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

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 pat...

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Detalles Bibliográficos
Autores principales: 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
Formato: Articulo
Lenguaje:Inglés
Publicado: 2011
Materias:
Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/29561
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0022532
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-29561
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
spellingShingle Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
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
Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
topic_facet Ciencias Médicas
Bioquímica
Amiloidosis
Apolipoproteína A-I
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.
format Articulo
Articulo
author 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_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_sort Ramella, Nahuel Alberto
title Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
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
publishDate 2011
url http://sedici.unlp.edu.ar/handle/10915/29561
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0022532
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