Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes
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 pa...
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_10665234_v50_n5_p312_Carrillo |
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todo:paper_10665234_v50_n5_p312_Carrillo2023-10-03T16:02:08Z Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes Carrillo, C. Cejas, S. Huber, A. González, N.S. Algranati, I.D. Agmatine Polyamine biosynthetic pathways Trypanosomatids enzyme activity Animals Arginine Carboxy-Lyases Ornithine Putrescine Trypanosoma cruzi Trypanosoma Trypanosoma cruzi 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10665234_v50_n5_p312_Carrillo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Agmatine Polyamine biosynthetic pathways Trypanosomatids enzyme activity Animals Arginine Carboxy-Lyases Ornithine Putrescine Trypanosoma cruzi Trypanosoma Trypanosoma cruzi |
| spellingShingle |
Agmatine Polyamine biosynthetic pathways Trypanosomatids enzyme activity Animals Arginine Carboxy-Lyases Ornithine Putrescine Trypanosoma cruzi Trypanosoma Trypanosoma cruzi Carrillo, C. Cejas, S. Huber, A. González, N.S. Algranati, I.D. Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| topic_facet |
Agmatine Polyamine biosynthetic pathways Trypanosomatids enzyme activity Animals Arginine Carboxy-Lyases Ornithine Putrescine Trypanosoma cruzi Trypanosoma Trypanosoma cruzi |
| description |
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. |
| format |
JOUR |
| author |
Carrillo, C. Cejas, S. Huber, A. González, N.S. Algranati, I.D. |
| author_facet |
Carrillo, C. Cejas, S. Huber, A. González, N.S. Algranati, I.D. |
| author_sort |
Carrillo, C. |
| title |
Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| title_short |
Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| title_full |
Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| title_fullStr |
Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| title_full_unstemmed |
Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes |
| title_sort |
lack of arginine decarboxylase in trypanosoma cruzi epimastigotes |
| url |
http://hdl.handle.net/20.500.12110/paper_10665234_v50_n5_p312_Carrillo |
| work_keys_str_mv |
AT carrilloc lackofargininedecarboxylaseintrypanosomacruziepimastigotes AT cejass lackofargininedecarboxylaseintrypanosomacruziepimastigotes AT hubera lackofargininedecarboxylaseintrypanosomacruziepimastigotes AT gonzalezns lackofargininedecarboxylaseintrypanosomacruziepimastigotes AT algranatiid lackofargininedecarboxylaseintrypanosomacruziepimastigotes |
| _version_ |
1807321747903479808 |