RESUMO
Endocrine-disrupting chemicals (EDCs) are widespread used and can interfere on hormone regulation with adverse consequences for both biota and human. Vitellogenin (vtg) is a yolk precursor protein synthesized by the liver in response to estrogen. In order to characterize the vtg of tropical fish Rhamdia quelen and establish a molecular biomarker, adult male individuals were exposed to 17-ß-estradiol (E2) for vtg induction and anti-R. quelen vtg polyclonal antibodies production. Vitellogenic female fish were used as positive control group. E2-induced vtg was characterized as a glycolipophosphoprotein of high molecular mass with peptide mass fingerprint very similar in E2-exposed male and vitellogenic female fish. A polyclonal serum containing anti-R. quelen vtg antibodies was produced and showed high specificity and sensibility to detect the vtg of three fish species: R. quelen, Piaractus mesopotamicus and Prochilodus lineatus. Wildlife and laboratory studies reported that EDCs released into the environment may alter the levels of plasma vtg in male fish, making this protein a valuable biomarker of xenoestrogens exposure. Then, we propose the use of anti-R. quelen vtg as a tool for biomonitoring studies and water quality assessment in Brazil and South American countries where the three fish species occur.
Assuntos
Peixes-Gato/sangue , Caraciformes/sangue , Proteínas de Peixes/sangue , Vitelogeninas/sangue , Animais , Anticorpos/imunologia , Anticorpos/metabolismo , Brasil , Peixes-Gato/metabolismo , Caraciformes/metabolismo , Estradiol/farmacologia , Estrogênios/farmacologia , Feminino , Proteínas de Peixes/imunologia , Proteínas de Peixes/metabolismo , Fígado/metabolismo , Masculino , Oócitos/metabolismo , Testículo/metabolismo , Vitelogeninas/imunologia , Vitelogeninas/metabolismoRESUMO
Proteins stored in insect hemolymph may serve as a source of amino acids and energy for metabolism and development. The expression of the main storage proteins was assessed in bacterial-challenged honey bees using real-time (RT)-PCR and Western blot. After ensuring that the immune system had been activated by measuring the ensuing expression of the innate immune response genes, defensin-1 (def-1) and prophenoloxidase (proPO), we verified the expression of four genes encoding storage proteins. The levels of vitellogenin (vg) mRNA and of the respective protein were significantly lowered in bees injected with bacteria or water only (injury). An equivalent response was observed in orally-infected bees. The levels of apolipophorin II/I (apoLp-II/I) and hexamerin (hex 70a) mRNAs did not significantly change, but levels of Hex 70a protein subunit showed a substantial decay after bacterial challenge or injury. Infection also caused a strong reduction in the levels of apoLp-III transcripts. Our findings are consistent with a down-regulation of the expression and accumulation of storage proteins as a consequence of activation of the immune system, suggesting that this phenomenon represents a strategy to redirect resources to combat injury or infection.
Assuntos
Infecções Bacterianas/imunologia , Abelhas/genética , Hemolinfa/imunologia , Proteínas de Insetos/genética , Animais , Apolipoproteínas/genética , Apolipoproteínas/imunologia , Apolipoproteínas/metabolismo , Infecções Bacterianas/metabolismo , Abelhas/imunologia , Abelhas/metabolismo , Catecol Oxidase/genética , Catecol Oxidase/imunologia , Catecol Oxidase/metabolismo , Defensinas/imunologia , Defensinas/metabolismo , Precursores Enzimáticos/genética , Precursores Enzimáticos/imunologia , Precursores Enzimáticos/metabolismo , Feminino , Regulação da Expressão Gênica , Hemolinfa/metabolismo , Proteínas de Insetos/imunologia , Proteínas de Insetos/metabolismo , RNA/análise , RNA Mensageiro/análise , Especificidade da Espécie , Estresse Fisiológico/genética , Estresse Fisiológico/imunologia , Vitelogeninas/genética , Vitelogeninas/imunologia , Vitelogeninas/metabolismoRESUMO
The eggs from oviparous organisms contain large amounts of vitellus, or yolk, which are utilized by the growing embryo. Vitellogenesis is the process of vitellus accumulation and involves massive heterosynthetic synthesis of the protein vitellogenin (Vg) and its deposition in the oocyte. This work summarizes data on Vg structure, synthesis, uptake by oocytes and its fate during embryogenesis. The hormonal control of vitellogenesis and its tissue, sex and temporal regulation are also discussed. Where it is available, data on structure and expression of Vg-coding genes are reviewed. Insect vitellogenesis is priorized although other oviparous animal groups outside insects are also treated.
Assuntos
Oogênese/fisiologia , Vitelogênese , Vitelogeninas/química , Animais , Vitelogeninas/genética , Vitelogeninas/imunologiaRESUMO
Se realizaron estudios comparativos de los pesos moleculares composicion quimica e identidad inmunológica de la vitelina (VN) de distintas especies de triatominos. Se determinó que la VN es una lipoglicofosfoproteina con 12.76% de hidratos de carbono 12.53% de lipidos y 0.6% de fósforo unido a mas aproteica. La VN nativa muestra por filtración en gel una única banda de 310 KDa. La VN delipidizada muestra por PAGE SDS una banda principal de 175 KDa coincidente con la banda hallada en la vitellogenina (VG). La composición de aminoácidos fue similar en las cuatro especies ensayadas
Assuntos
Animais , Masculino , Feminino , Triatominae/química , Vitelogeninas/química , Aminoácidos/análise , Eletroforese em Gel de Poliacrilamida , Peso Molecular , Vitelogênese , Vitelogeninas/imunologia , Vitelogeninas/isolamento & purificaçãoRESUMO
Se realizaron estudios comparativos de los pesos moleculares composicion quimica e identidad inmunológica de la vitelina (VN) de distintas especies de triatominos. Se determinó que la VN es una lipoglicofosfoproteina con 12.76% de hidratos de carbono 12.53% de lipidos y 0.6% de fósforo unido a mas aproteica. La VN nativa muestra por filtración en gel una única banda de 310 KDa. La VN delipidizada muestra por PAGE SDS una banda principal de 175 KDa coincidente con la banda hallada en la vitellogenina (VG). La composición de aminoácidos fue similar en las cuatro especies ensayadas (AU)
Assuntos
Estudo Comparativo , Animais , Masculino , Feminino , Vitelogeninas/química , Triatominae/química , Vitelogeninas/imunologia , Vitelogeninas/isolamento & purificação , Vitelogênese , Peso Molecular , Aminoácidos/análise , Eletroforese em Gel de PoliacrilamidaRESUMO
A comparative study was conducted on the molecular weight, chemical composition, and immunological identity of vitellin (VN) from Triatominae species. VN is a lipoglycophosprotein: 12.76% carbohydrates, 12.53% lipids, and 0.6% phosphorus of the protein mass. Native VN shows one band of 310 kDa by gel filtration. VN shows a main band of 175 kDa by SDS-PAGE coincident with a vitellogenin (VG) band. Amino acid composition was very similar in the four species tested: T.infestans, T.pallidipennis, R.prolixus and D.maximus. T.infestans VN-VG has a total immunological identity with D.maximus female haemolymph and egg homogenates.