Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding
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 oocyt...
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| Format: | Article |
| Language: | English |
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Fundação Oswaldo Cruz (FIOCRUZ)
2013-11-01
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| Series: | Memorias do Instituto Oswaldo Cruz |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836&lng=en&tlng=en |
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| author | Petter Franco Entringer Luciano Aparecido Meireles Grillo Emerson Guedes Pontes Ednildo Alcântara Machado Katia Calp Gondim |
| author_facet | Petter Franco Entringer Luciano Aparecido Meireles Grillo Emerson Guedes Pontes Ednildo Alcântara Machado Katia Calp Gondim |
| author_sort | Petter Franco Entringer |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-12T08:49:01Z |
| format | Article |
| id | doaj.art-9d7ae8e6294c424e9f21584bac6cdb16 |
| institution | Directory Open Access Journal |
| issn | 1678-8060 |
| language | English |
| last_indexed | 2024-03-12T08:49:01Z |
| publishDate | 2013-11-01 |
| publisher | Fundação Oswaldo Cruz (FIOCRUZ) |
| record_format | Article |
| series | Memorias do Instituto Oswaldo Cruz |
| spelling | doaj.art-9d7ae8e6294c424e9f21584bac6cdb162023-09-02T16:22:12ZengFundação Oswaldo Cruz (FIOCRUZ)Memorias do Instituto Oswaldo Cruz1678-80602013-11-01108783684410.1590/0074-0276130129S0074-02762013000700836Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feedingPetter Franco EntringerLuciano Aparecido Meireles GrilloEmerson Guedes PontesEdnildo Alcântara MachadoKatia Calp GondimLipophorin (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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836&lng=en&tlng=enhaematophagous insectlipophorin receptorovaryoocyteRhodnius prolixus |
| spellingShingle | Petter Franco Entringer Luciano Aparecido Meireles Grillo Emerson Guedes Pontes Ednildo Alcântara Machado Katia Calp Gondim Interaction of lipophorin with Rhodnius prolixus oocytes: biochemical properties and the importance of blood feeding Memorias do Instituto Oswaldo Cruz haematophagous insect lipophorin receptor ovary oocyte Rhodnius prolixus |
| title | 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_short | 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 |
| topic | haematophagous insect lipophorin receptor ovary oocyte Rhodnius prolixus |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762013000700836&lng=en&tlng=en |
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