Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates

Autores
Saporito Magriñá, Christian Martín; Facio, Maria Laura; Lopez Montañana, Lila Lucia; Pagano, Guadalupe Belén; Repetto, Marisa Gabriela
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Copper is a highly reactive element involved in a myriad of biological reactions. Thus, while essential for mammalian cells, its concentrations must be kept in check in order to avoid toxicity. This metal participates in redox reactions and may exacerbate oxidative stress in aerobic organisms. Nonetheless, the actual driving force of copper-induced cell death is yet unknown. Likely, free copper ions may target different biomolecules that are crucial for the proper functioning of an organism. In this work, we show that free copper induces protein aggregation in serum. The wide set of proteins present in these biological samples are not equally prone to copper-induced aggregation and some, such as albumin, are highly resistant, whereas γ-globulins are highly sensitive. The identity of the proteins in the aggregates becomes fairly homogeneous as metal concentrations go as low as 20 μM. The identification of the proteins by mass spectrometry indicates a preponderance of IgG and a minor presence of other different proteins. Therefore, free copper in blood may contribute to the formation of circulating protein aggregates with a core of IgG. This may impact health not only due to the activity of aggregated IgG but also due to the many proteins co-aggregated. Understanding whether the γ-globulin core and the heterogeneous subgroup of proteins elicit differential responses in the organisms requires further research.
Fil: Saporito Magriñá, Christian Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Facio, Maria Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Fisiopatología y Bioquímica Clínica; Argentina
Fil: Lopez Montañana, Lila Lucia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Pagano, Guadalupe Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Repetto, Marisa Gabriela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina
Materia
AGGREGATES
COPPER
IGG
IMMUNOGLOBULIN
PROTEIN
Γ-GLOBULIN
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:11336/227605
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/227605
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spelling Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregatesSaporito Magriñá, Christian MartínFacio, Maria LauraLopez Montañana, Lila LuciaPagano, Guadalupe BelénRepetto, Marisa GabrielaAGGREGATESCOPPERIGGIMMUNOGLOBULINPROTEINΓ-GLOBULINhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Copper is a highly reactive element involved in a myriad of biological reactions. Thus, while essential for mammalian cells, its concentrations must be kept in check in order to avoid toxicity. This metal participates in redox reactions and may exacerbate oxidative stress in aerobic organisms. Nonetheless, the actual driving force of copper-induced cell death is yet unknown. Likely, free copper ions may target different biomolecules that are crucial for the proper functioning of an organism. In this work, we show that free copper induces protein aggregation in serum. The wide set of proteins present in these biological samples are not equally prone to copper-induced aggregation and some, such as albumin, are highly resistant, whereas γ-globulins are highly sensitive. The identity of the proteins in the aggregates becomes fairly homogeneous as metal concentrations go as low as 20 μM. The identification of the proteins by mass spectrometry indicates a preponderance of IgG and a minor presence of other different proteins. Therefore, free copper in blood may contribute to the formation of circulating protein aggregates with a core of IgG. This may impact health not only due to the activity of aggregated IgG but also due to the many proteins co-aggregated. Understanding whether the γ-globulin core and the heterogeneous subgroup of proteins elicit differential responses in the organisms requires further research.Fil: Saporito Magriñá, Christian Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Facio, Maria Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Fisiopatología y Bioquímica Clínica; ArgentinaFil: Lopez Montañana, Lila Lucia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Pagano, Guadalupe Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Repetto, Marisa Gabriela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; ArgentinaRoyal Society of Chemistry2023-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/227605Saporito Magriñá, Christian Martín; Facio, Maria Laura; Lopez Montañana, Lila Lucia; Pagano, Guadalupe Belén; Repetto, Marisa Gabriela; Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates; Royal Society of Chemistry; Metallomics; 15; 2; 1-2023; 1-331756-5901CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/mtomcs/mfad005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:38:08Zoai:ri.conicet.gov.ar:11336/227605instacron: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:34982025-10-15 15:38:08.763CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
title Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
spellingShingle Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
Saporito Magriñá, Christian Martín
AGGREGATES
COPPER
IGG
IMMUNOGLOBULIN
PROTEIN
Γ-GLOBULIN
title_short Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
title_full Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
title_fullStr Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
title_full_unstemmed Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
title_sort Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
dc.creator.none.fl_str_mv Saporito Magriñá, Christian Martín
Facio, Maria Laura
Lopez Montañana, Lila Lucia
Pagano, Guadalupe Belén
Repetto, Marisa Gabriela
author Saporito Magriñá, Christian Martín
author_facet Saporito Magriñá, Christian Martín
Facio, Maria Laura
Lopez Montañana, Lila Lucia
Pagano, Guadalupe Belén
Repetto, Marisa Gabriela
author_role author
author2 Facio, Maria Laura
Lopez Montañana, Lila Lucia
Pagano, Guadalupe Belén
Repetto, Marisa Gabriela
author2_role author
author
author
author
dc.subject.none.fl_str_mv AGGREGATES
COPPER
IGG
IMMUNOGLOBULIN
PROTEIN
Γ-GLOBULIN
topic AGGREGATES
COPPER
IGG
IMMUNOGLOBULIN
PROTEIN
Γ-GLOBULIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Copper is a highly reactive element involved in a myriad of biological reactions. Thus, while essential for mammalian cells, its concentrations must be kept in check in order to avoid toxicity. This metal participates in redox reactions and may exacerbate oxidative stress in aerobic organisms. Nonetheless, the actual driving force of copper-induced cell death is yet unknown. Likely, free copper ions may target different biomolecules that are crucial for the proper functioning of an organism. In this work, we show that free copper induces protein aggregation in serum. The wide set of proteins present in these biological samples are not equally prone to copper-induced aggregation and some, such as albumin, are highly resistant, whereas γ-globulins are highly sensitive. The identity of the proteins in the aggregates becomes fairly homogeneous as metal concentrations go as low as 20 μM. The identification of the proteins by mass spectrometry indicates a preponderance of IgG and a minor presence of other different proteins. Therefore, free copper in blood may contribute to the formation of circulating protein aggregates with a core of IgG. This may impact health not only due to the activity of aggregated IgG but also due to the many proteins co-aggregated. Understanding whether the γ-globulin core and the heterogeneous subgroup of proteins elicit differential responses in the organisms requires further research.
Fil: Saporito Magriñá, Christian Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Facio, Maria Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Fisiopatología y Bioquímica Clínica; Argentina
Fil: Lopez Montañana, Lila Lucia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Pagano, Guadalupe Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Repetto, Marisa Gabriela. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina
description Copper is a highly reactive element involved in a myriad of biological reactions. Thus, while essential for mammalian cells, its concentrations must be kept in check in order to avoid toxicity. This metal participates in redox reactions and may exacerbate oxidative stress in aerobic organisms. Nonetheless, the actual driving force of copper-induced cell death is yet unknown. Likely, free copper ions may target different biomolecules that are crucial for the proper functioning of an organism. In this work, we show that free copper induces protein aggregation in serum. The wide set of proteins present in these biological samples are not equally prone to copper-induced aggregation and some, such as albumin, are highly resistant, whereas γ-globulins are highly sensitive. The identity of the proteins in the aggregates becomes fairly homogeneous as metal concentrations go as low as 20 μM. The identification of the proteins by mass spectrometry indicates a preponderance of IgG and a minor presence of other different proteins. Therefore, free copper in blood may contribute to the formation of circulating protein aggregates with a core of IgG. This may impact health not only due to the activity of aggregated IgG but also due to the many proteins co-aggregated. Understanding whether the γ-globulin core and the heterogeneous subgroup of proteins elicit differential responses in the organisms requires further research.
publishDate 2023
dc.date.none.fl_str_mv 2023-01
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/11336/227605
Saporito Magriñá, Christian Martín; Facio, Maria Laura; Lopez Montañana, Lila Lucia; Pagano, Guadalupe Belén; Repetto, Marisa Gabriela; Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates; Royal Society of Chemistry; Metallomics; 15; 2; 1-2023; 1-33
1756-5901
CONICET Digital
CONICET
url http://hdl.handle.net/11336/227605
identifier_str_mv Saporito Magriñá, Christian Martín; Facio, Maria Laura; Lopez Montañana, Lila Lucia; Pagano, Guadalupe Belén; Repetto, Marisa Gabriela; Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates; Royal Society of Chemistry; Metallomics; 15; 2; 1-2023; 1-33
1756-5901
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/mtomcs/mfad005
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 Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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_ 1846083500846874624
score 13.22299

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