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 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 omithine 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.
Carrillo
Carolina
C
Fundación Instituto Leloir, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, CONICET. A. Machado 151, 1405 Buenos Aires, Argentina.
Cejas
Silvina
S
Huber
Alejandra
A
González
Nélida S
NS
Algranati
Israel D
ID
D000818:Animals; D001120:Arginine / Q000378:metabolism; D002262:Carboxy-Lyases / Q000172:deficiency* / Q000378:metabolism; D009952:Ornithine / Q000378:metabolism; D011700:Putrescine / Q000378:metabolism; D014349:Trypanosoma cruzi / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism
D001120:Arginine; D009952:Ornithine; D002262:Carboxy-Lyases; C019722:arginine decarboxylase; D011700:Putrescine