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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/102723
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:37:11Zoai: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:34982025-10-22 11:37:11.526CONICET 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
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score 12.982451

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