Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding

Detalhes bibliográficos
Autor(a) principal: Entringer,Petter Franco
Data de Publicação: 2013
Outros Autores: Grillo,Luciano Aparecido Meireles, Pontes,Emerson Guedes, Machado,Ednildo Alcântara, Gondim,Katia Calp
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836
Resumo: Lipophorin (Lp) is the main haemolymphatic lipoprotein in insects and transports lipids between different organs. In adult females, lipophorin delivers lipids to growing oocytes. In this study, the interaction of this lipoprotein with the ovaries of Rhodnius prolixus was characterised using an oocyte membrane preparation and purified radiolabelled Lp (125I-Lp). Lp-specific binding to the oocyte membrane reached equilibrium after 40-60 min and when 125I-Lp was incubated with increasing amounts of membrane protein, corresponding increases in Lp binding were observed. The specific binding of Lp to the membrane preparation was a saturable process, with a Kdof 7.1 ± 0.9 x 10-8M and a maximal binding capacity of 430 ± 40 ng 125I-Lp/µg of membrane protein. The binding was calcium independent and pH sensitive, reaching its maximum at pH 5.2-5.7. Suramin inhibited the binding interaction between Lp and the oocyte membranes, which was completely abolished at 0.5 mM suramin. The oocyte membrane preparation from R. prolixus also showed binding to Lp from Manduca sexta. When Lp was fluorescently labelled and injected into vitellogenic females, the level of Lp-oocyte binding was much higher in females that were fed whole blood than in those fed blood plasma.
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spelling Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feedinghaematophagous insectlipophorin receptorovaryoocyteRhodnius prolixusLipophorin (Lp) is the main haemolymphatic lipoprotein in insects and transports lipids between different organs. In adult females, lipophorin delivers lipids to growing oocytes. In this study, the interaction of this lipoprotein with the ovaries of Rhodnius prolixus was characterised using an oocyte membrane preparation and purified radiolabelled Lp (125I-Lp). Lp-specific binding to the oocyte membrane reached equilibrium after 40-60 min and when 125I-Lp was incubated with increasing amounts of membrane protein, corresponding increases in Lp binding were observed. The specific binding of Lp to the membrane preparation was a saturable process, with a Kdof 7.1 ± 0.9 x 10-8M and a maximal binding capacity of 430 ± 40 ng 125I-Lp/µg of membrane protein. The binding was calcium independent and pH sensitive, reaching its maximum at pH 5.2-5.7. Suramin inhibited the binding interaction between Lp and the oocyte membranes, which was completely abolished at 0.5 mM suramin. The oocyte membrane preparation from R. prolixus also showed binding to Lp from Manduca sexta. When Lp was fluorescently labelled and injected into vitellogenic females, the level of Lp-oocyte binding was much higher in females that were fed whole blood than in those fed blood plasma.Instituto Oswaldo Cruz, Ministério da Saúde2013-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836Memórias do Instituto Oswaldo Cruz v.108 n.7 2013reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/0074-0276130129info:eu-repo/semantics/openAccessEntringer,Petter FrancoGrillo,Luciano Aparecido MeirelesPontes,Emerson GuedesMachado,Ednildo AlcântaraGondim,Katia Calpeng2020-04-25T17:51:36Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:19:13.028Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
title Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
spellingShingle Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
Entringer,Petter Franco
haematophagous insect
lipophorin receptor
ovary
oocyte
Rhodnius prolixus
title_short Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
title_full Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
title_fullStr Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
title_full_unstemmed Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
title_sort Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
author Entringer,Petter Franco
author_facet Entringer,Petter Franco
Grillo,Luciano Aparecido Meireles
Pontes,Emerson Guedes
Machado,Ednildo Alcântara
Gondim,Katia Calp
author_role author
author2 Grillo,Luciano Aparecido Meireles
Pontes,Emerson Guedes
Machado,Ednildo Alcântara
Gondim,Katia Calp
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Entringer,Petter Franco
Grillo,Luciano Aparecido Meireles
Pontes,Emerson Guedes
Machado,Ednildo Alcântara
Gondim,Katia Calp
dc.subject.por.fl_str_mv haematophagous insect
lipophorin receptor
ovary
oocyte
Rhodnius prolixus
topic haematophagous insect
lipophorin receptor
ovary
oocyte
Rhodnius prolixus
dc.description.none.fl_txt_mv Lipophorin (Lp) is the main haemolymphatic lipoprotein in insects and transports lipids between different organs. In adult females, lipophorin delivers lipids to growing oocytes. In this study, the interaction of this lipoprotein with the ovaries of Rhodnius prolixus was characterised using an oocyte membrane preparation and purified radiolabelled Lp (125I-Lp). Lp-specific binding to the oocyte membrane reached equilibrium after 40-60 min and when 125I-Lp was incubated with increasing amounts of membrane protein, corresponding increases in Lp binding were observed. The specific binding of Lp to the membrane preparation was a saturable process, with a Kdof 7.1 ± 0.9 x 10-8M and a maximal binding capacity of 430 ± 40 ng 125I-Lp/µg of membrane protein. The binding was calcium independent and pH sensitive, reaching its maximum at pH 5.2-5.7. Suramin inhibited the binding interaction between Lp and the oocyte membranes, which was completely abolished at 0.5 mM suramin. The oocyte membrane preparation from R. prolixus also showed binding to Lp from Manduca sexta. When Lp was fluorescently labelled and injected into vitellogenic females, the level of Lp-oocyte binding was much higher in females that were fed whole blood than in those fed blood plasma.
description Lipophorin (Lp) is the main haemolymphatic lipoprotein in insects and transports lipids between different organs. In adult females, lipophorin delivers lipids to growing oocytes. In this study, the interaction of this lipoprotein with the ovaries of Rhodnius prolixus was characterised using an oocyte membrane preparation and purified radiolabelled Lp (125I-Lp). Lp-specific binding to the oocyte membrane reached equilibrium after 40-60 min and when 125I-Lp was incubated with increasing amounts of membrane protein, corresponding increases in Lp binding were observed. The specific binding of Lp to the membrane preparation was a saturable process, with a Kdof 7.1 ± 0.9 x 10-8M and a maximal binding capacity of 430 ± 40 ng 125I-Lp/µg of membrane protein. The binding was calcium independent and pH sensitive, reaching its maximum at pH 5.2-5.7. Suramin inhibited the binding interaction between Lp and the oocyte membranes, which was completely abolished at 0.5 mM suramin. The oocyte membrane preparation from R. prolixus also showed binding to Lp from Manduca sexta. When Lp was fluorescently labelled and injected into vitellogenic females, the level of Lp-oocyte binding was much higher in females that were fed whole blood than in those fed blood plasma.
publishDate 2013
dc.date.none.fl_str_mv 2013-11-01
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://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0074-0276130129
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.108 n.7 2013
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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