Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>

Autores
García, Carlos Fernando; González Baró, María del Rosario; Garda, Horacio Alberto; Cunningham, Mónica Liliana; Pollero, Ricardo José
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Two lipovitellin (LV) forms containing the same apoproteins but differing in their lipid composition were isolated from Macrobrachium borelii eggs at early (LVe) and late (LVI) embryogenic stages and characterized. These two forms of LV, as well as liposomes prepared with lipids extracted from them, were used as simpler models to study the effect of the pesticide fenitrothion (FS) on their structures and functions. Rotational diffusion and fluorescence lifetime of two fluorescent probes [1,6-diphenyl-1,3,5-hexatriene (DPH) and 3-(p-(6-phenyl)-1,3,5-hexatrienal)phenylpropionic acid (DPH-PA)] were used to obtain information on structural changes induced by FS in the inner and outer regions of the LV, respectively. Comparison of the rotational behavior of these probes in native LV and liposomes (LP) from extracted LV lipids suggests that apoprotein-lipid interactions result in an ordered neutral lipid core. FS increased the lipid phase polarity of both LV and LP forms. The rotation of these probes in LP was not affected, suggesting a dependence of FS action on lipid-protein interactions. DPH-PA steady-state anisotropy showed that, unlike the LVe form, the LVI form was sensitive to extremely low FS concentrations. The ability of both LV to transfer palmitic acid to albumin was increased, but in a dissimilar manner, by the presence of FS. Such differences in the sensitivity of the LV at different steps of embryogenesis to FS influence the toxic action of this insecticide.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Ciencias Exactas
Bioquímica
Macrobrachium borellii
lipovitellin
fenitrothion
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/145027

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network_name_str SEDICI (UNLP)
spelling Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>García, Carlos FernandoGonzález Baró, María del RosarioGarda, Horacio AlbertoCunningham, Mónica LilianaPollero, Ricardo JoséCiencias ExactasBioquímicaMacrobrachium borelliilipovitellinfenitrothionTwo lipovitellin (LV) forms containing the same apoproteins but differing in their lipid composition were isolated from <i>Macrobrachium borelii</i> eggs at early (LVe) and late (LVI) embryogenic stages and characterized. These two forms of LV, as well as liposomes prepared with lipids extracted from them, were used as simpler models to study the effect of the pesticide fenitrothion (FS) on their structures and functions. Rotational diffusion and fluorescence lifetime of two fluorescent probes [1,6-diphenyl-1,3,5-hexatriene (DPH) and 3-(p-(6-phenyl)-1,3,5-hexatrienal)phenylpropionic acid (DPH-PA)] were used to obtain information on structural changes induced by FS in the inner and outer regions of the LV, respectively. Comparison of the rotational behavior of these probes in native LV and liposomes (LP) from extracted LV lipids suggests that apoprotein-lipid interactions result in an ordered neutral lipid core. FS increased the lipid phase polarity of both LV and LP forms. The rotation of these probes in LP was not affected, suggesting a dependence of FS action on lipid-protein interactions. DPH-PA steady-state anisotropy showed that, unlike the LVe form, the LVI form was sensitive to extremely low FS concentrations. The ability of both LV to transfer palmitic acid to albumin was increased, but in a dissimilar manner, by the presence of FS. Such differences in the sensitivity of the LV at different steps of embryogenesis to FS influence the toxic action of this insecticide.Instituto de Investigaciones Bioquímicas de La Plata2004-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf389-396http://sedici.unlp.edu.ar/handle/10915/145027enginfo:eu-repo/semantics/altIdentifier/issn/0024-4201info:eu-repo/semantics/altIdentifier/issn/1558-9307info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-004-1243-1info:eu-repo/semantics/altIdentifier/pmid/15357027info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:33Zoai:sedici.unlp.edu.ar:10915/145027Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:33.57SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
title Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
spellingShingle Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
García, Carlos Fernando
Ciencias Exactas
Bioquímica
Macrobrachium borellii
lipovitellin
fenitrothion
title_short Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
title_full Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
title_fullStr Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
title_full_unstemmed Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
title_sort Fenitrothion-Induced Structural and Functional Perturbations in the Yolk Lipoproteins of the Shrimp <i>Macrobrachium borellii</i>
dc.creator.none.fl_str_mv García, Carlos Fernando
González Baró, María del Rosario
Garda, Horacio Alberto
Cunningham, Mónica Liliana
Pollero, Ricardo José
author García, Carlos Fernando
author_facet García, Carlos Fernando
González Baró, María del Rosario
Garda, Horacio Alberto
Cunningham, Mónica Liliana
Pollero, Ricardo José
author_role author
author2 González Baró, María del Rosario
Garda, Horacio Alberto
Cunningham, Mónica Liliana
Pollero, Ricardo José
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Bioquímica
Macrobrachium borellii
lipovitellin
fenitrothion
topic Ciencias Exactas
Bioquímica
Macrobrachium borellii
lipovitellin
fenitrothion
dc.description.none.fl_txt_mv Two lipovitellin (LV) forms containing the same apoproteins but differing in their lipid composition were isolated from <i>Macrobrachium borelii</i> eggs at early (LVe) and late (LVI) embryogenic stages and characterized. These two forms of LV, as well as liposomes prepared with lipids extracted from them, were used as simpler models to study the effect of the pesticide fenitrothion (FS) on their structures and functions. Rotational diffusion and fluorescence lifetime of two fluorescent probes [1,6-diphenyl-1,3,5-hexatriene (DPH) and 3-(p-(6-phenyl)-1,3,5-hexatrienal)phenylpropionic acid (DPH-PA)] were used to obtain information on structural changes induced by FS in the inner and outer regions of the LV, respectively. Comparison of the rotational behavior of these probes in native LV and liposomes (LP) from extracted LV lipids suggests that apoprotein-lipid interactions result in an ordered neutral lipid core. FS increased the lipid phase polarity of both LV and LP forms. The rotation of these probes in LP was not affected, suggesting a dependence of FS action on lipid-protein interactions. DPH-PA steady-state anisotropy showed that, unlike the LVe form, the LVI form was sensitive to extremely low FS concentrations. The ability of both LV to transfer palmitic acid to albumin was increased, but in a dissimilar manner, by the presence of FS. Such differences in the sensitivity of the LV at different steps of embryogenesis to FS influence the toxic action of this insecticide.
Instituto de Investigaciones Bioquímicas de La Plata
description Two lipovitellin (LV) forms containing the same apoproteins but differing in their lipid composition were isolated from <i>Macrobrachium borelii</i> eggs at early (LVe) and late (LVI) embryogenic stages and characterized. These two forms of LV, as well as liposomes prepared with lipids extracted from them, were used as simpler models to study the effect of the pesticide fenitrothion (FS) on their structures and functions. Rotational diffusion and fluorescence lifetime of two fluorescent probes [1,6-diphenyl-1,3,5-hexatriene (DPH) and 3-(p-(6-phenyl)-1,3,5-hexatrienal)phenylpropionic acid (DPH-PA)] were used to obtain information on structural changes induced by FS in the inner and outer regions of the LV, respectively. Comparison of the rotational behavior of these probes in native LV and liposomes (LP) from extracted LV lipids suggests that apoprotein-lipid interactions result in an ordered neutral lipid core. FS increased the lipid phase polarity of both LV and LP forms. The rotation of these probes in LP was not affected, suggesting a dependence of FS action on lipid-protein interactions. DPH-PA steady-state anisotropy showed that, unlike the LVe form, the LVI form was sensitive to extremely low FS concentrations. The ability of both LV to transfer palmitic acid to albumin was increased, but in a dissimilar manner, by the presence of FS. Such differences in the sensitivity of the LV at different steps of embryogenesis to FS influence the toxic action of this insecticide.
publishDate 2004
dc.date.none.fl_str_mv 2004-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/145027
url http://sedici.unlp.edu.ar/handle/10915/145027
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0024-4201
info:eu-repo/semantics/altIdentifier/issn/1558-9307
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-004-1243-1
info:eu-repo/semantics/altIdentifier/pmid/15357027
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
389-396
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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