FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii

Detalhes bibliográficos
Autor(a) principal: Cruz, Laura Nogueira da
Data de Publicação: 2011
Outros Autores: Alves, Eduardo, Leal, Monica Teixeira, Juliano, Maria Aparecida [UNIFESP], Rosenthal, Philip J., Juliano, Luiz [UNIFESP], Garcia, Célia Regina da Silva
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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spelling 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
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