FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.1016/j.ijpara.2010.10.009 http://repositorio.unifesp.br/handle/11600/33483 |
Resumo: | Malaria is still a major health problem in developing countries. It is caused by the protist parasite Plasmodium, in which proteases are activated during the cell cycle. Ca(2+) is a ubiquitous signalling ion that appears to regulate protease activity through changes in its intracellular concentration. Proteases are crucial to Plasmodium development, but the role of Ca(2+) in their activity is not fully understood. Here we investigated the role of Ca(2+) in protease modulation among rodent Plasmodium spp. Using fluorescence resonance energy transfer (FRET) peptides, we verified protease activity elicited by Ca(2+) from the endoplasmatic reticulum (ER) after stimulation with thapsigargin (a sarco/endoplasmatic reticulum Ca(2+)-ATPase (SERCA) inhibitor) and from acidic compartments by stimulation with nigericin (a K(+)/H(+) exchanger) or monensin (a Na(+)/H(+) exchanger). Intracellular (BAPTA/AM) and extracellular (EGTA) Ca(2+) chelators were used to investigate the role played by Ca(2+) in protease activation. in Plasmodium berghei both EGTA and BAPTA blocked protease activation, whilst in Plasmodium yoelii these compounds caused protease activation. the effects of protease inhibitors on thapsigargin-induced proteolysis also differed between the species. Pepstatin A and phenylmethylsulphonyl fluoride (PMSF) increased thapsigargin-induced proteolysis in P. berghei but decreased it in P. yoelii. Conversely. E64 reduced proteolysis in P. berghei but stimulated it in P. yoelii. the data point out key differences in proteolytic responses to Ca(2+) between species of Plasmodium. (C) 2011 Australian Society for Parasitology Inc. Published by Elsevier B.V. All rights reserved. |
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FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoeliiMalariaPlasmodium bergheiPlasmodium yoeliiProtease activityCa(2+) modulationFRETMalaria is still a major health problem in developing countries. It is caused by the protist parasite Plasmodium, in which proteases are activated during the cell cycle. Ca(2+) is a ubiquitous signalling ion that appears to regulate protease activity through changes in its intracellular concentration. Proteases are crucial to Plasmodium development, but the role of Ca(2+) in their activity is not fully understood. Here we investigated the role of Ca(2+) in protease modulation among rodent Plasmodium spp. Using fluorescence resonance energy transfer (FRET) peptides, we verified protease activity elicited by Ca(2+) from the endoplasmatic reticulum (ER) after stimulation with thapsigargin (a sarco/endoplasmatic reticulum Ca(2+)-ATPase (SERCA) inhibitor) and from acidic compartments by stimulation with nigericin (a K(+)/H(+) exchanger) or monensin (a Na(+)/H(+) exchanger). Intracellular (BAPTA/AM) and extracellular (EGTA) Ca(2+) chelators were used to investigate the role played by Ca(2+) in protease activation. in Plasmodium berghei both EGTA and BAPTA blocked protease activation, whilst in Plasmodium yoelii these compounds caused protease activation. the effects of protease inhibitors on thapsigargin-induced proteolysis also differed between the species. Pepstatin A and phenylmethylsulphonyl fluoride (PMSF) increased thapsigargin-induced proteolysis in P. berghei but decreased it in P. yoelii. Conversely. E64 reduced proteolysis in P. berghei but stimulated it in P. yoelii. the data point out key differences in proteolytic responses to Ca(2+) between species of Plasmodium. (C) 2011 Australian Society for Parasitology Inc. Published by Elsevier B.V. All rights reserved.Univ São Paulo, Inst Biociencias, Dept Physiol, BR-05508900 São Paulo, BrazilUniv São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508900 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, BR-04044020 São Paulo, BrazilUniv Calif San Francisco, Dept Med, San Francisco, CA 94143 USAUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, BR-04044020 São Paulo, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Elsevier B.V.Universidade de São Paulo (USP)Universidade Federal de São Paulo (UNIFESP)Univ Calif San FranciscoCruz, Laura Nogueira daAlves, EduardoLeal, Monica TeixeiraJuliano, Maria Aparecida [UNIFESP]Rosenthal, Philip J.Juliano, Luiz [UNIFESP]Garcia, Célia Regina da Silva2016-01-24T14:06:13Z2016-01-24T14:06:13Z2011-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion363-372application/pdfhttp://dx.doi.org/10.1016/j.ijpara.2010.10.009International Journal for Parasitology. Oxford: Elsevier B.V., v. 41, n. 3-4, p. 363-372, 2011.10.1016/j.ijpara.2010.10.009WOS000288736700012.pdf0020-7519http://repositorio.unifesp.br/handle/11600/33483WOS:000288736700012engInternational Journal for Parasitologyinfo:eu-repo/semantics/openAccesshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-07-31T15:00:45Zoai:repositorio.unifesp.br/:11600/33483Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-07-31T15:00:45Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
title |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
spellingShingle |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii Cruz, Laura Nogueira da Malaria Plasmodium berghei Plasmodium yoelii Protease activity Ca(2+) modulation FRET |
title_short |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
title_full |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
title_fullStr |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
title_full_unstemmed |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
title_sort |
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii |
author |
Cruz, Laura Nogueira da |
author_facet |
Cruz, Laura Nogueira da Alves, Eduardo Leal, Monica Teixeira Juliano, Maria Aparecida [UNIFESP] Rosenthal, Philip J. Juliano, Luiz [UNIFESP] Garcia, Célia Regina da Silva |
author_role |
author |
author2 |
Alves, Eduardo Leal, Monica Teixeira Juliano, Maria Aparecida [UNIFESP] Rosenthal, Philip J. Juliano, Luiz [UNIFESP] Garcia, Célia Regina da Silva |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Federal de São Paulo (UNIFESP) Univ Calif San Francisco |
dc.contributor.author.fl_str_mv |
Cruz, Laura Nogueira da Alves, Eduardo Leal, Monica Teixeira Juliano, Maria Aparecida [UNIFESP] Rosenthal, Philip J. Juliano, Luiz [UNIFESP] Garcia, Célia Regina da Silva |
dc.subject.por.fl_str_mv |
Malaria Plasmodium berghei Plasmodium yoelii Protease activity Ca(2+) modulation FRET |
topic |
Malaria Plasmodium berghei Plasmodium yoelii Protease activity Ca(2+) modulation FRET |
description |
Malaria is still a major health problem in developing countries. It is caused by the protist parasite Plasmodium, in which proteases are activated during the cell cycle. Ca(2+) is a ubiquitous signalling ion that appears to regulate protease activity through changes in its intracellular concentration. Proteases are crucial to Plasmodium development, but the role of Ca(2+) in their activity is not fully understood. Here we investigated the role of Ca(2+) in protease modulation among rodent Plasmodium spp. Using fluorescence resonance energy transfer (FRET) peptides, we verified protease activity elicited by Ca(2+) from the endoplasmatic reticulum (ER) after stimulation with thapsigargin (a sarco/endoplasmatic reticulum Ca(2+)-ATPase (SERCA) inhibitor) and from acidic compartments by stimulation with nigericin (a K(+)/H(+) exchanger) or monensin (a Na(+)/H(+) exchanger). Intracellular (BAPTA/AM) and extracellular (EGTA) Ca(2+) chelators were used to investigate the role played by Ca(2+) in protease activation. in Plasmodium berghei both EGTA and BAPTA blocked protease activation, whilst in Plasmodium yoelii these compounds caused protease activation. the effects of protease inhibitors on thapsigargin-induced proteolysis also differed between the species. Pepstatin A and phenylmethylsulphonyl fluoride (PMSF) increased thapsigargin-induced proteolysis in P. berghei but decreased it in P. yoelii. Conversely. E64 reduced proteolysis in P. berghei but stimulated it in P. yoelii. the data point out key differences in proteolytic responses to Ca(2+) between species of Plasmodium. (C) 2011 Australian Society for Parasitology Inc. Published by Elsevier B.V. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-03-01 2016-01-24T14:06:13Z 2016-01-24T14:06:13Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.ijpara.2010.10.009 International Journal for Parasitology. Oxford: Elsevier B.V., v. 41, n. 3-4, p. 363-372, 2011. 10.1016/j.ijpara.2010.10.009 WOS000288736700012.pdf 0020-7519 http://repositorio.unifesp.br/handle/11600/33483 WOS:000288736700012 |
url |
http://dx.doi.org/10.1016/j.ijpara.2010.10.009 http://repositorio.unifesp.br/handle/11600/33483 |
identifier_str_mv |
International Journal for Parasitology. Oxford: Elsevier B.V., v. 41, n. 3-4, p. 363-372, 2011. 10.1016/j.ijpara.2010.10.009 WOS000288736700012.pdf 0020-7519 WOS:000288736700012 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
International Journal for Parasitology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
dc.format.none.fl_str_mv |
363-372 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
_version_ |
1814268359615709184 |