Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis

Autores
Ramella, Nahuel Alberto; Rimoldi, Omar Jorge; Prieto, Eduardo Daniel; Schinella, Guillermo; Sánchez, Susana; Jaureguiberry, M. Soledad; Vela, María Elena; Ferreira, Sergio T.; Tricerri, María Alejandra
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.
Facultad de Ciencias Médicas
Materia
Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/29561
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/29561
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Human apolipoprotein A-I-derived amyloid: its association with atherosclerosisRamella, Nahuel AlbertoRimoldi, Omar JorgePrieto, Eduardo DanielSchinella, GuillermoSánchez, SusanaJaureguiberry, M. SoledadVela, María ElenaFerreira, Sergio T.Tricerri, María AlejandraCiencias MédicasBioquímicaAmiloidosisApolipoproteína A-IAmyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.Facultad de Ciencias Médicas2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/29561enginfo:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0022532info:eu-repo/semantics/altIdentifier/issn/1932-6203info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0022532info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar/Creative Commons Attribution 2.5 Argentina (CC BY 2.5)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:29:55Zoai:sedici.unlp.edu.ar:10915/29561Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:29:55.823SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
title Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
spellingShingle Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
Ramella, Nahuel Alberto
Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
title_short Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
title_full Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
title_fullStr Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
title_full_unstemmed Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
title_sort Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
dc.creator.none.fl_str_mv Ramella, Nahuel Alberto
Rimoldi, Omar Jorge
Prieto, Eduardo Daniel
Schinella, Guillermo
Sánchez, Susana
Jaureguiberry, M. Soledad
Vela, María Elena
Ferreira, Sergio T.
Tricerri, María Alejandra
author Ramella, Nahuel Alberto
author_facet Ramella, Nahuel Alberto
Rimoldi, Omar Jorge
Prieto, Eduardo Daniel
Schinella, Guillermo
Sánchez, Susana
Jaureguiberry, M. Soledad
Vela, María Elena
Ferreira, Sergio T.
Tricerri, María Alejandra
author_role author
author2 Rimoldi, Omar Jorge
Prieto, Eduardo Daniel
Schinella, Guillermo
Sánchez, Susana
Jaureguiberry, M. Soledad
Vela, María Elena
Ferreira, Sergio T.
Tricerri, María Alejandra
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
topic Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
dc.description.none.fl_txt_mv Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.
Facultad de Ciencias Médicas
description Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/29561
url http://sedici.unlp.edu.ar/handle/10915/29561
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0022532
info:eu-repo/semantics/altIdentifier/issn/1932-6203
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0022532
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar/
Creative Commons Attribution 2.5 Argentina (CC BY 2.5)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar/
Creative Commons Attribution 2.5 Argentina (CC BY 2.5)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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