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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Detalles Bibliográficos
Autores principales: Carrillo, C., Canepa, G.E., Algranati, I.D., Pereira, C.A.
Formato: JOUR
Materias:
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
Xenopus laevis
Amino Acid Sequence
Animals
Molecular Sequence Data
Protein Binding
Protozoan Proteins
Eukaryota
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v344_n3_p936_Carrillo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

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