplicative form, the bloodstream trypomastigote, in the mammalian host. There is also a replicative form, the epimastigote, and a nonreplicative form, the infective metacyclic trypomastigote, in the insect vector (Brener, 1973). Although at present all these developmental stages can be obtained in axenic culture (Contreras et al., 1985) or in mammalian cell culture (Andrews and Colli, 1982), or from infected mammals (Gutteridge et al., 1978), most metabolic and enzymological studies so far have been performed with cultured epimastigotes, presumably identical to those naturally present in the insect vector. Comparative studies using epimastigotes, amastigotes, and bloodstream trypomastigotes (Gutteridge and Rogerson, 1979) suggest that, at variance with African trypanosomes (Opperdoes, 1987), the different developmental stages of T. cruzi have qualitatively similar metabolic characteristics.

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References

  • Adroher, F. J., Osuna, A., and Lupiáñez, J. A., 1987, Fructose 1,6-bisphosphatase activity in two Trypanosoma cruzi morphological forms, J. Parasitol. 73:438–441.

    PubMed  CAS  Google Scholar 

  • Adroher, F. J., Osuna, A., and Lupiáñez, J. A., 1988, Differential energetic metabolism during Trypanosoma cruzi differentiation. 1. Citrate synthase, NADP-isocitrate dehydrogenase, and succinate dehydrogenase, Arch. Biochem. Biophys. 267:252–261.

    PubMed  CAS  Google Scholar 

  • Adroher, F. J., Osuna, A., and Lupiáñez, J. A., 1990, Differential energetic metabolism during Trypanosoma cruzi differentiation. II. Hexokinase, phosphofructokinase, and pyruvate kinase, Mol. Cell. Biochem. 94:71–80.

    PubMed  CAS  Google Scholar 

  • Affranchino, J. L., Tarlovsky, M. N. S. de, and Stoppani, A. O. M., 1985, Respiratory control in mitochondria from Trypanosoma cruzi, Mol. Biochem. Parasitol. 16:289–298.

    PubMed  CAS  Google Scholar 

  • Affranchino, J. L., Schwarcz de Tarlovsky, M. S., and Stoppani, A. O. M., 1986, Terminal oxidases in the Trypanosomatid Trypanosoma cruzi, Comp. Biochem. Physiol. 85:381–388.

    CAS  Google Scholar 

  • Aguilar, Z., and Urbina, J. A., 1986, The phosphofructokinase of Trypanosoma (Schizotrypanum) cruzi: Purification and kinetic mechanism, Mol. Biochem. Parasitol. 21:103–111.

    PubMed  CAS  Google Scholar 

  • Andrews, N. W., and Colli, W., 1982, Adhesion and interiorization of Trypanosoma cruzi in mammalian cells, J. Protozool. 29:264–269.

    PubMed  CAS  Google Scholar 

  • Arauzo, S., and Cazzulo, J. J., 1989, The NADP-linked aldehyde reductase from Trypanosoma cruzi. Subcellular localization and some properties, FEMS Microbiol. Lett. 58:283–286.

    CAS  Google Scholar 

  • Ashall, F., 1990, Characterization of an alkaline peptidase of Trypanosoma cruzi and other Tryp-nosomatids, Mol. Biochem. Parasitol. 38:77–88.

    PubMed  CAS  Google Scholar 

  • Avila, J. L., Bretaña, A., Casanova, M. A., Avila, A., and Rodriguez, F., 1979a, Trypanosoma cruzi: Defined medium for continuous cultivation of virulent parasites, Exp. Parasitol. 48:27–35.

    PubMed  CAS  Google Scholar 

  • Avila, J. L., Casanova, M. A., Avila, A., and Bretaña, A., 1979b, Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay, J. Protozool. 26:304–311.

    PubMed  CAS  Google Scholar 

  • Avila, J. L., Pérez-Kepp, R., and Bretaña, A., 1983, A minimal medium for 1he cultivation of infective Trypanosoma cruzi epimastigotes, J. Gen. Microbiol. 129:285–291.

    PubMed  CAS  Google Scholar 

  • Bacchi, C. J., Hutner, S. H., Ciaccio, E. I., and Marcus, S. M., 1968, (Vpolarographic studies on soluble and mitochondrial enzymes of Crithidia fasciculata; Glycerol phosphate enzymes, J. Protozool. 15:576–584.

    PubMed  CAS  Google Scholar 

  • Baernstein, H. D., 1953, Malic dehydrogenase and related enzymes in the culture form of Trypanosoma cruzi, Exp. Parasitol. 2:380–396.

    PubMed  CAS  Google Scholar 

  • Barros, E. G., and Caldas, R. A., 1983, Partial purification and characterization of glutamic-pyruvic transaminase from Trypanosoma cruzi, Comp. Biochem. Physiol. 74B:449–452.

    Google Scholar 

  • Bash-Lewinson, D., and Grossowicz, N., 1957, Transaminases of Trypanosoma cruzi, Bull. Res. Counc. Israel 6E:91–92.

    Google Scholar 

  • Boiso, J. F. de, Docampo, R., and Stoppani, A. O. M., 1979a, Citocromos de la forma epimastigote del Trypanosoma cruzi, Rev. Arg. Microbiol. 11:22–36.

    Google Scholar 

  • Boiso, J. F. de, Docampo, R., Stoppani, A. O. M., and Frasch, A. C. C., 1979b, Efecto de la antimicina A sobre la respiración y el crecimiento del Trypanosoma cruzi, Medicina (Buenos Aires) 39:362–368.

    Google Scholar 

  • Bongertz, V., and Hungerer, K. D., 1978, Trypanosoma cruzi: Isolation and characterization of a protease, Exp. Parasitol. 45:8–18.

    PubMed  CAS  Google Scholar 

  • Bontempi, E., Franke de Cazzulo, B. M., Ruiz, A. M., and Cazzulo, J. J., 1984, Purification and some properties of an acidic protease from epimastigotes of Trypanosoma cruzi, Comp. Biochem. Physiol. 77B:599–604.

    CAS  Google Scholar 

  • Bontempi, E., Martinez, J., and Cazzulo, J. J., 1989, Subcellular localization of a cysteine proteinase from Trypanosoma cruzi, Mol. Biochem. Parasitol. 33:43–47.

    PubMed  CAS  Google Scholar 

  • Boveris, A., Hertig, C. M., and Turrens, J. F., 1986, Fumarate reductase and other mitochondrial activities in Trypanosoma cruzi, Mol. Biochem. Parasitol. 19:163–169.

    PubMed  CAS  Google Scholar 

  • Bowman, I. B. R., Tobie, E. J., and von Brand, Th., 1963, CO2 fixation studies with the culture form of Trypanosoma cruzi, Comp. Biochem. Physiol. 9:105–114.

    CAS  Google Scholar 

  • Brener, Z., 1973, Biology of Trypanosoma cruzi, Annu. Rev. Microbiol. 27:347–382.

    PubMed  CAS  Google Scholar 

  • Cáceres, O., and Fernandes, J. F., 1976, Glucose metabolism, growth and differentiation of Trypanosoma cruzi, Rev. Brasil. Biol. 36:397–410.

    PubMed  Google Scholar 

  • Camargo, E. P., Coelho, J. A., Moraes, G., and Figueiredo, E. N., 1978, Trypanosoma spp., Leishmania spp. and Leptomonas spp.: Enzymes of ornithine-arginine metabolism, Exp. Parasitol. 46:141–144.

    CAS  Google Scholar 

  • Campetella, O., Martinez, J., and Cazzulo, J. J., 1990, A major cysteine proteinase is developmentally regulated in Trypanosoma cruzi, FEMS Microbiol. Lett. 67:145–150.

    CAS  Google Scholar 

  • Cannata, J. J. B., and Cazzulo, J. J., 1984a, The aerobic fermentation of glucose by Trypanosoma cruzi, Comp. Biochem. Physiol. 79B:297–308.

    CAS  Google Scholar 

  • Cannata, J. J. B., and Cazzulo, J. J., 1984b, Glycosomal and mitochondrial malate dehydrogenases in epimastigotes of Trypanosoma cruzi, Mol. Biochem. Parasitol. 11:37–49.

    PubMed  CAS  Google Scholar 

  • Cannata, J. J. B., Frasch, A. C. C., Cataldi de Flombaum, M. A., Segura, E. L., and Cazzulo, J. J., 1979, Two forms of malic enzyme with different regulatory properties in Trypanosoma cruzi, Biochem. J. 184:409–419.

    PubMed  CAS  Google Scholar 

  • Cannata, J. J. B., Docampo, R., Valle, E., Franke de Cazzulo, B. M., and Cazzulo, J. J., 1980, Distribution intracelular de las enzimas fijadoras de CO2 en Trypanosoma cruzi y Crithidia fasciculata, Medicina (Buenos Aires) 40(Suppl. 1):143–153.

    Google Scholar 

  • Cannata, J. J. B., Valle, E., Docampo, R., and Cazzulo, J. J., 1982, Subcellular localization of phosphoenolpyruvate carboxykinase in the trypanosomatids Trypanosoma cruzi and Crithidia fasciculata, Mol. Biochem. Parasitol. 6:151–160.

    PubMed  CAS  Google Scholar 

  • Cameiro, M., and Caldas, R. A., 1982, Evidence for three respiratory terminals in Trypanosoma cruzi epimastigotes, Acta Trop. 39:41–49.

    Google Scholar 

  • Cameiro, V. T. C., and Caldas, R. A., 1983, Regulatory studies of L-glutamate dehydrogenase from Trypanosoma cruzi epimastigotes, Comp. Biochem. Physiol. 75B:61–64.

    Google Scholar 

  • Cataldi de Flombaum, M. A., and Stoppant, A. O. M., 1981, Influence of efrapeptin, aurovertin and citreoviridin on the mitochondrial adenosine triphosphatase from Trypanosoma cruzi, Mol. Biochem. Parasitol. 3:143–155.

    PubMed  CAS  Google Scholar 

  • Cataldi de Flombaum, M. A., Cannata, J. J. B., Cazzulo, J. J., and Segura, E. L., 1977, CO2-fixing enzymes in Trypanosoma cruzi, Comp. Biochem. Physiol 58B:67–69.

    Google Scholar 

  • Cataldi de Flombaum, M. A., Frasch, A. C. C., and Stoppani, A. O. M., 1979, Adenosine triphosphatase from Trypanosoma cruzi: Purification and properties, Comp. Biochem. Physiol. 65B:103–109.

    Google Scholar 

  • Cazzulo, J. J., 1984, Protein and amino acid catabolism in Trypanosoma cruzi, Comp. Biochem. Physiol. 79B:309–320.

    CAS  Google Scholar 

  • Cazzulo, J. J., Juan, S. M., and Segura, E. L., 1977, Glutamate dehydrogenase and aspartate aminotransferase in Trypanosoma cruzi, Comp. Biochem. Physiol. 56B:301–303.

    Google Scholar 

  • Cazzulo, J. J., Franke de Cazzulo, B. M., Higa, A. L, and Segura, E. L., 1979, NAD-linked glutamate dehydrogenase in Trypanosoma cruzi, Comp. Biochem. Physiol 64B:129–131.

    CAS  Google Scholar 

  • Cazzulo, J. J., Valle, E., Docampo, R., and Cannata, J. J. B., 1980, Intracellular distribution of CO2-fixing enzymes in Trypanosoma cruzi and Crithidia fasciculata, J. Gen. Microbiol. 117:271–274.

    PubMed  CAS  Google Scholar 

  • Cazzulo, J. J., Franke de Cazzulo, B. M., Engel, J. C., and Cannata, J. J. B., 1985, End products and enzyme levels of aerobic glucose fermentation in Trypanosomatids, Mol. Biochem. Parasitol. 16:329–343.

    PubMed  CAS  Google Scholar 

  • Cazzulo, J. J., Arauzo, S., Franke de Cazzulo, B. M., and Cannata, J. J. B., 1988a, On the production of glycerol and L-alanine during the aerobic fermentation of glucose by Trypanosomatids, FEMS Microbiol Lett. 51:187–192.

    CAS  Google Scholar 

  • Cazzulo, J. J., Nowicki, C., Santomé, J. A., Wernstedt, C., and Hellman, U., 1988b, Amino acid composition and N-terminal sequence of the NADP-linked glutamate dehydrogenase from Trypanosoma cruzi, FEMS Microbiol. Lett. 56:215–220.

    CAS  Google Scholar 

  • Cazzulo, J. J., Couso, R., Raimondi, A., Wernstedt, C., and Hellman, U., 1989a, Further characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi, Mol. Biochem. Parasitol. 33:33–41.

    PubMed  CAS  Google Scholar 

  • Cazzulo, J. J., Cazzulo Franke, M. C., and Franke de Cazzulo, B. M., 1989b, On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes, FEMS Microbiol. Lett. 59:259–264.

    CAS  Google Scholar 

  • Cazzulo, J. J., Hellman, U., Couso, R., and Parodi, A. J. A., 1990a, Amino acid and carbohydrate composition of a lysosomal cysteine proteinase from Trypanosoma cruzi. Absence of phosphorylated mannose residues, Mol. Biochem. Parasitol. 38:41–48.

    PubMed  CAS  Google Scholar 

  • Cazzulo, J. J., Cazzulo Franke, M. C., Martinez, J., and Franke de Cazzulo, B. M., 1990b, Some kinetic properties of a cysteine proteinase (Cruzipain) from Trypanosoma cruzi, Biochim. Biophys. Acta 1037:186–191.

    PubMed  CAS  Google Scholar 

  • Chang, S. L., 1948, Studies on hemoflagellates. IV. Observations concerning some biochemical activities in culture, and respiration of three species of Leishmanias and Trypanosoma cruzi, J. Infect. Dis. 82:109–121.

    PubMed  CAS  Google Scholar 

  • Contreras, V. T., Salles, J. M., Thomas, N., Morel, C. M., and Goldenberg, S., 1985, In vitro differentiation of Trypanosoma cruzi under chemically defined conditions, Mol. Biochem. Parasitai. 16:315–327.

    CAS  Google Scholar 

  • Coronel, C. E., Rovai, L. E., Gerez de Burgos, N. M., Burgos, C., and Blanco, A., 1981, Properties of α-hydroxyacid dehydrogenase isoenzymes from Trypanosoma cruzi, Mol. Biochem. Parasitol. 4:29–38.

    PubMed  CAS  Google Scholar 

  • Dahlmann, B., Kopp, F., Kuehn, L., Niedel, B., Pfeifer, G., Hegerl, R., and Baumeister, W., 1989, The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria, FEBS Lett. 251:125–131.

    PubMed  CAS  Google Scholar 

  • De los Santos, C., Buldain, G., Frydman, B., Cannata, J. J. B., and Cazzulo, J. J., 1985, Carbon-13 nuclear magnetic resonance analysis of (1-13C)-glucose metabolism in Crithidia fasciculata Evidence of CO2 fixation by phosphoenolpyruvate carboxykinase, Eur. J. Biochem. 149:421–429.

    PubMed  Google Scholar 

  • De Sastre, M. B. R., and Stoppani, A. O. M., 1973, Demonstration of Mg2+-activated adenosine triphosphatase in Trypanosoma cruzi, FEBS Lett. 31:137–142.

    PubMed  Google Scholar 

  • DeSouza, W., 1984, Cell biology of Trypanosoma cruzi, Int. Rev. Cytol. 86:197–285.

    CAS  Google Scholar 

  • Eakin, A. E., Bouvier, J., Sakanari, J. A., Craik, C. S., and McKerrow, J. H., 1990, Amplification and sequencing of genomic DNA fragments encoding cysteine proteinases from protozoan parasites, Mol. Biochem. Parasitol. 39:1–8.

    PubMed  CAS  Google Scholar 

  • Engel, J. C., Franke de Cazzulo, B. M., Stoppani, A. O. M., Cannata, J. J. B., and Cazzulo, J. J., 1987, Aerobic glucose fermentation by Trypanosoma cruzi axenic culture amastigote-like forms during growth and differentiation to epimastigotes, Mol. Biochem. Parasitol. 25:1–10.

    Google Scholar 

  • Frasch, A. C. C., Segura, E. L., Cazzulo, J. J., and Stoppani, A. O. M., 1978a, Adenosine triphosphatase activities in Trypanosoma cruzi, Comp. Biochem. Physiol. 60B:271–275.

    CAS  Google Scholar 

  • Frasch, A. C. C., Cazzulo, J. J., and Stoppani, A. O. M., 1978b, Solubilization and some properties of the Mg2+-activated adenosine triphosphatase from Trypanosoma cruzi, Comp. Biochem. Physiol. 61B:207–212.

    CAS  Google Scholar 

  • Frydman, B., de los Santos, C., Cannata, J. J. B., and Cazzulo, J. J., 1990, Carbon-13 nuclear magnetic resonance analysis of [1-13C]glucose metabolism in Trypanosoma cruzi. Evidence of the presence of two alanine pools and of two CO2 fixation reactions, Eur. J. Biochem. 192:363–368.

    PubMed  CAS  Google Scholar 

  • Grieg, S., and Ashall, F., 1990, Electrophoretic detection of Trypanosoma cruzi peptidases, Mol. Biochem. Parasitol. 39:31–38.

    Google Scholar 

  • Gutteridge, W. E., 1981, Trypanosoma cruzi: Recent biochemical advances, Trans. R. Soc. Trop. Med. Hyg. 75:484–492.

    PubMed  CAS  Google Scholar 

  • Gutteridge, W. E., and Rogerson, G. W., 1979, Biochemical aspects of the biology of Trypanosoma cruzi, in Biology of the Kinetoplastida, Vol. 2 (W. H. Lumsden and D. A. Evans, eds.), pp. 619–652, Academic Press, London.

    Google Scholar 

  • Gutteridge, W. E., Cover, B., and Gaborak, M., 1978, Isolation of blood and intracellular forms of Trypanosoma cruzi and preliminary study of their metabolism, Parasitology 76:159–176.

    PubMed  CAS  Google Scholar 

  • Itow, S., and Camargo, E. P., 1977, Proteolytic activities in cell extracts of Trypanosoma cruzi, J. Protozool. 24:591–595.

    PubMed  CAS  Google Scholar 

  • Juan, S. M., Cazzulo, J. J., and Segura, E. L., 1976, The pyruvate kinase from Trypanosoma cruzi, Acta Physiol. Latinoam. 26:424–426.

    CAS  Google Scholar 

  • Juan, S. M., Cazzulo, J. J., and Segura, E. L., 1977, The citrate synthase from Trypanosoma cruzi, J. Parasitol. 63:921–922.

    PubMed  CAS  Google Scholar 

  • Juan, S. M., Segura, E. L., and Cazzulo, J. J., 1978, Purification and some properties of the NADP-linked glutamate dehydrogenase from Trypanosoma cruzi, Int. J. Biochem. 9:395–400.

    PubMed  CAS  Google Scholar 

  • Krettli, A., Thomas, N., and Eisen, H., 1980, Escape mechanisms of Trypanosoma cruzi from the host immune system, in Les Colloques de l’INSERM. Cancer Immunology and Parasite Immunology, Vol. 97 (L. Israel, P. Lagrange, and J. C. Salomon, eds.), pp. 553–558, INSERM, Paris.

    Google Scholar 

  • Kusel, J. P., and Storey, B. T., 1972, Evidence for the presence of two phosphorylation sites in mitochondria isolated from the trypanosomatid hemoflagellate Crithidia fasciculata, Biochem. Biophys. Res. Commun. 46:501–507.

    PubMed  CAS  Google Scholar 

  • Mancilla, R., and Náquira, C., 1964, Comparative metabolism of 14C-glucose in two strains of Trypanosoma cruzi, J. Protozool. 11:509–513.

    PubMed  CAS  Google Scholar 

  • Mancilla, R., Náquira, C., and Lanas, C., 1967, Protein biosynthesis in Trypanosomatidae. II. The metabolic fate of DL-leucine-1-13C in Trypanosoma cruzi, Exp. Parasitol. 21:154–159.

    PubMed  CAS  Google Scholar 

  • Miles, M. A., Souza, A., Póvoa, M., Shaw, J. J., Lainson, R., and Toyé, P. J., 1978, Isozymic heterogeneity of Trypanosoma cruzi in the first autochtonous patients with Chagas’ disease in Amazonian Brazil, Nature 272:819–821.

    PubMed  CAS  Google Scholar 

  • Miles, M. A., Lanham, S. M., de Souza, A. A., and Póvoa, M., 1980, Further enzymic characters of Trypanosoma cruzi and their evaluation for strain identification, Trans. R. Soc. Trop. Med. Hyg. 74:221–237.

    PubMed  CAS  Google Scholar 

  • Montamat, E. E., Arauzo, S. S., and Blanco, A., 1987, Subcellular localization of leucine aminotransferase and α-hydroxyacid dehydrogenase in Trypanosoma cruzi, Mol. Biochem. Parasitol. 22:185–193.

    PubMed  CAS  Google Scholar 

  • Mottram, J. C., North, M. J., Barry, J. D., and Coombs, G. H., 1989, A cysteine proteinase cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension, FEBS Lett. 258:211–215.

    PubMed  CAS  Google Scholar 

  • Nosei, C., and Avila, J. L., 1985, Serine hydroxymethyltransferase activity in Trypanosoma cruzi, Trypanosoma rangeli and American Leishmania spp., Comp. Biochem. Physiol. 81:701–704.

    CAS  Google Scholar 

  • O’Daly, J. A., Serrano, L. E., and Rodriguez, M. B., 1983, Free amino acid pool and proteolytic enzymes in Trypanosoma cruzi cultured in vitro, Int. J. Parasitol. 13:433–440.

    PubMed  Google Scholar 

  • Opperdoes, F. R., 1987, Compartmentation of carbohydrate metabolism in Trypanosomes, Annu. Rev. Microbiol. 41:127–151.

    PubMed  CAS  Google Scholar 

  • Opperdoes, F. R., and Borst, P., 1977, Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: The glycosome, FEBS Lett. 80:360–364.

    PubMed  CAS  Google Scholar 

  • Opperdoes, F. R., de Rijke, D., and Borst, P., 1976, Reactions involved in energy transfer in trypanosomes. I. Characterization of the mitochondrial adenine nucleotide translocator and the ATPase of Crithidia luciliae, Comp. Biochem. Physiol. 54B:7–12.

    Google Scholar 

  • Opperdoes, F. R., Borst, P., Bakker, S., and Leene, W., 1977, Localization of glycerol-3-phosphate oxidase in the mitochondrion and particulate NAD+-linked glycerol-3-phosphate dehydrogenase in the microbodies of the bloodstream form of Trypanosoma brucei, Eur. J. Biochem. 76:29–39.

    PubMed  CAS  Google Scholar 

  • Piras, M. M., Henriquez, D., and Piras, R., 1985, The effect of proteolytic enzymes and protease inhibitors on the interaction Trypanosoma cruzi-fibroblasts, Mol. Biochem. Parasitol. 14:151–163.

    PubMed  CAS  Google Scholar 

  • Racagni, G. E., and Machado de Domenech, E. E., 1983, Characterization of Trypanosoma cruzi hexokinase, Mol. Biochem. Parasitol. 9:181–188.

    PubMed  CAS  Google Scholar 

  • Rangel, H. A., Araújo, P. M. F., Repka, D., and Costa, M. G., 1981a, Trypanosoma cruzi: Isolation and characterization of a proteinase, Exp. Parasitol. 52:199–209.

    PubMed  CAS  Google Scholar 

  • Rangel, H. A., Araújo, P. M. F., Camargo, I. J. B., Bonfitto, M., Repka, D., Sakurada, J., and Atta, A. M., 1981b, Detection of a proteinase common to epimastigote, trypomastigote and amastigote of different strains of Trypanosoma cruzi, Tropenmed. Parasit. 32:87–92.

    CAS  Google Scholar 

  • Raw, I., 1959, Some aspects of carbohydrate metabolism of cultural forms of Trypanosoma cruzi, Rev. Inst. Med. Trop. Sao Paulo 1:192–194.

    CAS  Google Scholar 

  • Rodriguez, F., Ramirez, J. L., and Rangel-Aldao, R., 1990, Gene expression of tubulin during the differentiation of Trypanosoma cruzi, Abstracts, VIPAABS Congress, Sao Paulo, Brazil, p. 70.

    Google Scholar 

  • Ryley, J. F., 1956, Studies on the metabolism of Protozoa. 7. Comparative carbohydrate metabolism of eleven species of Trypanosome, Biochem. J. 62:215–222.

    PubMed  CAS  Google Scholar 

  • Sakanari, J. A., Staunton, C. E., Eakin, A. E., Craik, C. S., and McKerrow, J. H., 1989, Serine proteases from nematode and protozoan parasites: Isolation of sequence homologs using generic molecular probes, Proc. Natl. Acad. Sci. USA 86:4863–4867.

    PubMed  CAS  Google Scholar 

  • Schwarcz de Tarlovsky, M. S., Affranchino, J. L., Stoppani, A. O. M., Isola, E. L. D., Lammel, E. M., and Gonzalez Cappa, S. M., 1985, Citocromos en diferentes estadios; cepas y poblaciones de Trypanosoma cruzi, Rev. Arg. Microbiol. 17:121–130.

    CAS  Google Scholar 

  • van Schaftingen, E., Opperdoes, F. R., and Hers, H.-G., 1985, Stimulation of Trypanosoma brueei pyruvate kinase by fructose 2,6-bisphosphate, Eur. J. Biochem. 153:403–406.

    PubMed  Google Scholar 

  • Stoppani, A. O. M., and Boiso, J. F. de, 1973, Oxidative phosphorylation in Trypanosoma cruzi, Experientia 29:1494–1496.

    PubMed  CAS  Google Scholar 

  • Stoppani, A. O. M., Docampo, R., Boiso, J. F. de, and Frasch, A. C. C., 1980, Effect of inhibitors of electron transport and oxidative phosphorylation on Trypanosoma cruzi respiration and growth, Mol. Biochem. Parasitol. 2:3–21.

    PubMed  CAS  Google Scholar 

  • Sylvester, D., and Krassner, S. M., 1976, Proline metabolism in Trypanosoma cruzi epimastigotes, Comp. Biochem. Physiol. 55B:443–447.

    Google Scholar 

  • Taylor, M. B., and Gutteridge, W. E., 1986a, The occurrence and distribution of α-hydroxy-acid dehydrogenase in some members of the order Kinetoplastida, FEBS Lett. 199:237–241.

    PubMed  CAS  Google Scholar 

  • Taylor, M. B., and Gutteridge, W. E., 1986b, The regulation of phosphofructokinase in epimastigote Trypanosoma cruzi, FEBS Lett. 201:262–266.

    PubMed  CAS  Google Scholar 

  • Taylor, M. B., and Gutteridge, W. E., 1987, Trypanosoma cruzi: Subcellular distribution of glycolytic and some related enzymes in epimastigotes, Exp. Parasitol. 63:84–97.

    PubMed  CAS  Google Scholar 

  • Taylor, M. B., Berghausen, H., Heyworth, P., Messenger, N., Rees, L. J., and Gutteridge, W. E., 1980, Subcellular localisation of some glycolytic enzymes in parasitic flagellated protozoa, Int. J. Biochem. 11:117–120.

    PubMed  CAS  Google Scholar 

  • Teixeira, A. R. L., and Santana, J. M., 1989, Trypanosoma cruzi: Endocytosis and degradation of specific antibodies by parasite forms, Am. J. Trop. Med. Hyg. 40:165–170.

    PubMed  CAS  Google Scholar 

  • Toner, J. J., and Weber, M. M., 1972, Respiratory control in mitochondria from Crithidia fasciculata, Biochim. Biophys. Res. Commun. 46:652–660.

    CAS  Google Scholar 

  • Urbina, J. A., 1987, The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: Molecular, kinetic, and regulatory properties, Arch. Biochem. Biophys. 258:186–195.

    PubMed  CAS  Google Scholar 

  • Urbina, J. A., and Azavache, V., 1984, Regulation of energy metabolism in Trypanosoma (Schizotrypanum) cruzi epimastigotes. II. NAD+-dependent glutamate dehydrogenase, Mol. Biochem. Parasitol. 11:241–255.

    PubMed  CAS  Google Scholar 

  • Urbina, J. A., and Crespo, A., 1984, Regulation of energy metabolism in Trypanosoma (Schizotrypanum) cruzi epimastigotes. I. Hexokinase and phosphofructokinase, Mol. Biochem. Parasitol. 11:225–239.

    PubMed  CAS  Google Scholar 

  • Urbina, J. A., Osorno, C. E., and Rojas, A., 1989, The central role of phosphoenol pyruvate carboxykinase in the energy metabolism of Trypanosoma cruzi. Studies using 3-mercaptopicolinic acid, Mem. Inst. Oswaldo Cruz 84(Suppl. II):59.

    Google Scholar 

  • Von Brand, Th., 1979, Biochemistry and Physiology of Endoparasites, Elsevier/North Holland, Amsterdam.

    Google Scholar 

  • Walter, R. D., and Ebert, F., 1979, Evidence for NADH-and NADPH-linked glutamate dehydrogenases in Trypanosoma cruzi epimastigotes, J. Protozool. 26:653–656.

    PubMed  CAS  Google Scholar 

  • Williamson, J., and Desowitz, R. S., 1961, The chemical composition of trypanosomes. I. Protein, amino acid and sugar analysis, Exp. Parasitol. 11:161–175.

    PubMed  CAS  Google Scholar 

  • Yoshida, N., and Camargo, E. P., 1978, Ureotelism and ammonotelism in Trypanosomatids, J. Bacteriol. 136:1184–1186.

    PubMed  CAS  Google Scholar 

  • Zeledón, R., 1960, Comparative physiological studies on four species of hemoflagellates in culture. V. Transaminases, Rev. Brasil. Biol. 20:309–414.

    Google Scholar 

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© 1992 Springer Science+Business Media New York

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Cazzulo, J.J. (1992). Energy Metabolism in Trypanosoma cruzi . In: Avila, J.L., Harris, J.R. (eds) Intracellular Parasites. Subcellular Biochemistry, vol 18. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1651-8_7

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  • DOI: https://doi.org/10.1007/978-1-4899-1651-8_7

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