StarD7 behaves as a fusogenic protein in model and cell membrane bilayers
- Autores
- Angeletti, Sofia Claudia; Sanchez, Julieta Maria; Chamley, Larry W.; Genti de Raimondi, Susana; Perillo, Maria Angelica
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- StarD7 is a surface active protein, structurally related with the START lipid transport family. So, the present work was aimed at elucidating a potential mechanism of action for StarD7 that could be related to its interaction with a lipid–membrane interface. We applied an assay based on the fluorescence de-quenching of BD-HPC-labeled DMPC–DMPS 4:1 mol/mol SUVs (donor liposomes) induced by the dilution with non-labeled DMPC–DMPS 4:1 mol/mol LUVs (acceptor liposomes). Recombinant StarD7 accelerated the dilution of BD-HPC in a concentration-dependent manner. This result could have been explained by either a bilayer fusion or monomeric transport of the labeled lipid between donor and acceptor liposomes. Further experiments (fluorescence energy transfer between DPH-HPC/BD-HPC, liposome size distribution analysis by dynamic light scattering, and the multinuclear giant cell formation induced by recombinant StarD7) strongly indicated that bilayer fusion was the mechanism responsible for the StarD7-induced lipid dilution. The efficiency of lipid dilution was dependent on StarD7 electrostatic interactions with the lipid–water interface, as shown by the pH- and salt-induced modulation. Moreover, this process was favored by phosphatidylethanolamine which is known to stabilize non-lamellar phases considered as intermediary in the fusion process. Altogether these findings allow postulate StarD7 as a fusogenic protein.
Fil: Angeletti, Sofia Claudia. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; Argentina
Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Chamley, Larry W.. The University of Auckland; Nueva Zelanda
Fil: Genti de Raimondi, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina - Materia
-
Stard7
Bilayer Fusion
Steady State Fluorescence De-Quenching
Dynamic Light Scattering
Fret
Trophoblast Syncytialisation - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/42830
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CONICET Digital (CONICET) |
spelling |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayersAngeletti, Sofia ClaudiaSanchez, Julieta MariaChamley, Larry W.Genti de Raimondi, SusanaPerillo, Maria AngelicaStard7Bilayer FusionSteady State Fluorescence De-QuenchingDynamic Light ScatteringFretTrophoblast Syncytialisationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1StarD7 is a surface active protein, structurally related with the START lipid transport family. So, the present work was aimed at elucidating a potential mechanism of action for StarD7 that could be related to its interaction with a lipid–membrane interface. We applied an assay based on the fluorescence de-quenching of BD-HPC-labeled DMPC–DMPS 4:1 mol/mol SUVs (donor liposomes) induced by the dilution with non-labeled DMPC–DMPS 4:1 mol/mol LUVs (acceptor liposomes). Recombinant StarD7 accelerated the dilution of BD-HPC in a concentration-dependent manner. This result could have been explained by either a bilayer fusion or monomeric transport of the labeled lipid between donor and acceptor liposomes. Further experiments (fluorescence energy transfer between DPH-HPC/BD-HPC, liposome size distribution analysis by dynamic light scattering, and the multinuclear giant cell formation induced by recombinant StarD7) strongly indicated that bilayer fusion was the mechanism responsible for the StarD7-induced lipid dilution. The efficiency of lipid dilution was dependent on StarD7 electrostatic interactions with the lipid–water interface, as shown by the pH- and salt-induced modulation. Moreover, this process was favored by phosphatidylethanolamine which is known to stabilize non-lamellar phases considered as intermediary in the fusion process. Altogether these findings allow postulate StarD7 as a fusogenic protein.Fil: Angeletti, Sofia Claudia. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; ArgentinaFil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Chamley, Larry W.. The University of Auckland; Nueva ZelandaFil: Genti de Raimondi, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaElsevier Science2012-03-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/42830Angeletti, Sofia Claudia; Sanchez, Julieta Maria; Chamley, Larry W.; Genti de Raimondi, Susana; Perillo, Maria Angelica; StarD7 behaves as a fusogenic protein in model and cell membrane bilayers; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 3; 3-3-2012; 425-4330005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273611003749?via%3Dihubinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2011.10.024info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:24:56Zoai:ri.conicet.gov.ar:11336/42830instacron: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:34982025-09-29 10:24:57.152CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
title |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
spellingShingle |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers Angeletti, Sofia Claudia Stard7 Bilayer Fusion Steady State Fluorescence De-Quenching Dynamic Light Scattering Fret Trophoblast Syncytialisation |
title_short |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
title_full |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
title_fullStr |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
title_full_unstemmed |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
title_sort |
StarD7 behaves as a fusogenic protein in model and cell membrane bilayers |
dc.creator.none.fl_str_mv |
Angeletti, Sofia Claudia Sanchez, Julieta Maria Chamley, Larry W. Genti de Raimondi, Susana Perillo, Maria Angelica |
author |
Angeletti, Sofia Claudia |
author_facet |
Angeletti, Sofia Claudia Sanchez, Julieta Maria Chamley, Larry W. Genti de Raimondi, Susana Perillo, Maria Angelica |
author_role |
author |
author2 |
Sanchez, Julieta Maria Chamley, Larry W. Genti de Raimondi, Susana Perillo, Maria Angelica |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Stard7 Bilayer Fusion Steady State Fluorescence De-Quenching Dynamic Light Scattering Fret Trophoblast Syncytialisation |
topic |
Stard7 Bilayer Fusion Steady State Fluorescence De-Quenching Dynamic Light Scattering Fret Trophoblast Syncytialisation |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
StarD7 is a surface active protein, structurally related with the START lipid transport family. So, the present work was aimed at elucidating a potential mechanism of action for StarD7 that could be related to its interaction with a lipid–membrane interface. We applied an assay based on the fluorescence de-quenching of BD-HPC-labeled DMPC–DMPS 4:1 mol/mol SUVs (donor liposomes) induced by the dilution with non-labeled DMPC–DMPS 4:1 mol/mol LUVs (acceptor liposomes). Recombinant StarD7 accelerated the dilution of BD-HPC in a concentration-dependent manner. This result could have been explained by either a bilayer fusion or monomeric transport of the labeled lipid between donor and acceptor liposomes. Further experiments (fluorescence energy transfer between DPH-HPC/BD-HPC, liposome size distribution analysis by dynamic light scattering, and the multinuclear giant cell formation induced by recombinant StarD7) strongly indicated that bilayer fusion was the mechanism responsible for the StarD7-induced lipid dilution. The efficiency of lipid dilution was dependent on StarD7 electrostatic interactions with the lipid–water interface, as shown by the pH- and salt-induced modulation. Moreover, this process was favored by phosphatidylethanolamine which is known to stabilize non-lamellar phases considered as intermediary in the fusion process. Altogether these findings allow postulate StarD7 as a fusogenic protein. Fil: Angeletti, Sofia Claudia. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; Argentina Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina Fil: Chamley, Larry W.. The University of Auckland; Nueva Zelanda Fil: Genti de Raimondi, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina |
description |
StarD7 is a surface active protein, structurally related with the START lipid transport family. So, the present work was aimed at elucidating a potential mechanism of action for StarD7 that could be related to its interaction with a lipid–membrane interface. We applied an assay based on the fluorescence de-quenching of BD-HPC-labeled DMPC–DMPS 4:1 mol/mol SUVs (donor liposomes) induced by the dilution with non-labeled DMPC–DMPS 4:1 mol/mol LUVs (acceptor liposomes). Recombinant StarD7 accelerated the dilution of BD-HPC in a concentration-dependent manner. This result could have been explained by either a bilayer fusion or monomeric transport of the labeled lipid between donor and acceptor liposomes. Further experiments (fluorescence energy transfer between DPH-HPC/BD-HPC, liposome size distribution analysis by dynamic light scattering, and the multinuclear giant cell formation induced by recombinant StarD7) strongly indicated that bilayer fusion was the mechanism responsible for the StarD7-induced lipid dilution. The efficiency of lipid dilution was dependent on StarD7 electrostatic interactions with the lipid–water interface, as shown by the pH- and salt-induced modulation. Moreover, this process was favored by phosphatidylethanolamine which is known to stabilize non-lamellar phases considered as intermediary in the fusion process. Altogether these findings allow postulate StarD7 as a fusogenic protein. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-03-03 |
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/11336/42830 Angeletti, Sofia Claudia; Sanchez, Julieta Maria; Chamley, Larry W.; Genti de Raimondi, Susana; Perillo, Maria Angelica; StarD7 behaves as a fusogenic protein in model and cell membrane bilayers; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 3; 3-3-2012; 425-433 0005-2736 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/42830 |
identifier_str_mv |
Angeletti, Sofia Claudia; Sanchez, Julieta Maria; Chamley, Larry W.; Genti de Raimondi, Susana; Perillo, Maria Angelica; StarD7 behaves as a fusogenic protein in model and cell membrane bilayers; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 3; 3-3-2012; 425-433 0005-2736 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://www.sciencedirect.com/science/article/pii/S0005273611003749?via%3Dihub info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2011.10.024 |
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 |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |