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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3139661/ https://www.ncbi.nlm.nih.gov/pubmed/21811627 http://dx.doi.org/10.1371/journal.pone.0022532 |
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author | Ramella, Nahuel A. Rimoldi, Omar J. Prieto, Eduardo D. Schinella, Guillermo R. Sanchez, Susana A. Jaureguiberry, María S. Vela, María E. Ferreira, Sergio T. Tricerri, M. Alejandra |
author_facet | Ramella, Nahuel A. Rimoldi, Omar J. Prieto, Eduardo D. Schinella, Guillermo R. Sanchez, Susana A. Jaureguiberry, María S. Vela, María E. Ferreira, Sergio T. Tricerri, M. Alejandra |
author_sort | Ramella, Nahuel A. |
collection | PubMed |
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 | Online Article Text |
id | pubmed-3139661 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-31396612011-08-02 Human Apolipoprotein A-I-Derived Amyloid: Its Association with Atherosclerosis Ramella, Nahuel A. Rimoldi, Omar J. Prieto, Eduardo D. Schinella, Guillermo R. Sanchez, Susana A. Jaureguiberry, María S. Vela, María E. Ferreira, Sergio T. Tricerri, M. Alejandra PLoS One Research Article 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. Public Library of Science 2011-07-19 /pmc/articles/PMC3139661/ /pubmed/21811627 http://dx.doi.org/10.1371/journal.pone.0022532 Text en Ramella et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ramella, Nahuel A. Rimoldi, Omar J. Prieto, Eduardo D. Schinella, Guillermo R. Sanchez, Susana A. Jaureguiberry, María S. Vela, María E. Ferreira, Sergio T. Tricerri, M. Alejandra Human Apolipoprotein A-I-Derived Amyloid: Its Association with Atherosclerosis |
title | 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_short | Human Apolipoprotein A-I-Derived Amyloid: Its Association with Atherosclerosis |
title_sort | human apolipoprotein a-i-derived amyloid: its association with atherosclerosis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3139661/ https://www.ncbi.nlm.nih.gov/pubmed/21811627 http://dx.doi.org/10.1371/journal.pone.0022532 |
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