Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit
- Autores
- Brites, Fernando Daniel; Martin, Maximiliano Emanuel; Guillas, Isabelle; Kontush, Anatol
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Uptake of low-density lipoprotein (LDL) particles by macrophages represents a key step in the development of atherosclerotic plaques, leading to the foam cell formation. Chemical modification of LDL is however necessary to induce this process. Proatherogenic LDL modifications include aggregation, enzymatic digestion and oxidation. LDL oxidation by one-electron (free radicals) and two-electron oxidants dramatically increases LDL affinity to macrophage scavenger receptors, leading to rapid LDL uptake and fatty streak formation. Circulating high-density lipoprotein (HDL) particles, primarily small, dense, protein-rich HDL3, provide potent protection of LDL from oxidative damage by free radicals, resulting in the inhibition of the generation of pro-inflammatory oxidized lipids. HDL-mediated inactivation of lipid hydroperoxides involves their initial transfer from LDL to HDL and subsequent reduction to inactive hydroxides by redox-active Met residues of apolipoprotein A-I. Several HDL-associated enzymes are present at elevated concentrations in HDL3 relative to large, light HDL2 and can be involved in the inactivation of short-chain oxidized phospholipids. Therefore, HDL represents a multimolecular complex capable of acquiring and inactivating proatherogenic lipids. Antioxidative function of HDL can be impaired in several metabolic and inflammatory diseases. Structural and compositional anomalies in the HDL proteome and lipidome underlie such functional deficiency. Concomitant normalization of the metabolism, circulating levels, composition and biological activities of HDL particles, primarily those of small, dense HDL3, can constitute future therapeutic target.
Fil: Brites, Fernando Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; Argentina
Fil: Martin, Maximiliano Emanuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; Argentina
Fil: Guillas, Isabelle. Universite Pierre et Marie Curie; Francia. Inserm; Francia
Fil: Kontush, Anatol. Universite Pierre et Marie Curie; Francia. Inserm; Francia - Materia
- HDL
- Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/49754
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Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefitBrites, Fernando DanielMartin, Maximiliano EmanuelGuillas, IsabelleKontush, AnatolHDLhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Uptake of low-density lipoprotein (LDL) particles by macrophages represents a key step in the development of atherosclerotic plaques, leading to the foam cell formation. Chemical modification of LDL is however necessary to induce this process. Proatherogenic LDL modifications include aggregation, enzymatic digestion and oxidation. LDL oxidation by one-electron (free radicals) and two-electron oxidants dramatically increases LDL affinity to macrophage scavenger receptors, leading to rapid LDL uptake and fatty streak formation. Circulating high-density lipoprotein (HDL) particles, primarily small, dense, protein-rich HDL3, provide potent protection of LDL from oxidative damage by free radicals, resulting in the inhibition of the generation of pro-inflammatory oxidized lipids. HDL-mediated inactivation of lipid hydroperoxides involves their initial transfer from LDL to HDL and subsequent reduction to inactive hydroxides by redox-active Met residues of apolipoprotein A-I. Several HDL-associated enzymes are present at elevated concentrations in HDL3 relative to large, light HDL2 and can be involved in the inactivation of short-chain oxidized phospholipids. Therefore, HDL represents a multimolecular complex capable of acquiring and inactivating proatherogenic lipids. Antioxidative function of HDL can be impaired in several metabolic and inflammatory diseases. Structural and compositional anomalies in the HDL proteome and lipidome underlie such functional deficiency. Concomitant normalization of the metabolism, circulating levels, composition and biological activities of HDL particles, primarily those of small, dense HDL3, can constitute future therapeutic target.Fil: Brites, Fernando Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; ArgentinaFil: Martin, Maximiliano Emanuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; ArgentinaFil: Guillas, Isabelle. Universite Pierre et Marie Curie; Francia. Inserm; FranciaFil: Kontush, Anatol. Universite Pierre et Marie Curie; Francia. Inserm; FranciaElsevier2017-12-19info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/49754Brites, Fernando Daniel; Martin, Maximiliano Emanuel; Guillas, Isabelle; Kontush, Anatol; Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit; Elsevier; BBA Clinical; 8; 19-12-2017; 66-772214-6474CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbacli.2017.07.002info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2214647417300326info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:03:57Zoai:ri.conicet.gov.ar:11336/49754instacron: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 10:03:57.978CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
title |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
spellingShingle |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit Brites, Fernando Daniel HDL |
title_short |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
title_full |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
title_fullStr |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
title_full_unstemmed |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
title_sort |
Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit |
dc.creator.none.fl_str_mv |
Brites, Fernando Daniel Martin, Maximiliano Emanuel Guillas, Isabelle Kontush, Anatol |
author |
Brites, Fernando Daniel |
author_facet |
Brites, Fernando Daniel Martin, Maximiliano Emanuel Guillas, Isabelle Kontush, Anatol |
author_role |
author |
author2 |
Martin, Maximiliano Emanuel Guillas, Isabelle Kontush, Anatol |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
HDL |
topic |
HDL |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.3 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
Uptake of low-density lipoprotein (LDL) particles by macrophages represents a key step in the development of atherosclerotic plaques, leading to the foam cell formation. Chemical modification of LDL is however necessary to induce this process. Proatherogenic LDL modifications include aggregation, enzymatic digestion and oxidation. LDL oxidation by one-electron (free radicals) and two-electron oxidants dramatically increases LDL affinity to macrophage scavenger receptors, leading to rapid LDL uptake and fatty streak formation. Circulating high-density lipoprotein (HDL) particles, primarily small, dense, protein-rich HDL3, provide potent protection of LDL from oxidative damage by free radicals, resulting in the inhibition of the generation of pro-inflammatory oxidized lipids. HDL-mediated inactivation of lipid hydroperoxides involves their initial transfer from LDL to HDL and subsequent reduction to inactive hydroxides by redox-active Met residues of apolipoprotein A-I. Several HDL-associated enzymes are present at elevated concentrations in HDL3 relative to large, light HDL2 and can be involved in the inactivation of short-chain oxidized phospholipids. Therefore, HDL represents a multimolecular complex capable of acquiring and inactivating proatherogenic lipids. Antioxidative function of HDL can be impaired in several metabolic and inflammatory diseases. Structural and compositional anomalies in the HDL proteome and lipidome underlie such functional deficiency. Concomitant normalization of the metabolism, circulating levels, composition and biological activities of HDL particles, primarily those of small, dense HDL3, can constitute future therapeutic target. Fil: Brites, Fernando Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; Argentina Fil: Martin, Maximiliano Emanuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica. Laboratorio de Lípidos y Artroesclerosis; Argentina Fil: Guillas, Isabelle. Universite Pierre et Marie Curie; Francia. Inserm; Francia Fil: Kontush, Anatol. Universite Pierre et Marie Curie; Francia. Inserm; Francia |
description |
Uptake of low-density lipoprotein (LDL) particles by macrophages represents a key step in the development of atherosclerotic plaques, leading to the foam cell formation. Chemical modification of LDL is however necessary to induce this process. Proatherogenic LDL modifications include aggregation, enzymatic digestion and oxidation. LDL oxidation by one-electron (free radicals) and two-electron oxidants dramatically increases LDL affinity to macrophage scavenger receptors, leading to rapid LDL uptake and fatty streak formation. Circulating high-density lipoprotein (HDL) particles, primarily small, dense, protein-rich HDL3, provide potent protection of LDL from oxidative damage by free radicals, resulting in the inhibition of the generation of pro-inflammatory oxidized lipids. HDL-mediated inactivation of lipid hydroperoxides involves their initial transfer from LDL to HDL and subsequent reduction to inactive hydroxides by redox-active Met residues of apolipoprotein A-I. Several HDL-associated enzymes are present at elevated concentrations in HDL3 relative to large, light HDL2 and can be involved in the inactivation of short-chain oxidized phospholipids. Therefore, HDL represents a multimolecular complex capable of acquiring and inactivating proatherogenic lipids. Antioxidative function of HDL can be impaired in several metabolic and inflammatory diseases. Structural and compositional anomalies in the HDL proteome and lipidome underlie such functional deficiency. Concomitant normalization of the metabolism, circulating levels, composition and biological activities of HDL particles, primarily those of small, dense HDL3, can constitute future therapeutic target. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-12-19 |
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/11336/49754 Brites, Fernando Daniel; Martin, Maximiliano Emanuel; Guillas, Isabelle; Kontush, Anatol; Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit; Elsevier; BBA Clinical; 8; 19-12-2017; 66-77 2214-6474 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/49754 |
identifier_str_mv |
Brites, Fernando Daniel; Martin, Maximiliano Emanuel; Guillas, Isabelle; Kontush, Anatol; Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit; Elsevier; BBA Clinical; 8; 19-12-2017; 66-77 2214-6474 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbacli.2017.07.002 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2214647417300326 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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1842269829335089152 |
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13.13397 |