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dc.contributor.author
Saporito Magriñá, Christian Martín
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Facio, Maria Laura
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Lopez Montañana, Lila Lucia
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Pagano, Guadalupe Belén
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Repetto, Marisa Gabriela
dc.date.available
2024-02-20T14:39:48Z
dc.date.issued
2023-01
dc.identifier.citation
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
dc.identifier.issn
1756-5901
dc.identifier.uri
http://hdl.handle.net/11336/227605
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Royal Society of Chemistry
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
AGGREGATES
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COPPER
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IGG
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IMMUNOGLOBULIN
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PROTEIN
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Γ-GLOBULIN
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Copper-induced aggregation of IgG: a potential driving force for the formation of circulating protein aggregates
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-02-20T12:50:30Z
dc.journal.volume
15
dc.journal.number
2
dc.journal.pagination
1-33
dc.journal.pais
Reino Unido
dc.journal.ciudad
Cambridge
dc.description.fil
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
dc.description.fil
Fil: Facio, Maria Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Fisiopatología y Bioquímica Clínica; Argentina
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Fil: Lopez Montañana, Lila Lucia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
dc.description.fil
Fil: Pagano, Guadalupe Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
dc.description.fil
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
dc.journal.title
Metallomics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1093/mtomcs/mfad005
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