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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/42830
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/42830
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str 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 Técnicas2025-10-22T11:57:39Zoai: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:34982025-10-22 11:57:39.853CONICET 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
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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score 12.982451

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