Ferritin-dependent radical generation in rat liver homogenates
- Autores
- Rousseau, Iván; Puntarulo, Susana Ángela
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The hypothesis of this study was that mammalian ferritin (FER) has the ability of releasing Fe in the tissue to catalyze the generation of free radicals, such as ascorbyl (A) and hydroxyl radical (OH), that might lead to the damage of FER itself. The rat liver homogenates exhibited an electron paramagnetic resonance (EPR) signal with the spectral features (a(H)=1.88 G, g=2.0054) of A. The addition to the reaction medium of isolated rat liver FER increased by 3-fold the EPR signal, as compared to the recorded value in its absence. Isolated microsomes from rat liver incubated during 10 min showed a signal with the spectral features (a(H)=15G, g=2.0062) of OH. The addition of FER in the presence of either ethylenediamine-tetraacetic acid (EDTA) or adenosine-5'-triphosphate (ATP) significantly increased the recorded spectra. The labile Fe pool (LIP) in the homogenate was assessed by EPR. The rat liver homogenates exhibited an EPR signal with the spectral features (g=4.3) of the Fe(2+) and was significantly increased by the addition of FER (3-fold). The oxidation profile of the isolated FER from rat liver was analyzed after incubation with 10 mM ascorbate (AH(-)). A drastic increase in the width of the band suggested alterations to the protein structure. The FER content of tryptophan (Trp) and thiols was significantly lower when the incubation was performed in the presence of AH(-) as compared to the recorded effect in its absence. The data in tissue homogenates presented here showed that radical generation is associated to FER Fe release, and moreover that the FER protein itself was affected during this process.
Fil: Rousseau, Iván. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Puntarulo, Susana Ángela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina - Materia
-
FERRITIN
LABILE IRON POOL
FREE RADICAL - 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:11336/102723
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Ferritin-dependent radical generation in rat liver homogenatesRousseau, IvánPuntarulo, Susana ÁngelaFERRITINLABILE IRON POOLFREE RADICALhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The hypothesis of this study was that mammalian ferritin (FER) has the ability of releasing Fe in the tissue to catalyze the generation of free radicals, such as ascorbyl (A) and hydroxyl radical (OH), that might lead to the damage of FER itself. The rat liver homogenates exhibited an electron paramagnetic resonance (EPR) signal with the spectral features (a(H)=1.88 G, g=2.0054) of A. The addition to the reaction medium of isolated rat liver FER increased by 3-fold the EPR signal, as compared to the recorded value in its absence. Isolated microsomes from rat liver incubated during 10 min showed a signal with the spectral features (a(H)=15G, g=2.0062) of OH. The addition of FER in the presence of either ethylenediamine-tetraacetic acid (EDTA) or adenosine-5'-triphosphate (ATP) significantly increased the recorded spectra. The labile Fe pool (LIP) in the homogenate was assessed by EPR. The rat liver homogenates exhibited an EPR signal with the spectral features (g=4.3) of the Fe(2+) and was significantly increased by the addition of FER (3-fold). The oxidation profile of the isolated FER from rat liver was analyzed after incubation with 10 mM ascorbate (AH(-)). A drastic increase in the width of the band suggested alterations to the protein structure. The FER content of tryptophan (Trp) and thiols was significantly lower when the incubation was performed in the presence of AH(-) as compared to the recorded effect in its absence. The data in tissue homogenates presented here showed that radical generation is associated to FER Fe release, and moreover that the FER protein itself was affected during this process.Fil: Rousseau, Iván. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Puntarulo, Susana Ángela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Ireland2009-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/mswordapplication/pdfhttp://hdl.handle.net/11336/102723Rousseau, Iván; Puntarulo, Susana Ángela; Ferritin-dependent radical generation in rat liver homogenates; Elsevier Ireland; Toxicology; 264; 3; 10-2009; 155-1610300-483XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.journals.elsevier.com/toxicologyinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.tox.2009.07.019info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:07:16Zoai:ri.conicet.gov.ar:11336/102723instacron: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 10:07:16.398CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Ferritin-dependent radical generation in rat liver homogenates |
title |
Ferritin-dependent radical generation in rat liver homogenates |
spellingShingle |
Ferritin-dependent radical generation in rat liver homogenates Rousseau, Iván FERRITIN LABILE IRON POOL FREE RADICAL |
title_short |
Ferritin-dependent radical generation in rat liver homogenates |
title_full |
Ferritin-dependent radical generation in rat liver homogenates |
title_fullStr |
Ferritin-dependent radical generation in rat liver homogenates |
title_full_unstemmed |
Ferritin-dependent radical generation in rat liver homogenates |
title_sort |
Ferritin-dependent radical generation in rat liver homogenates |
dc.creator.none.fl_str_mv |
Rousseau, Iván Puntarulo, Susana Ángela |
author |
Rousseau, Iván |
author_facet |
Rousseau, Iván Puntarulo, Susana Ángela |
author_role |
author |
author2 |
Puntarulo, Susana Ángela |
author2_role |
author |
dc.subject.none.fl_str_mv |
FERRITIN LABILE IRON POOL FREE RADICAL |
topic |
FERRITIN LABILE IRON POOL FREE RADICAL |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The hypothesis of this study was that mammalian ferritin (FER) has the ability of releasing Fe in the tissue to catalyze the generation of free radicals, such as ascorbyl (A) and hydroxyl radical (OH), that might lead to the damage of FER itself. The rat liver homogenates exhibited an electron paramagnetic resonance (EPR) signal with the spectral features (a(H)=1.88 G, g=2.0054) of A. The addition to the reaction medium of isolated rat liver FER increased by 3-fold the EPR signal, as compared to the recorded value in its absence. Isolated microsomes from rat liver incubated during 10 min showed a signal with the spectral features (a(H)=15G, g=2.0062) of OH. The addition of FER in the presence of either ethylenediamine-tetraacetic acid (EDTA) or adenosine-5'-triphosphate (ATP) significantly increased the recorded spectra. The labile Fe pool (LIP) in the homogenate was assessed by EPR. The rat liver homogenates exhibited an EPR signal with the spectral features (g=4.3) of the Fe(2+) and was significantly increased by the addition of FER (3-fold). The oxidation profile of the isolated FER from rat liver was analyzed after incubation with 10 mM ascorbate (AH(-)). A drastic increase in the width of the band suggested alterations to the protein structure. The FER content of tryptophan (Trp) and thiols was significantly lower when the incubation was performed in the presence of AH(-) as compared to the recorded effect in its absence. The data in tissue homogenates presented here showed that radical generation is associated to FER Fe release, and moreover that the FER protein itself was affected during this process. Fil: Rousseau, Iván. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina Fil: Puntarulo, Susana Ángela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
description |
The hypothesis of this study was that mammalian ferritin (FER) has the ability of releasing Fe in the tissue to catalyze the generation of free radicals, such as ascorbyl (A) and hydroxyl radical (OH), that might lead to the damage of FER itself. The rat liver homogenates exhibited an electron paramagnetic resonance (EPR) signal with the spectral features (a(H)=1.88 G, g=2.0054) of A. The addition to the reaction medium of isolated rat liver FER increased by 3-fold the EPR signal, as compared to the recorded value in its absence. Isolated microsomes from rat liver incubated during 10 min showed a signal with the spectral features (a(H)=15G, g=2.0062) of OH. The addition of FER in the presence of either ethylenediamine-tetraacetic acid (EDTA) or adenosine-5'-triphosphate (ATP) significantly increased the recorded spectra. The labile Fe pool (LIP) in the homogenate was assessed by EPR. The rat liver homogenates exhibited an EPR signal with the spectral features (g=4.3) of the Fe(2+) and was significantly increased by the addition of FER (3-fold). The oxidation profile of the isolated FER from rat liver was analyzed after incubation with 10 mM ascorbate (AH(-)). A drastic increase in the width of the band suggested alterations to the protein structure. The FER content of tryptophan (Trp) and thiols was significantly lower when the incubation was performed in the presence of AH(-) as compared to the recorded effect in its absence. The data in tissue homogenates presented here showed that radical generation is associated to FER Fe release, and moreover that the FER protein itself was affected during this process. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-10 |
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/11336/102723 Rousseau, Iván; Puntarulo, Susana Ángela; Ferritin-dependent radical generation in rat liver homogenates; Elsevier Ireland; Toxicology; 264; 3; 10-2009; 155-161 0300-483X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/102723 |
identifier_str_mv |
Rousseau, Iván; Puntarulo, Susana Ángela; Ferritin-dependent radical generation in rat liver homogenates; Elsevier Ireland; Toxicology; 264; 3; 10-2009; 155-161 0300-483X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.journals.elsevier.com/toxicology info:eu-repo/semantics/altIdentifier/doi/10.1016/j.tox.2009.07.019 |
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/msword application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Ireland |
publisher.none.fl_str_mv |
Elsevier Ireland |
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 |
_version_ |
1844613930169663488 |
score |
13.070432 |