Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.

Detalhes bibliográficos
Autor(a) principal: Cota, Renata Guerra de Sá
Data de Publicação: 2005
Outros Autores: Borges, William de Castro, Evangelista, Elísio Alberto, Kettelhut, Isis do Carmo, Rodrigues, Vanderlei
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFOP
Texto Completo: http://www.repositorio.ufop.br/handle/123456789/4284
https://doi.org/10.1016/j.exppara.2005.01.002
Resumo: Proteasomes are multi-subunit proteases involved in several mechanisms and thought to contribute to the regulation of cellular homeostasis. Here, we report for the Wrst time biochemical evidence for the existence of a ubiquitin–proteasome proteolytic pathway in this parasite. Proteasomes from both cercariae and adult worms exhibited a high preference for hydrolysis of the substrate Suc- LLVY-AMC, although in the cercariae extract the rate of hydrolysis was 50% lower when compared to adult worms extracts. The same diVerence in proteasome activities was observed when endogenous proteins were broken down in the presence of ATP and ubiquitin. Additionally, accumulation of high molecular weight conjugates was observed when cercariae were pre-incubated with proteasome inhibitors. Finally, we present evidence that during experimental schistosomiasis, proteasome inhibitors were able to reduce the number of lung stage schistosomula, reduce the worm burden and consequently decrease the egg output in infected mice.
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spelling Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.Schistosoma mansoniParasitesProteasomes are multi-subunit proteases involved in several mechanisms and thought to contribute to the regulation of cellular homeostasis. Here, we report for the Wrst time biochemical evidence for the existence of a ubiquitin–proteasome proteolytic pathway in this parasite. Proteasomes from both cercariae and adult worms exhibited a high preference for hydrolysis of the substrate Suc- LLVY-AMC, although in the cercariae extract the rate of hydrolysis was 50% lower when compared to adult worms extracts. The same diVerence in proteasome activities was observed when endogenous proteins were broken down in the presence of ATP and ubiquitin. Additionally, accumulation of high molecular weight conjugates was observed when cercariae were pre-incubated with proteasome inhibitors. Finally, we present evidence that during experimental schistosomiasis, proteasome inhibitors were able to reduce the number of lung stage schistosomula, reduce the worm burden and consequently decrease the egg output in infected mice.2015-01-20T15:43:25Z2015-01-20T15:43:25Z2005info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfSÁ, R. G. et al. Schistosoma mansoni: functional proteasomes are required for development in the vertebrate host. Experimental Parasitology, v. 109, n. 4, p. 228-236, 2005. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0014489405000093>. Acesso em: 08 nov. 2014.0014-4894http://www.repositorio.ufop.br/handle/123456789/4284https://doi.org/10.1016/j.exppara.2005.01.002O periódico Experimental Parasitology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3521411366469.info:eu-repo/semantics/openAccessCota, Renata Guerra de SáBorges, William de CastroEvangelista, Elísio AlbertoKettelhut, Isis do CarmoRodrigues, Vanderleiengreponame:Repositório Institucional da UFOPinstname:Universidade Federal de Ouro Preto (UFOP)instacron:UFOP2019-06-11T15:48:00Zoai:repositorio.ufop.br:123456789/4284Repositório InstitucionalPUBhttp://www.repositorio.ufop.br/oai/requestrepositorio@ufop.edu.bropendoar:32332019-06-11T15:48Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)false
dc.title.none.fl_str_mv Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
title Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
spellingShingle Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
Cota, Renata Guerra de Sá
Schistosoma mansoni
Parasites
title_short Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
title_full Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
title_fullStr Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
title_full_unstemmed Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
title_sort Schistosoma mansoni : functional proteasomes are required for development in the vertebrate host.
author Cota, Renata Guerra de Sá
author_facet Cota, Renata Guerra de Sá
Borges, William de Castro
Evangelista, Elísio Alberto
Kettelhut, Isis do Carmo
Rodrigues, Vanderlei
author_role author
author2 Borges, William de Castro
Evangelista, Elísio Alberto
Kettelhut, Isis do Carmo
Rodrigues, Vanderlei
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Cota, Renata Guerra de Sá
Borges, William de Castro
Evangelista, Elísio Alberto
Kettelhut, Isis do Carmo
Rodrigues, Vanderlei
dc.subject.por.fl_str_mv Schistosoma mansoni
Parasites
topic Schistosoma mansoni
Parasites
description Proteasomes are multi-subunit proteases involved in several mechanisms and thought to contribute to the regulation of cellular homeostasis. Here, we report for the Wrst time biochemical evidence for the existence of a ubiquitin–proteasome proteolytic pathway in this parasite. Proteasomes from both cercariae and adult worms exhibited a high preference for hydrolysis of the substrate Suc- LLVY-AMC, although in the cercariae extract the rate of hydrolysis was 50% lower when compared to adult worms extracts. The same diVerence in proteasome activities was observed when endogenous proteins were broken down in the presence of ATP and ubiquitin. Additionally, accumulation of high molecular weight conjugates was observed when cercariae were pre-incubated with proteasome inhibitors. Finally, we present evidence that during experimental schistosomiasis, proteasome inhibitors were able to reduce the number of lung stage schistosomula, reduce the worm burden and consequently decrease the egg output in infected mice.
publishDate 2005
dc.date.none.fl_str_mv 2005
2015-01-20T15:43:25Z
2015-01-20T15:43:25Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv SÁ, R. G. et al. Schistosoma mansoni: functional proteasomes are required for development in the vertebrate host. Experimental Parasitology, v. 109, n. 4, p. 228-236, 2005. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0014489405000093>. Acesso em: 08 nov. 2014.
0014-4894
http://www.repositorio.ufop.br/handle/123456789/4284
https://doi.org/10.1016/j.exppara.2005.01.002
identifier_str_mv SÁ, R. G. et al. Schistosoma mansoni: functional proteasomes are required for development in the vertebrate host. Experimental Parasitology, v. 109, n. 4, p. 228-236, 2005. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0014489405000093>. Acesso em: 08 nov. 2014.
0014-4894
url http://www.repositorio.ufop.br/handle/123456789/4284
https://doi.org/10.1016/j.exppara.2005.01.002
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFOP
instname:Universidade Federal de Ouro Preto (UFOP)
instacron:UFOP
instname_str Universidade Federal de Ouro Preto (UFOP)
instacron_str UFOP
institution UFOP
reponame_str Repositório Institucional da UFOP
collection Repositório Institucional da UFOP
repository.name.fl_str_mv Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)
repository.mail.fl_str_mv repositorio@ufop.edu.br
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