5-Aminolevulinic acid synthesis in epimastigotes of Trypanosoma cruzi
Background and aims: Trypanosoma cruzi is the causative agent of Chagas disease or American trypanosomiasis. The parasite manifests a nutritional requirement for heme compounds because of its biosynthesis deficiency. The aim of this study has been to investigate the presence of metabolites and enzym...
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| Otros Autores: | , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier Ltd
2003
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 10854caa a22010457a 4500 | ||
|---|---|---|---|
| 001 | PAPER-4889 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203429.0 | ||
| 008 | 190411s2003 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0038025755 | |
| 024 | 7 | |2 cas |a 5 aminolevulinate synthase, 9037-14-3; aminolevulinic acid, 106-60-5; aminotransferase, 9031-66-7; heme, 14875-96-8; porphobilinogen, 487-90-1; porphobilinogen synthase, 9036-37-7; porphyrin, 24869-67-8 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a IJBBF | ||
| 100 | 1 | |a Lombardo, M.E. | |
| 245 | 1 | 0 | |a 5-Aminolevulinic acid synthesis in epimastigotes of Trypanosoma cruzi |
| 260 | |b Elsevier Ltd |c 2003 | ||
| 270 | 1 | 0 | |m Batlle, A.Viamonte 1881, 10 A CP-1056 Buenos Aires, Argentina; email: batlle@mail.retina.ar |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Araujo, L.S., Lombardo, M.E., Batlle A.M.del, C., Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae (1994) The International Journal of Biochemistry & Cell Biology, 26, pp. 1377-1381 | ||
| 504 | |a Araujo, L.S., Lombardo, M.E., Rossetti, M.V., Batlle A.M.del, C., Saccharomyces cerevisiae Porphobilinogenase: Some physical and kinetic properties (1989) Comparative Biochemistry and Physiology, 92 B, pp. 297-301 | ||
| 504 | |a Demasi, M., Costa, C.A., Pascual, C., Llesuy, S., Bechara, E.J.H., Oxidative tissue response promoted by 5-aminolevulinic acid promptly induces the increase of plasma antioxidant capacity (1997) Free Radical Research, 26, pp. 235-243 | ||
| 504 | |a Drew, P.D., Ades, I.Z., Regulation of the stability of chicken embryo liver δ-aminolevulinate synthase mRNA by hemin (1989) Biochemical and Biophysical Research Communications, 162, pp. 102-107 | ||
| 504 | |a Foley, T., Beale, S.I., δ-Aminolevulinic acid formation from γ,δ-dioxovaleric acid in extracts of Euglena gracilis (1982) Plant Physiology, 70, pp. 1495-1502 | ||
| 504 | |a Hamilton, J.W., Bement, W.J., Sinclair, P.R., Sinclair, J.F., Alcedo, J.A., Wetterhahn, K.E., Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription (1991) Archives of Biochemistry and Biophysics, 289, pp. 387-392 | ||
| 504 | |a Hamilton, J.W., Bement, W.J., Sinclair, J.F., Wetterhahn, K.E., Expression of 5-aminolaevulinate synthase and cytochrome P450 mRNA in chicken embryo hepatocytes in vivo and in culture (1988) The Biochemical Journal, 255, pp. 267-275 | ||
| 504 | |a Jerzykowski, T., Winter, R., Matsuszewski, W., γ,δ-Dioxovalerate as a substrate for the glyoxalase enzyme system (1973) The Biochemical Journal, 135, pp. 713-719 | ||
| 504 | |a Lascelles, J., Adaptation to for bacteriochlorophyll in R. spheroides: Changes in activity of enzymes concerned in pyrrole synthesis (1959) The Biochemical Journal, 62, pp. 78-83 | ||
| 504 | |a Lombardo, M.E., Araujo, L.S., Juknat, A.A., Batlle A.M.del, C., Effect of illumination of growth, chlorophyll content and δ-aminolevulinic acid synthesis in Euglena gracilis (1988) Comparative Biochemistry and Physiology, 91, pp. 279-284 | ||
| 504 | |a Lombardo, M.E., Araujo, L.S., Juknat, A.A., Batlle A.M.del, C., Glutamate:4,5-dioxovaleric acid transaminase from Euglena gracilis (1989) European Journal of Biochemistry, 182, pp. 657-660 | ||
| 504 | |a Mauzerall, D., Granick, S., The occurrence and determination of ALA and PBG in urine (1956) The Journal of Biological Chemistry, 219, pp. 435-446 | ||
| 504 | |a Noguchi, T., Mori, R., Biosynthesis of porphyryn precursors in mammals. Identity of alanine:γ,δ-dioxovalerate aminotransferase with alanine:glyoxylate aminotransferase (1981) The Journal of Biological Chemistry, 256, pp. 10335-10339 | ||
| 504 | |a Pereira, B., Curi, R., Kokubun, E., Bechara, E.J.H., 5-Aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats (1992) Journal of Applied Physiology, 72, pp. 226-230 | ||
| 504 | |a Rimington, C., Spectral-absorption coefficients of some porphyrins in the Soret-band region (1960) The Biochemical Journal, 75, pp. 620-623 | ||
| 504 | |a Sagar, R., Salotra, P., Bhatnagar, R., Datta, K., L-Alanine:4,5-dioxovalerate transaminase in Leishmania donovani that differs from mammalian enzyme (1995) Microbiological Research, 150, pp. 419-423 | ||
| 504 | |a Salzman, T.A., Batlle A.M.del, C., De Souza, W., Heme synthesis in Trypanosoma cruzi: Influence of the strain and culture medium (1986) Comparative Biochemistry and Physiology, 83 B, pp. 57-61 | ||
| 504 | |a Salzman, T.A., Stella, A.M., Wider de Xifra, E.A., Batlle A.M.del, C., Docampo, R., Stoppani, A.O.M., Porphyrin biosynthesis in parasitic hemophlagellates: Functional and defective enzymes in Trypanosoma cruzi (1982) Comparative Biochemistry and Physiology, B72, pp. 663-667 | ||
| 504 | |a Segura, E.L., Subias, E., Esteva, M., Cabeza Meckert, P., Bronzina, A., Laguens, R.P., Características de infectividad de tres poblaciones de cultivo de Trypanosoma cruzi (1980) Medicina Buenos Aires, 40 (SUPPL. 1), pp. 97-102 | ||
| 504 | |a Shioi, Y., Nagamine, M., Sasa, T., Purification and properties of L-alanine:4,5-dioxovalerate aminotransferase from Chlorella regularis (1984) Archives of Biochemistry and Biophysics, 234, pp. 117-124 | ||
| 504 | |a Srivastava, P., Sharma, G.D., Kamboj, K.K., Rastogi, A.K., Pandey, V.C., Heme metabolism in promastigotes of Leishmania donovani (1997) Molecular and Cellular Biochemistry, 171, pp. 65-68 | ||
| 504 | |a Tuboi, S., Kim, H.J., Kikuchi, G., Occurrence and properties of two types of δ-aminolevulinate synthetase in Rhodopseudomonas spheroides (1970) Archives of Biochemistry and Biophysics, 138, pp. 147-154 | ||
| 504 | |a Varticovski, L., Kushner, J.P., Burnham, B.F., Biosynthesis of porphyrin precursors. Purification and characterization of mammaliam L-alanine:γ,δ-dioxovaleric acid aminotransferase (1980) The Journal of Biological Chemistry, 255, pp. 3742-3747 | ||
| 504 | |a Viale, A.A., Wider, E.A., Batlle A.M.del, C., Porphyrin biosynthesis in Rhodopseudomonas palustris. XI. Extraction and characterization of δ-aminolevulinate synthetase (1987) Comparative Biochemistry and Physiology, 87 B, pp. 607-613 | ||
| 520 | 3 | |a Background and aims: Trypanosoma cruzi is the causative agent of Chagas disease or American trypanosomiasis. The parasite manifests a nutritional requirement for heme compounds because of its biosynthesis deficiency. The aim of this study has been to investigate the presence of metabolites and enzymes of porphyrin pathway, as well as ALA formation in epimastigotes of T. cruzi, Tulahuén strain, Tul 2 stock. Methods: Succinyl CoA synthetase, 5-aminolevulinic acid (ALA) synthetase, 4,5-dioxovaleric (DOVA) transaminase, ALA dehydratase and porphobilinogenase activities, as well as ALA, porphobilinogen (PBG), free porphyrins and heme content were measured in a parasite cells-free extract. Extracellular content of these metabolites was also determined. Results: DOVA, PBG, porphyrins and heme were not detected in acellular extracts of T. cruzi. However ALA was detected both intra- and extracellularly This is the first time that the presence of ALA (98% of intracellularly formed ALA) is demonstrated in the extracellular medium of a parasite culture. Regarding the ALA synthesizing enzymes, DOVA transaminase levels found were low (7.13±0.49EU/mg protein), whilst ALA synthetase (ALA-S) activity was undetectable. A compound of non-protein nature, low molecular weight, heat unstable, inhibiting bacterial ALA-S activity was detected in an acellular extract of T. cruzi. This inhibitor could not be identified with either ALA, DOVA or heme. Conclusions: ALA synthesis is functional in the parasite and it would be regulated by the heme levels, both directly and through the inhibitor factor detected. ALA formed can not be metabolized further, because the necessary enzymes are not active, therefore it should be excreted to avoid intracellular cytotoxicity. © 2003 Elsevier Science Ltd. All rights reserved. |l eng | |
| 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: Marı́a Elisa Lombardo and Alcira Batlle hold the post of Scientific Researchers at the Argentine National Research Council (CONICET). Lidia Susana Araujo is a Research Fellow of the University of Buenos Aires. This work was supported by grants from the CONICET, the UBA and the Agencia of Promoción Cientı́fica y Tecnológica. | ||
| 593 | |a Ctro. Invest. Porfirinas y Porfirias, Cd. Univ. Pabellón II 2do, Piso, 1428 Buenos Aires, Argentina | ||
| 593 | |a Viamonte 1881, 10 A CP-1056 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a 5-AMINOLEVULINIC ACID |
| 690 | 1 | 0 | |a 5-AMINOLEVULINIC ACID SYNTHETASE INHIBITION |
| 690 | 1 | 0 | |a HEME SYNTHESIS |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a 4,5 DIOXOVALERIC TRANSAMINASE |
| 690 | 1 | 0 | |a 5 AMINOLEVULINATE SYNTHASE |
| 690 | 1 | 0 | |a AMINOLEVULINIC ACID |
| 690 | 1 | 0 | |a AMINOTRANSFERASE |
| 690 | 1 | 0 | |a BACTERIAL ENZYME |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a PORPHOBILINOGEN |
| 690 | 1 | 0 | |a PORPHOBILINOGEN SYNTHASE |
| 690 | 1 | 0 | |a PORPHYRIN |
| 690 | 1 | 0 | |a PORPHYRIN DERIVATIVE |
| 690 | 1 | 0 | |a SUCCINYL COENZYME A SYNTHETASE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a AMINO ACID METABOLISM |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CELL FREE SYSTEM |
| 690 | 1 | 0 | |a CYTOTOXICITY |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a EPIMASTIGOTE |
| 690 | 1 | 0 | |a METABOLITE |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a SYNTHESIS |
| 690 | 1 | 0 | |a THERMOSTABILITY |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a BACTERIA (MICROORGANISMS) |
| 690 | 1 | 0 | |a TRYPANOSOMA |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 700 | 1 | |a Araujo, L.S. | |
| 700 | 1 | |a Batlle, A. | |
| 773 | 0 | |d Elsevier Ltd, 2003 |g v. 35 |h pp. 1263-1271 |k n. 8 |p Int. J. Biochem. Cell Biol. |x 13572725 |w (AR-BaUEN)CENRE-5218 |t International Journal of Biochemistry and Cell Biology | |
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