IFABP portal region insertion during membrane interaction depends on phospholipid composition

Autores
de Gerónimo, Eduardo; Rodriguez Sawicki, Luciana; Botasso Arias, Natalia; Franchini, Gisela Raquel; Zamarreño, Fernando; Costabel, Marcelo Daniel; Corsico, Betina; Falomir Lockhart, Lisandro Jorge
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Intestinal fatty acid-binding protein (IFABP) is highly expressed in the intestinal epithelium and it belongs to the family of soluble lipid binding proteins. These proteins are thought to participate in most aspects of the biology of lipids, regulating its availability for specific metabolic pathways, targeting and vectorial trafficking of lipids to specific subcellular compartments. The present study is based on the ability of IFABP to interact with phospholipid membranes, and we characterized its immersion into the bilayer´s hydrophobic central region occupied by the acyl-chains. We constructed a series of Trp-mutants of IFABP to selectively probe the interaction of different regions of the protein, particularly the elements forming the portal domain that is proposed to regulate the exit and entry of ligands to/from the binding cavity. We employed several fluorescent techniques based on selective quenching induced by soluble or membrane confined agents. The results indicate that the portal region of IFABP penetrates deeply into the phospholipid bilayer, especially when CL-containing vesicles are employed. The orientation of the protein and the degree of penetration were highly dependent on the lipid composition, the superficial net charge and the ionic strength of the medium. These results may be relevant to understand the mechanism of ligand transfer and the specificity responsible for the unique functions of each member of the FABP family.
Fil: de Gerónimo, Eduardo. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires. Estación Experimental Agropecuaria Balcarce. Area de Investigación en Agronomía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Rodriguez Sawicki, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Botasso Arias, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Zamarreño, Fernando. Universidad Nacional del Sur. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Costabel, Marcelo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Bahía Blanca. Instituto de Física del Sur; Argentina. Universidad Nacional del Sur. Departamento de Física; Argentina
Fil: Corsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Falomir Lockhart, Lisandro Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Materia
Fatty Acid Binding Protein
Proteinlipid Interaction
Intracellular Lipid Traffic
Intestinal Lipid Traffic
Brominated Phospholipid
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:11336/2042
Acceder
id CONICETDig_6328849f3190f2b54b825fca8d0dc1c9
oai_identifier_str oai:ri.conicet.gov.ar:11336/2042
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling IFABP portal region insertion during membrane interaction depends on phospholipid compositionde Gerónimo, EduardoRodriguez Sawicki, LucianaBotasso Arias, NataliaFranchini, Gisela RaquelZamarreño, FernandoCostabel, Marcelo DanielCorsico, BetinaFalomir Lockhart, Lisandro JorgeFatty Acid Binding ProteinProteinlipid InteractionIntracellular Lipid TrafficIntestinal Lipid TrafficBrominated Phospholipidhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Intestinal fatty acid-binding protein (IFABP) is highly expressed in the intestinal epithelium and it belongs to the family of soluble lipid binding proteins. These proteins are thought to participate in most aspects of the biology of lipids, regulating its availability for specific metabolic pathways, targeting and vectorial trafficking of lipids to specific subcellular compartments. The present study is based on the ability of IFABP to interact with phospholipid membranes, and we characterized its immersion into the bilayer´s hydrophobic central region occupied by the acyl-chains. We constructed a series of Trp-mutants of IFABP to selectively probe the interaction of different regions of the protein, particularly the elements forming the portal domain that is proposed to regulate the exit and entry of ligands to/from the binding cavity. We employed several fluorescent techniques based on selective quenching induced by soluble or membrane confined agents. The results indicate that the portal region of IFABP penetrates deeply into the phospholipid bilayer, especially when CL-containing vesicles are employed. The orientation of the protein and the degree of penetration were highly dependent on the lipid composition, the superficial net charge and the ionic strength of the medium. These results may be relevant to understand the mechanism of ligand transfer and the specificity responsible for the unique functions of each member of the FABP family.Fil: de Gerónimo, Eduardo. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires. Estación Experimental Agropecuaria Balcarce. Area de Investigación en Agronomía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaFil: Rodriguez Sawicki, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaFil: Botasso Arias, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaFil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaFil: Zamarreño, Fernando. Universidad Nacional del Sur. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Costabel, Marcelo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Bahía Blanca. Instituto de Física del Sur; Argentina. Universidad Nacional del Sur. Departamento de Física; ArgentinaFil: Corsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaFil: Falomir Lockhart, Lisandro Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; ArgentinaElsevier2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/2042de Gerónimo, Eduardo; Rodriguez Sawicki, Luciana; Botasso Arias, Natalia; Franchini, Gisela Raquel; Zamarreño, Fernando; et al.; IFABP portal region insertion during membrane interaction depends on phospholipid composition; Elsevier; Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids; 1841; 1; 1-2014; 141-1501388-1981enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbalip.2013.10.011info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1388198113002345info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:54:58Zoai:ri.conicet.gov.ar:11336/2042instacron: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:34982025-11-12 09:54:58.365CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv IFABP portal region insertion during membrane interaction depends on phospholipid composition
title IFABP portal region insertion during membrane interaction depends on phospholipid composition
spellingShingle IFABP portal region insertion during membrane interaction depends on phospholipid composition
de Gerónimo, Eduardo
Fatty Acid Binding Protein
Proteinlipid Interaction
Intracellular Lipid Traffic
Intestinal Lipid Traffic
Brominated Phospholipid
title_short IFABP portal region insertion during membrane interaction depends on phospholipid composition
title_full IFABP portal region insertion during membrane interaction depends on phospholipid composition
title_fullStr IFABP portal region insertion during membrane interaction depends on phospholipid composition
title_full_unstemmed IFABP portal region insertion during membrane interaction depends on phospholipid composition
title_sort IFABP portal region insertion during membrane interaction depends on phospholipid composition
dc.creator.none.fl_str_mv de Gerónimo, Eduardo
Rodriguez Sawicki, Luciana
Botasso Arias, Natalia
Franchini, Gisela Raquel
Zamarreño, Fernando
Costabel, Marcelo Daniel
Corsico, Betina
Falomir Lockhart, Lisandro Jorge
author de Gerónimo, Eduardo
author_facet de Gerónimo, Eduardo
Rodriguez Sawicki, Luciana
Botasso Arias, Natalia
Franchini, Gisela Raquel
Zamarreño, Fernando
Costabel, Marcelo Daniel
Corsico, Betina
Falomir Lockhart, Lisandro Jorge
author_role author
author2 Rodriguez Sawicki, Luciana
Botasso Arias, Natalia
Franchini, Gisela Raquel
Zamarreño, Fernando
Costabel, Marcelo Daniel
Corsico, Betina
Falomir Lockhart, Lisandro Jorge
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Fatty Acid Binding Protein
Proteinlipid Interaction
Intracellular Lipid Traffic
Intestinal Lipid Traffic
Brominated Phospholipid
topic Fatty Acid Binding Protein
Proteinlipid Interaction
Intracellular Lipid Traffic
Intestinal Lipid Traffic
Brominated Phospholipid
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Intestinal fatty acid-binding protein (IFABP) is highly expressed in the intestinal epithelium and it belongs to the family of soluble lipid binding proteins. These proteins are thought to participate in most aspects of the biology of lipids, regulating its availability for specific metabolic pathways, targeting and vectorial trafficking of lipids to specific subcellular compartments. The present study is based on the ability of IFABP to interact with phospholipid membranes, and we characterized its immersion into the bilayer´s hydrophobic central region occupied by the acyl-chains. We constructed a series of Trp-mutants of IFABP to selectively probe the interaction of different regions of the protein, particularly the elements forming the portal domain that is proposed to regulate the exit and entry of ligands to/from the binding cavity. We employed several fluorescent techniques based on selective quenching induced by soluble or membrane confined agents. The results indicate that the portal region of IFABP penetrates deeply into the phospholipid bilayer, especially when CL-containing vesicles are employed. The orientation of the protein and the degree of penetration were highly dependent on the lipid composition, the superficial net charge and the ionic strength of the medium. These results may be relevant to understand the mechanism of ligand transfer and the specificity responsible for the unique functions of each member of the FABP family.
Fil: de Gerónimo, Eduardo. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires. Estación Experimental Agropecuaria Balcarce. Area de Investigación en Agronomía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Rodriguez Sawicki, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Botasso Arias, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Zamarreño, Fernando. Universidad Nacional del Sur. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Costabel, Marcelo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Bahía Blanca. Instituto de Física del Sur; Argentina. Universidad Nacional del Sur. Departamento de Física; Argentina
Fil: Corsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
Fil: Falomir Lockhart, Lisandro Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - La Plata. Instituto de Investigaciones Bioquímicas de la Plata; Argentina
description Intestinal fatty acid-binding protein (IFABP) is highly expressed in the intestinal epithelium and it belongs to the family of soluble lipid binding proteins. These proteins are thought to participate in most aspects of the biology of lipids, regulating its availability for specific metabolic pathways, targeting and vectorial trafficking of lipids to specific subcellular compartments. The present study is based on the ability of IFABP to interact with phospholipid membranes, and we characterized its immersion into the bilayer´s hydrophobic central region occupied by the acyl-chains. We constructed a series of Trp-mutants of IFABP to selectively probe the interaction of different regions of the protein, particularly the elements forming the portal domain that is proposed to regulate the exit and entry of ligands to/from the binding cavity. We employed several fluorescent techniques based on selective quenching induced by soluble or membrane confined agents. The results indicate that the portal region of IFABP penetrates deeply into the phospholipid bilayer, especially when CL-containing vesicles are employed. The orientation of the protein and the degree of penetration were highly dependent on the lipid composition, the superficial net charge and the ionic strength of the medium. These results may be relevant to understand the mechanism of ligand transfer and the specificity responsible for the unique functions of each member of the FABP family.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/2042
de Gerónimo, Eduardo; Rodriguez Sawicki, Luciana; Botasso Arias, Natalia; Franchini, Gisela Raquel; Zamarreño, Fernando; et al.; IFABP portal region insertion during membrane interaction depends on phospholipid composition; Elsevier; Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids; 1841; 1; 1-2014; 141-150
1388-1981
url http://hdl.handle.net/11336/2042
identifier_str_mv de Gerónimo, Eduardo; Rodriguez Sawicki, Luciana; Botasso Arias, Natalia; Franchini, Gisela Raquel; Zamarreño, Fernando; et al.; IFABP portal region insertion during membrane interaction depends on phospholipid composition; Elsevier; Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids; 1841; 1; 1-2014; 141-150
1388-1981
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbalip.2013.10.011
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1388198113002345
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
publisher.none.fl_str_mv Elsevier
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 13.24909

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