Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi
Wild-type Trypanosoma cruzi epimastigotes lack arginine decarboxylase (ADC) enzymatic activity. However, the transformation of these parasites with a recombinant plasmid containing the oat ADC cDNA coding region gave rise to the transient heterologous expression of the enzyme, suggesting the absence...
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2004
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paper:paper_03044165_v1674_n3_p223_Carrillo2023-06-08T15:29:50Z Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi Carrillo, Carolina Serra, María Pía Pereira, Claudio Alejandro González, Nélida Susana Algranati, Israel David Agmatine Arginine decarboxylase Polyamine biosynthesis Transgenic parasite Trypanosoma cruzi epimastigote alpha difluoromethylarginine arginine decarboxylase gene article bioinformatics biolistic transformation catalysis catalyst controlled study DNA sequence enzyme activity enzyme assay enzyme inhibition gene expression genetic code genetic recombination genome half life time heterologous expression intermethod comparison metabolic regulation nonhuman plant polymerase chain reaction priority journal reaction analysis sequence analysis stoichiometry transgene Trypanosoma cruzi wild type Amino Acid Sequence Animals Animals, Genetically Modified Avena sativa Base Sequence Carboxy-Lyases DNA Primers DNA, Complementary Enzyme Inhibitors Molecular Sequence Data Open Reading Frames Recombinant Proteins Transfection Trypanosoma cruzi Trypanosoma Trypanosoma cruzi Wild-type Trypanosoma cruzi epimastigotes lack arginine decarboxylase (ADC) enzymatic activity. However, the transformation of these parasites with a recombinant plasmid containing the oat ADC cDNA coding region gave rise to the transient heterologous expression of the enzyme, suggesting the absence of endogenous mechanisms that could inhibit the expression of a hypothetical own ADC gene or the assay used to measure its enzymatic activity. The foreign ADC enzyme expressed in the transgenic T. cruzi was characterized by identification of the products, the stoichiometry of the catalysed reaction, the specific inhibition by α-difluoromethylarginine (DFMA) and the study of its metabolic turnover. The half-life of the heterologous ADC activity in T. cruzi was about 150 min. Bioinformatics studies and polymerase chain reaction (PCR) analyses seem to indicate the absence of ADC-like DNA sequences in the wild-type T. cruzi genome. © 2004 Published by Elsevier B.V. Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Serra, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044165_v1674_n3_p223_Carrillo http://hdl.handle.net/20.500.12110/paper_03044165_v1674_n3_p223_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 Arginine decarboxylase Polyamine biosynthesis Transgenic parasite Trypanosoma cruzi epimastigote alpha difluoromethylarginine arginine decarboxylase gene article bioinformatics biolistic transformation catalysis catalyst controlled study DNA sequence enzyme activity enzyme assay enzyme inhibition gene expression genetic code genetic recombination genome half life time heterologous expression intermethod comparison metabolic regulation nonhuman plant polymerase chain reaction priority journal reaction analysis sequence analysis stoichiometry transgene Trypanosoma cruzi wild type Amino Acid Sequence Animals Animals, Genetically Modified Avena sativa Base Sequence Carboxy-Lyases DNA Primers DNA, Complementary Enzyme Inhibitors Molecular Sequence Data Open Reading Frames Recombinant Proteins Transfection Trypanosoma cruzi Trypanosoma Trypanosoma cruzi |
| spellingShingle |
Agmatine Arginine decarboxylase Polyamine biosynthesis Transgenic parasite Trypanosoma cruzi epimastigote alpha difluoromethylarginine arginine decarboxylase gene article bioinformatics biolistic transformation catalysis catalyst controlled study DNA sequence enzyme activity enzyme assay enzyme inhibition gene expression genetic code genetic recombination genome half life time heterologous expression intermethod comparison metabolic regulation nonhuman plant polymerase chain reaction priority journal reaction analysis sequence analysis stoichiometry transgene Trypanosoma cruzi wild type Amino Acid Sequence Animals Animals, Genetically Modified Avena sativa Base Sequence Carboxy-Lyases DNA Primers DNA, Complementary Enzyme Inhibitors Molecular Sequence Data Open Reading Frames Recombinant Proteins Transfection Trypanosoma cruzi Trypanosoma Trypanosoma cruzi Carrillo, Carolina Serra, María Pía Pereira, Claudio Alejandro González, Nélida Susana Algranati, Israel David Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| topic_facet |
Agmatine Arginine decarboxylase Polyamine biosynthesis Transgenic parasite Trypanosoma cruzi epimastigote alpha difluoromethylarginine arginine decarboxylase gene article bioinformatics biolistic transformation catalysis catalyst controlled study DNA sequence enzyme activity enzyme assay enzyme inhibition gene expression genetic code genetic recombination genome half life time heterologous expression intermethod comparison metabolic regulation nonhuman plant polymerase chain reaction priority journal reaction analysis sequence analysis stoichiometry transgene Trypanosoma cruzi wild type Amino Acid Sequence Animals Animals, Genetically Modified Avena sativa Base Sequence Carboxy-Lyases DNA Primers DNA, Complementary Enzyme Inhibitors Molecular Sequence Data Open Reading Frames Recombinant Proteins Transfection Trypanosoma cruzi Trypanosoma Trypanosoma cruzi |
| description |
Wild-type Trypanosoma cruzi epimastigotes lack arginine decarboxylase (ADC) enzymatic activity. However, the transformation of these parasites with a recombinant plasmid containing the oat ADC cDNA coding region gave rise to the transient heterologous expression of the enzyme, suggesting the absence of endogenous mechanisms that could inhibit the expression of a hypothetical own ADC gene or the assay used to measure its enzymatic activity. The foreign ADC enzyme expressed in the transgenic T. cruzi was characterized by identification of the products, the stoichiometry of the catalysed reaction, the specific inhibition by α-difluoromethylarginine (DFMA) and the study of its metabolic turnover. The half-life of the heterologous ADC activity in T. cruzi was about 150 min. Bioinformatics studies and polymerase chain reaction (PCR) analyses seem to indicate the absence of ADC-like DNA sequences in the wild-type T. cruzi genome. © 2004 Published by Elsevier B.V. |
| author |
Carrillo, Carolina Serra, María Pía Pereira, Claudio Alejandro González, Nélida Susana Algranati, Israel David |
| author_facet |
Carrillo, Carolina Serra, María Pía Pereira, Claudio Alejandro González, Nélida Susana Algranati, Israel David |
| author_sort |
Carrillo, Carolina |
| title |
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| title_short |
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| title_full |
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| title_fullStr |
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| title_full_unstemmed |
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi |
| title_sort |
heterologous expression of a plant arginine decarboxylase gene in trypanosoma cruzi |
| publishDate |
2004 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044165_v1674_n3_p223_Carrillo http://hdl.handle.net/20.500.12110/paper_03044165_v1674_n3_p223_Carrillo |
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