Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
Open accessAbstract
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.
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ThT fluorescence intensity is low in aqueous solution but increases upon binding of the probe to amyloid aggregates.
“ThT fluorescence intensity is low in aqueous solution, but it increases upon binding of the probe to amyloid aggregates”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [40]
ThT has been used previously to monitor the aggregation and amyloidogenic propensity of apolipoproteins.
“has been used previously to monitor the aggregation and amyloidogenic propensity of apolipoproteins (39,40)”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [40]
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Katsarou, M., Stratikos, E., & Chroni, A. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m088732 · Cited by 22 · see citing works
- Authors
- Ramella, N. A., Rimoldi, O. J., Prieto, E. D., Schinella, G. R., Sanchez, S. A., Jaureguiberry, M. S., Vela, M. E., Ferreira, S. T., & Tricerri, M. A.
- Affiliations
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- Universidad Nacional de La Plata (AR)
- Universidade Federal do Rio de Janeiro (BR)
- Corresponding author
- Tricerri, M. Alejandra
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2011-07-19
- Volume
- 6
- Issue
- 7
- Pages
- e22532
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3139661
- OpenAlex
- W2085498526
- Cited by
- 66
- References
- 3
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 1 · 2021: 5 · 2020: 10 · 2019: 1 · 2018: 4 · 2017: 7 · 2016: 8 · 2015: 8 · 2014: 3 · 2013: 3 · 2012: 6
- FWCI
- 1.69
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, cc-by)
- Americanae (AECID Library) (submittedVersion, other-oa)
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- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
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- Greater South Information System
- Funders
- Consejo Nacional de Investigaciones Científicas y Técnicas (PIP 112)
- Universidad Nacional de La Plata
- National Institutes of Health
- National Center for Research Resources (P41RR003155, 5P41 RR03155)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Keywords
- apolipoprotein A-I, amyloidosis, atherosclerosis, protein misfolding, protein aggregation, chronic inflammation, low pH, extracellular matrix binding, neutrophils, oxidative cleavage, proteolytic cleavage, atherogenesis
- MeSH terms
- Amyloid, Anilino Naphthalenesulfonates, Animals, Cholesterol, Cricetulus, Cricetinae, Heparin, Humans, Hydrogen-Ion Concentration, Hypochlorous Acid, Oxidation-Reduction, Protein Binding, Solvents, Tetradecanoylphorbol Acetate, Thiazoles, Tryptophan, CHO Cells, Apolipoprotein A-I, Protein Structure, Secondary, Protein Folding, Neutrophil Activation, Protein Structure, Quaternary, Atherosclerosis, Benzothiazoles, Matrix Metalloproteinase 12, Protein Stability, Proteolysis
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