Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights

Autores
Uranga, Romina Maria; Antollini, Silvia Susana; Salvador, Gabriela Alejandra
Año de publicación
2014
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
We have previously demonstrated that oligomeric amyloid β peptide (oAβ), known as the most harmful species of Aβ, concomitant with iron overload led to synaptic injury and local activation of several signaling cascades. In this work, we characterized hippocampal neuronal response to oAβ exposure both in the presence and absence of iron. HT22 neurons exposed to iron overload displayed increased lipid peroxidation, slight loss of mitochondrial function, and activation of ERK and Akt pathways. oAβ neither induced an increase in lipid peroxidation nor altered mitochondrial function. However, oAβ alone triggered the activation of ERK and Akt, and the coincubation with oAβ/iron restored pAkt and pERK to the control levels. In addition, we also studied the effect of iron, oAβ and both conditions together, on the biophysical state of the plasma membrane by measuring the generalized polarization of the fluorescence probe Laurdan and the fluorescence anisotropy of DPH and TMA-DPH. Both studies showed that the presence of iron (even at the highest concentration tested), oAβ, or both conditions together, did not perturb the lipid order of the membrane. We conclude that oAβ activates signaling pathways in the absence of oxidative stress or membrane disturbances in hippocampal neurons.
Fil: Uranga, Romina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Salvador, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Rosario
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Materia
NEURODEGENERATION
AMYLOID PEPTIDE
HIPPOCAMPUS
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:11336/235389

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network_name_str CONICET Digital (CONICET)
spelling Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insightsUranga, Romina MariaAntollini, Silvia SusanaSalvador, Gabriela AlejandraNEURODEGENERATIONAMYLOID PEPTIDEHIPPOCAMPUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We have previously demonstrated that oligomeric amyloid β peptide (oAβ), known as the most harmful species of Aβ, concomitant with iron overload led to synaptic injury and local activation of several signaling cascades. In this work, we characterized hippocampal neuronal response to oAβ exposure both in the presence and absence of iron. HT22 neurons exposed to iron overload displayed increased lipid peroxidation, slight loss of mitochondrial function, and activation of ERK and Akt pathways. oAβ neither induced an increase in lipid peroxidation nor altered mitochondrial function. However, oAβ alone triggered the activation of ERK and Akt, and the coincubation with oAβ/iron restored pAkt and pERK to the control levels. In addition, we also studied the effect of iron, oAβ and both conditions together, on the biophysical state of the plasma membrane by measuring the generalized polarization of the fluorescence probe Laurdan and the fluorescence anisotropy of DPH and TMA-DPH. Both studies showed that the presence of iron (even at the highest concentration tested), oAβ, or both conditions together, did not perturb the lipid order of the membrane. We conclude that oAβ activates signaling pathways in the absence of oxidative stress or membrane disturbances in hippocampal neurons.Fil: Uranga, Romina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Salvador, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaL Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología MolecularRosarioArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularTech Science Press2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/235389Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights; L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Rosario; Argentina; 2014; 112-1120327-9545CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v38nSuppl.S/34067/pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:02:17Zoai:ri.conicet.gov.ar:11336/235389instacron: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:34982025-09-03 10:02:17.586CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
title Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
spellingShingle Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
Uranga, Romina Maria
NEURODEGENERATION
AMYLOID PEPTIDE
HIPPOCAMPUS
title_short Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
title_full Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
title_fullStr Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
title_full_unstemmed Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
title_sort Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights
dc.creator.none.fl_str_mv Uranga, Romina Maria
Antollini, Silvia Susana
Salvador, Gabriela Alejandra
author Uranga, Romina Maria
author_facet Uranga, Romina Maria
Antollini, Silvia Susana
Salvador, Gabriela Alejandra
author_role author
author2 Antollini, Silvia Susana
Salvador, Gabriela Alejandra
author2_role author
author
dc.subject.none.fl_str_mv NEURODEGENERATION
AMYLOID PEPTIDE
HIPPOCAMPUS
topic NEURODEGENERATION
AMYLOID PEPTIDE
HIPPOCAMPUS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We have previously demonstrated that oligomeric amyloid β peptide (oAβ), known as the most harmful species of Aβ, concomitant with iron overload led to synaptic injury and local activation of several signaling cascades. In this work, we characterized hippocampal neuronal response to oAβ exposure both in the presence and absence of iron. HT22 neurons exposed to iron overload displayed increased lipid peroxidation, slight loss of mitochondrial function, and activation of ERK and Akt pathways. oAβ neither induced an increase in lipid peroxidation nor altered mitochondrial function. However, oAβ alone triggered the activation of ERK and Akt, and the coincubation with oAβ/iron restored pAkt and pERK to the control levels. In addition, we also studied the effect of iron, oAβ and both conditions together, on the biophysical state of the plasma membrane by measuring the generalized polarization of the fluorescence probe Laurdan and the fluorescence anisotropy of DPH and TMA-DPH. Both studies showed that the presence of iron (even at the highest concentration tested), oAβ, or both conditions together, did not perturb the lipid order of the membrane. We conclude that oAβ activates signaling pathways in the absence of oxidative stress or membrane disturbances in hippocampal neurons.
Fil: Uranga, Romina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Salvador, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Rosario
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
description We have previously demonstrated that oligomeric amyloid β peptide (oAβ), known as the most harmful species of Aβ, concomitant with iron overload led to synaptic injury and local activation of several signaling cascades. In this work, we characterized hippocampal neuronal response to oAβ exposure both in the presence and absence of iron. HT22 neurons exposed to iron overload displayed increased lipid peroxidation, slight loss of mitochondrial function, and activation of ERK and Akt pathways. oAβ neither induced an increase in lipid peroxidation nor altered mitochondrial function. However, oAβ alone triggered the activation of ERK and Akt, and the coincubation with oAβ/iron restored pAkt and pERK to the control levels. In addition, we also studied the effect of iron, oAβ and both conditions together, on the biophysical state of the plasma membrane by measuring the generalized polarization of the fluorescence probe Laurdan and the fluorescence anisotropy of DPH and TMA-DPH. Both studies showed that the presence of iron (even at the highest concentration tested), oAβ, or both conditions together, did not perturb the lipid order of the membrane. We conclude that oAβ activates signaling pathways in the absence of oxidative stress or membrane disturbances in hippocampal neurons.
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/235389
Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights; L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Rosario; Argentina; 2014; 112-112
0327-9545
CONICET Digital
CONICET
url http://hdl.handle.net/11336/235389
identifier_str_mv Hippocampal neuronal response to amyloid β peptide oligomers. Biological and biophysical insights; L Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Rosario; Argentina; 2014; 112-112
0327-9545
CONICET Digital
CONICET
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language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v38nSuppl.S/34067/pdf
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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/
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application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Tech Science Press
publisher.none.fl_str_mv Tech Science Press
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