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Lack of Arginine Decarboxylase in Trypanosoma cruzi Epimastigotes
Author(s) -
CARRILLO CAROLINA,
CEJAS SILVINA,
HUBER ALEJANDRA,
GONZÁLEZ NÉLIDA S.,
ALGRANATI ISRAEL D.
Publication year - 2003
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.2003.tb00141.x
Subject(s) - arginine decarboxylase , trypanosoma cruzi , agmatine , putrescine , arginine , biology , biochemistry , enzyme , spermidine , polyamine , arginase , in vivo , microbiology and biotechnology , amino acid , parasite hosting , computer science , world wide web
. 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 CO 2 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.