Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi

Trypanosoma cruzi, the etiological agent of Chagas' disease, is the only eukaryotic cell which lacks the ability to synthesize polyamines de novo. In this work, we describe for the first time the molecular and biochemical properties of a high-affinity spermidine transporter from T. cruzi. The t...

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Autores principales: Carrillo, C., Canepa, G.E., Algranati, I.D., Pereira, C.A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v344_n3_p936_Carrillo
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spelling todo:paper_0006291X_v344_n3_p936_Carrillo2023-10-03T14:03:51Z Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi Carrillo, C. Canepa, G.E. Algranati, I.D. Pereira, C.A. Arginine Chagas' disease Permease Polyamines Putrescine Spermidine Trypanosoma cruzi amino acid arginine polyamine putrescine spermidine spermidine transporter unclassified drug article epimastigote gene expression nucleotide sequence polyamine synthesis priority journal protein determination protein expression protein transport Trypanosoma cruzi Xenopus laevis Amino Acid Sequence Animals Molecular Sequence Data Protein Binding Protozoan Proteins Spermidine Trypanosoma cruzi Eukaryota Trypanosoma cruzi Xenopus laevis Trypanosoma cruzi, the etiological agent of Chagas' disease, is the only eukaryotic cell which lacks the ability to synthesize polyamines de novo. In this work, we describe for the first time the molecular and biochemical properties of a high-affinity spermidine transporter from T. cruzi. The transporter gene TcPAT12 was functionally expressed in Xenopus laevis oocytes, showing high levels of spermidine uptake. Similar apparent affinity constants for spermidine uptake were obtained when comparing T. cruzi epimastigotes and heterologous expressed TcPAT12 in X. laevis. In addition, TcPAT12 also transports putrescine and the amino acid l-arginine at lower rates than spermidine. © 2006 Elsevier Inc. All rights reserved. Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Canepa, G.E. 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. Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v344_n3_p936_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 Arginine
Chagas' disease
Permease
Polyamines
Putrescine
Spermidine
Trypanosoma cruzi
amino acid
arginine
polyamine
putrescine
spermidine
spermidine transporter
unclassified drug
article
epimastigote
gene expression
nucleotide sequence
polyamine synthesis
priority journal
protein determination
protein expression
protein transport
Trypanosoma cruzi
Xenopus laevis
Amino Acid Sequence
Animals
Molecular Sequence Data
Protein Binding
Protozoan Proteins
Spermidine
Trypanosoma cruzi
Eukaryota
Trypanosoma cruzi
Xenopus laevis
spellingShingle Arginine
Chagas' disease
Permease
Polyamines
Putrescine
Spermidine
Trypanosoma cruzi
amino acid
arginine
polyamine
putrescine
spermidine
spermidine transporter
unclassified drug
article
epimastigote
gene expression
nucleotide sequence
polyamine synthesis
priority journal
protein determination
protein expression
protein transport
Trypanosoma cruzi
Xenopus laevis
Amino Acid Sequence
Animals
Molecular Sequence Data
Protein Binding
Protozoan Proteins
Spermidine
Trypanosoma cruzi
Eukaryota
Trypanosoma cruzi
Xenopus laevis
Carrillo, C.
Canepa, G.E.
Algranati, I.D.
Pereira, C.A.
Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
topic_facet Arginine
Chagas' disease
Permease
Polyamines
Putrescine
Spermidine
Trypanosoma cruzi
amino acid
arginine
polyamine
putrescine
spermidine
spermidine transporter
unclassified drug
article
epimastigote
gene expression
nucleotide sequence
polyamine synthesis
priority journal
protein determination
protein expression
protein transport
Trypanosoma cruzi
Xenopus laevis
Amino Acid Sequence
Animals
Molecular Sequence Data
Protein Binding
Protozoan Proteins
Spermidine
Trypanosoma cruzi
Eukaryota
Trypanosoma cruzi
Xenopus laevis
description Trypanosoma cruzi, the etiological agent of Chagas' disease, is the only eukaryotic cell which lacks the ability to synthesize polyamines de novo. In this work, we describe for the first time the molecular and biochemical properties of a high-affinity spermidine transporter from T. cruzi. The transporter gene TcPAT12 was functionally expressed in Xenopus laevis oocytes, showing high levels of spermidine uptake. Similar apparent affinity constants for spermidine uptake were obtained when comparing T. cruzi epimastigotes and heterologous expressed TcPAT12 in X. laevis. In addition, TcPAT12 also transports putrescine and the amino acid l-arginine at lower rates than spermidine. © 2006 Elsevier Inc. All rights reserved.
format JOUR
author Carrillo, C.
Canepa, G.E.
Algranati, I.D.
Pereira, C.A.
author_facet Carrillo, C.
Canepa, G.E.
Algranati, I.D.
Pereira, C.A.
author_sort Carrillo, C.
title Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
title_short Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
title_full Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
title_fullStr Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
title_full_unstemmed Molecular and functional characterization of a spermidine transporter (TcPAT12) from Trypanosoma cruzi
title_sort molecular and functional characterization of a spermidine transporter (tcpat12) from trypanosoma cruzi
url http://hdl.handle.net/20.500.12110/paper_0006291X_v344_n3_p936_Carrillo
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