L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis.
Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the infection in the mammalian host. L-arginine is not synthesized b...
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ftdoajarticles:oai:doaj.org/article:5d276a9c5b0f4bcc82cef116fc506b06 2023-05-15T15:16:40+02:00 L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. Juliana Ide Aoki Sandra Marcia Muxel Ricardo Andrade Zampieri Stephanie Maia Acuña Juliane Cristina Ribeiro Fernandes Rubia Heloisa Vanderlinde Maria Carmen Oliveira de Pinho Sales Lucile Maria Floeter-Winter 2017-10-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0006025 https://doaj.org/article/5d276a9c5b0f4bcc82cef116fc506b06 EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC5693463?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0006025 https://doaj.org/article/5d276a9c5b0f4bcc82cef116fc506b06 PLoS Neglected Tropical Diseases, Vol 11, Iss 10, p e0006025 (2017) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2017 ftdoajarticles https://doi.org/10.1371/journal.pntd.0006025 2022-12-31T06:33:24Z Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the infection in the mammalian host. L-arginine is not synthesized by the parasite, so its uptake occurs through the amino acid permease 3 (AAP3). AAP3 is codified by two copies genes (5.1 and 4.7 copies), organized in tandem in the parasite genome. One copy presents the expression regulated by L-arginine availability.RNA-seq data revealed 14 amino acid transporters differentially expressed in the comparison of La-WT vs. La-arg- promastigotes and axenic amastigotes. The 5.1 and 4.7 aap3 transcripts were down-regulated in La-WT promastigotes vs. axenic amastigotes, and in La-WT vs. La-arg- promastigotes. In contrast, transcripts of other transporters were up-regulated in the same comparisons. The amount of 5.1 and 4.7 aap3 mRNA of intracellular amastigotes was also determined in sample preparations from macrophages, obtained from BALB/c and C57BL/6 mice and the human THP-1 lineage infected with La-WT or La-arg-, revealing that the genetic host background is also important. We also determined the aap3 mRNA and AAP3 protein amounts of promastigotes and axenic amastigotes in different environmental growth conditions, varying pH, temperature and L-arginine availability. Interestingly, the increase of temperature increased the AAP3 level in plasma membrane and consequently the L-arginine uptake, independently of pH and L-arginine availability. In addition, we demonstrated that besides the plasma membrane localization, AAP3 was also localized in the glycosome of L. amazonensis promastigotes and axenic amastigotes.In this report, we described the differential transcriptional profiling of amino acids transporters from La-WT and La-arg- promastigotes and axenic amastigotes. We also showed the increased AAP3 levels under amino acid starvation or its decrease in L-arginine supplementation. The ... Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLOS Neglected Tropical Diseases 11 10 e0006025 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Juliana Ide Aoki Sandra Marcia Muxel Ricardo Andrade Zampieri Stephanie Maia Acuña Juliane Cristina Ribeiro Fernandes Rubia Heloisa Vanderlinde Maria Carmen Oliveira de Pinho Sales Lucile Maria Floeter-Winter L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the infection in the mammalian host. L-arginine is not synthesized by the parasite, so its uptake occurs through the amino acid permease 3 (AAP3). AAP3 is codified by two copies genes (5.1 and 4.7 copies), organized in tandem in the parasite genome. One copy presents the expression regulated by L-arginine availability.RNA-seq data revealed 14 amino acid transporters differentially expressed in the comparison of La-WT vs. La-arg- promastigotes and axenic amastigotes. The 5.1 and 4.7 aap3 transcripts were down-regulated in La-WT promastigotes vs. axenic amastigotes, and in La-WT vs. La-arg- promastigotes. In contrast, transcripts of other transporters were up-regulated in the same comparisons. The amount of 5.1 and 4.7 aap3 mRNA of intracellular amastigotes was also determined in sample preparations from macrophages, obtained from BALB/c and C57BL/6 mice and the human THP-1 lineage infected with La-WT or La-arg-, revealing that the genetic host background is also important. We also determined the aap3 mRNA and AAP3 protein amounts of promastigotes and axenic amastigotes in different environmental growth conditions, varying pH, temperature and L-arginine availability. Interestingly, the increase of temperature increased the AAP3 level in plasma membrane and consequently the L-arginine uptake, independently of pH and L-arginine availability. In addition, we demonstrated that besides the plasma membrane localization, AAP3 was also localized in the glycosome of L. amazonensis promastigotes and axenic amastigotes.In this report, we described the differential transcriptional profiling of amino acids transporters from La-WT and La-arg- promastigotes and axenic amastigotes. We also showed the increased AAP3 levels under amino acid starvation or its decrease in L-arginine supplementation. The ... |
format |
Article in Journal/Newspaper |
author |
Juliana Ide Aoki Sandra Marcia Muxel Ricardo Andrade Zampieri Stephanie Maia Acuña Juliane Cristina Ribeiro Fernandes Rubia Heloisa Vanderlinde Maria Carmen Oliveira de Pinho Sales Lucile Maria Floeter-Winter |
author_facet |
Juliana Ide Aoki Sandra Marcia Muxel Ricardo Andrade Zampieri Stephanie Maia Acuña Juliane Cristina Ribeiro Fernandes Rubia Heloisa Vanderlinde Maria Carmen Oliveira de Pinho Sales Lucile Maria Floeter-Winter |
author_sort |
Juliana Ide Aoki |
title |
L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
title_short |
L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
title_full |
L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
title_fullStr |
L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
title_full_unstemmed |
L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis. |
title_sort |
l-arginine availability and arginase activity: characterization of amino acid permease 3 in leishmania amazonensis. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2017 |
url |
https://doi.org/10.1371/journal.pntd.0006025 https://doaj.org/article/5d276a9c5b0f4bcc82cef116fc506b06 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 11, Iss 10, p e0006025 (2017) |
op_relation |
http://europepmc.org/articles/PMC5693463?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0006025 https://doaj.org/article/5d276a9c5b0f4bcc82cef116fc506b06 |
op_doi |
https://doi.org/10.1371/journal.pntd.0006025 |
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PLOS Neglected Tropical Diseases |
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11 |
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10 |
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