The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-m...

Autores
Fruttero, Leonardo Luis; Leyria, Jimena; Moyetta, Natalia Rita; Ramos, Fabián O.; Settembrini, Beatriz Patricia; Canavoso, Lilian Etelvina
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In insects, lipid transfer to the tissues is mediated by lipophorin, the major circulating lipoprotein, mainly through a nonendocytic pathway involving docking receptors. Currently, the role of such receptors in lipid metabolism remains poorly understood. In this work, we performed a histological characterization of the fat body of the Chagas’ disease vector, Panstrongylus megistus (Burmeister), subjected to different nutritional conditions. In addition, we addressed the role of the β-chain of ATP synthase (β-ATPase) in the process of lipid transfer from lipophorin to the fat body. Fifth-instar nymphs in either fasting or fed condition were employed in the assays. Histological examination revealed that the fat body was composed by diverse trophocyte phenotypes. In the fasting condition, the cells were smaller and presented a homogeneous cytoplasmic content.The fat body of fed insects increased in size mainly due to the enlargement of lipid stores. In this condition, trophocytes contained abundant lipid droplets, and the rough endoplasmic reticulum was highly developed and mitochondria appeared elongated. Immunofluorescence assays showed that the β-ATPase, a putative lipophorin receptor, was located on the surface of fat body cells colocalizing partially with lipophorin, which suggests their interaction. No changes in β-ATPase expression were found in fasting and fed insects. Blocking the lipophorin–β-ATPase interaction impaired the lipophorin-mediated lipid transfer to the fat body. The results showed that the nutritional status of the insect influenced the morphohistological features of the tissue. Besides, these findings suggest that β-ATPase functions as a lipophorin docking receptor in the fat body.
Fil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Leyria, Jimena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Moyetta, Natalia Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Ramos, Fabián O.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Settembrini, Beatriz Patricia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Museo Argentino de Ciencias Naturales "Bernardino Rivadavia"; Argentina
Fil: Canavoso, Lilian Etelvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Materia
DOCKING RECEPTOR
FAT BODY
LIPID METABOLISM
LIPOPHORIN
TRIATOMINAE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/128905
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transferFruttero, Leonardo LuisLeyria, JimenaMoyetta, Natalia RitaRamos, Fabián O.Settembrini, Beatriz PatriciaCanavoso, Lilian EtelvinaDOCKING RECEPTORFAT BODYLIPID METABOLISMLIPOPHORINTRIATOMINAEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In insects, lipid transfer to the tissues is mediated by lipophorin, the major circulating lipoprotein, mainly through a nonendocytic pathway involving docking receptors. Currently, the role of such receptors in lipid metabolism remains poorly understood. In this work, we performed a histological characterization of the fat body of the Chagas’ disease vector, Panstrongylus megistus (Burmeister), subjected to different nutritional conditions. In addition, we addressed the role of the β-chain of ATP synthase (β-ATPase) in the process of lipid transfer from lipophorin to the fat body. Fifth-instar nymphs in either fasting or fed condition were employed in the assays. Histological examination revealed that the fat body was composed by diverse trophocyte phenotypes. In the fasting condition, the cells were smaller and presented a homogeneous cytoplasmic content.The fat body of fed insects increased in size mainly due to the enlargement of lipid stores. In this condition, trophocytes contained abundant lipid droplets, and the rough endoplasmic reticulum was highly developed and mitochondria appeared elongated. Immunofluorescence assays showed that the β-ATPase, a putative lipophorin receptor, was located on the surface of fat body cells colocalizing partially with lipophorin, which suggests their interaction. No changes in β-ATPase expression were found in fasting and fed insects. Blocking the lipophorin–β-ATPase interaction impaired the lipophorin-mediated lipid transfer to the fat body. The results showed that the nutritional status of the insect influenced the morphohistological features of the tissue. Besides, these findings suggest that β-ATPase functions as a lipophorin docking receptor in the fat body.Fil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Leyria, Jimena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Moyetta, Natalia Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Ramos, Fabián O.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Settembrini, Beatriz Patricia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Museo Argentino de Ciencias Naturales "Bernardino Rivadavia"; ArgentinaFil: Canavoso, Lilian Etelvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaUniversity of Arizona2019-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/128905Fruttero, Leonardo Luis; Leyria, Jimena; Moyetta, Natalia Rita; Ramos, Fabián O.; Settembrini, Beatriz Patricia; et al.; The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer; University of Arizona; Journal of Insect Science; 19; 16; 7-2019; 1-81536-2442CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jinsectscience/article/19/4/16/5539020info:eu-repo/semantics/altIdentifier/doi/10.1093/jisesa/iez078info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:15:00Zoai:ri.conicet.gov.ar:11336/128905instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:15:00.645CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
title The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
spellingShingle The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
Fruttero, Leonardo Luis
DOCKING RECEPTOR
FAT BODY
LIPID METABOLISM
LIPOPHORIN
TRIATOMINAE
title_short The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
title_full The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
title_fullStr The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
title_full_unstemmed The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
title_sort The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer
dc.creator.none.fl_str_mv Fruttero, Leonardo Luis
Leyria, Jimena
Moyetta, Natalia Rita
Ramos, Fabián O.
Settembrini, Beatriz Patricia
Canavoso, Lilian Etelvina
author Fruttero, Leonardo Luis
author_facet Fruttero, Leonardo Luis
Leyria, Jimena
Moyetta, Natalia Rita
Ramos, Fabián O.
Settembrini, Beatriz Patricia
Canavoso, Lilian Etelvina
author_role author
author2 Leyria, Jimena
Moyetta, Natalia Rita
Ramos, Fabián O.
Settembrini, Beatriz Patricia
Canavoso, Lilian Etelvina
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv DOCKING RECEPTOR
FAT BODY
LIPID METABOLISM
LIPOPHORIN
TRIATOMINAE
topic DOCKING RECEPTOR
FAT BODY
LIPID METABOLISM
LIPOPHORIN
TRIATOMINAE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In insects, lipid transfer to the tissues is mediated by lipophorin, the major circulating lipoprotein, mainly through a nonendocytic pathway involving docking receptors. Currently, the role of such receptors in lipid metabolism remains poorly understood. In this work, we performed a histological characterization of the fat body of the Chagas’ disease vector, Panstrongylus megistus (Burmeister), subjected to different nutritional conditions. In addition, we addressed the role of the β-chain of ATP synthase (β-ATPase) in the process of lipid transfer from lipophorin to the fat body. Fifth-instar nymphs in either fasting or fed condition were employed in the assays. Histological examination revealed that the fat body was composed by diverse trophocyte phenotypes. In the fasting condition, the cells were smaller and presented a homogeneous cytoplasmic content.The fat body of fed insects increased in size mainly due to the enlargement of lipid stores. In this condition, trophocytes contained abundant lipid droplets, and the rough endoplasmic reticulum was highly developed and mitochondria appeared elongated. Immunofluorescence assays showed that the β-ATPase, a putative lipophorin receptor, was located on the surface of fat body cells colocalizing partially with lipophorin, which suggests their interaction. No changes in β-ATPase expression were found in fasting and fed insects. Blocking the lipophorin–β-ATPase interaction impaired the lipophorin-mediated lipid transfer to the fat body. The results showed that the nutritional status of the insect influenced the morphohistological features of the tissue. Besides, these findings suggest that β-ATPase functions as a lipophorin docking receptor in the fat body.
Fil: Fruttero, Leonardo Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Leyria, Jimena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Moyetta, Natalia Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Ramos, Fabián O.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Settembrini, Beatriz Patricia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Museo Argentino de Ciencias Naturales "Bernardino Rivadavia"; Argentina
Fil: Canavoso, Lilian Etelvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
description In insects, lipid transfer to the tissues is mediated by lipophorin, the major circulating lipoprotein, mainly through a nonendocytic pathway involving docking receptors. Currently, the role of such receptors in lipid metabolism remains poorly understood. In this work, we performed a histological characterization of the fat body of the Chagas’ disease vector, Panstrongylus megistus (Burmeister), subjected to different nutritional conditions. In addition, we addressed the role of the β-chain of ATP synthase (β-ATPase) in the process of lipid transfer from lipophorin to the fat body. Fifth-instar nymphs in either fasting or fed condition were employed in the assays. Histological examination revealed that the fat body was composed by diverse trophocyte phenotypes. In the fasting condition, the cells were smaller and presented a homogeneous cytoplasmic content.The fat body of fed insects increased in size mainly due to the enlargement of lipid stores. In this condition, trophocytes contained abundant lipid droplets, and the rough endoplasmic reticulum was highly developed and mitochondria appeared elongated. Immunofluorescence assays showed that the β-ATPase, a putative lipophorin receptor, was located on the surface of fat body cells colocalizing partially with lipophorin, which suggests their interaction. No changes in β-ATPase expression were found in fasting and fed insects. Blocking the lipophorin–β-ATPase interaction impaired the lipophorin-mediated lipid transfer to the fat body. The results showed that the nutritional status of the insect influenced the morphohistological features of the tissue. Besides, these findings suggest that β-ATPase functions as a lipophorin docking receptor in the fat body.
publishDate 2019
dc.date.none.fl_str_mv 2019-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/128905
Fruttero, Leonardo Luis; Leyria, Jimena; Moyetta, Natalia Rita; Ramos, Fabián O.; Settembrini, Beatriz Patricia; et al.; The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer; University of Arizona; Journal of Insect Science; 19; 16; 7-2019; 1-8
1536-2442
CONICET Digital
CONICET
url http://hdl.handle.net/11336/128905
identifier_str_mv Fruttero, Leonardo Luis; Leyria, Jimena; Moyetta, Natalia Rita; Ramos, Fabián O.; Settembrini, Beatriz Patricia; et al.; The fat body of the hematophagous insect, panstrongylus megistus (Hemiptera: Reduviidae): Histological features and participation of the β-chain of ATP synthase in the lipophorin-mediated lipid transfer; University of Arizona; Journal of Insect Science; 19; 16; 7-2019; 1-8
1536-2442
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jinsectscience/article/19/4/16/5539020
info:eu-repo/semantics/altIdentifier/doi/10.1093/jisesa/iez078
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv University of Arizona
publisher.none.fl_str_mv University of Arizona
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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