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Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles
The lung provides the main route for nanomaterial exposure. Surfactant protein A (SP-A) is an important respiratory innate immune molecule with the ability to bind or opsonise pathogens to enhance phagocytic removal from the airways. We hypothesised that SP-A, like surfactant protein D, may interact...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Informa Healthcare
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486002/ https://www.ncbi.nlm.nih.gov/pubmed/25676620 http://dx.doi.org/10.3109/17435390.2014.992487 |
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author | McKenzie, Zofi Kendall, Michaela Mackay, Rose-Marie Whitwell, Harry Elgy, Christine Ding, Ping Mahajan, Sumeet Morgan, Cliff Griffiths, Mark Clark, Howard Madsen, Jens |
author_facet | McKenzie, Zofi Kendall, Michaela Mackay, Rose-Marie Whitwell, Harry Elgy, Christine Ding, Ping Mahajan, Sumeet Morgan, Cliff Griffiths, Mark Clark, Howard Madsen, Jens |
author_sort | McKenzie, Zofi |
collection | PubMed |
description | The lung provides the main route for nanomaterial exposure. Surfactant protein A (SP-A) is an important respiratory innate immune molecule with the ability to bind or opsonise pathogens to enhance phagocytic removal from the airways. We hypothesised that SP-A, like surfactant protein D, may interact with inhaled nanoparticulates, and that this interaction will be affected by nanoparticle (NP) surface characteristics. In this study, we characterise the interaction of SP-A with unmodified (U-PS) and amine-modified (A-PS) polystyrene particles of varying size and zeta potential using dynamic light scatter analysis. SP-A associated with both 100 nm U-PS and A-PS in a calcium-independent manner. SP-A induced significant calcium-dependent agglomeration of 100 nm U-PS NPs but resulted in calcium-independent inhibition of A-PS self agglomeration. SP-A enhanced uptake of 100 nm U-PS into macrophage-like RAW264.7 cells in a dose-dependent manner but in contrast inhibited A-PS uptake. Reduced association of A-PS particles in RAW264.7 cells following pre-incubation of SP-A was also observed with coherent anti-Stokes Raman spectroscopy. Consistent with these findings, alveolar macrophages (AMs) from SP-A(−/−) mice were more efficient at uptake of 100 nm A-PS compared with wild type C57Bl/6 macrophages. No difference in uptake was observed with 500 nm U-PS or A-PS particles. Pre-incubation with SP-A resulted in a significant decrease in uptake of 100 nm A-PS in macrophages isolated from both groups of mice. In contrast, increased uptake by AMs of U-PS was observed after pre-incubation with SP-A. Thus we have demonstrated that SP-A promotes uptake of non-toxic U-PS particles but inhibits the clearance of potentially toxic A-PS particles by blocking uptake into macrophages. |
format | Online Article Text |
id | pubmed-4486002 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Informa Healthcare |
record_format | MEDLINE/PubMed |
spelling | pubmed-44860022016-02-24 Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles McKenzie, Zofi Kendall, Michaela Mackay, Rose-Marie Whitwell, Harry Elgy, Christine Ding, Ping Mahajan, Sumeet Morgan, Cliff Griffiths, Mark Clark, Howard Madsen, Jens Nanotoxicology Original Article The lung provides the main route for nanomaterial exposure. Surfactant protein A (SP-A) is an important respiratory innate immune molecule with the ability to bind or opsonise pathogens to enhance phagocytic removal from the airways. We hypothesised that SP-A, like surfactant protein D, may interact with inhaled nanoparticulates, and that this interaction will be affected by nanoparticle (NP) surface characteristics. In this study, we characterise the interaction of SP-A with unmodified (U-PS) and amine-modified (A-PS) polystyrene particles of varying size and zeta potential using dynamic light scatter analysis. SP-A associated with both 100 nm U-PS and A-PS in a calcium-independent manner. SP-A induced significant calcium-dependent agglomeration of 100 nm U-PS NPs but resulted in calcium-independent inhibition of A-PS self agglomeration. SP-A enhanced uptake of 100 nm U-PS into macrophage-like RAW264.7 cells in a dose-dependent manner but in contrast inhibited A-PS uptake. Reduced association of A-PS particles in RAW264.7 cells following pre-incubation of SP-A was also observed with coherent anti-Stokes Raman spectroscopy. Consistent with these findings, alveolar macrophages (AMs) from SP-A(−/−) mice were more efficient at uptake of 100 nm A-PS compared with wild type C57Bl/6 macrophages. No difference in uptake was observed with 500 nm U-PS or A-PS particles. Pre-incubation with SP-A resulted in a significant decrease in uptake of 100 nm A-PS in macrophages isolated from both groups of mice. In contrast, increased uptake by AMs of U-PS was observed after pre-incubation with SP-A. Thus we have demonstrated that SP-A promotes uptake of non-toxic U-PS particles but inhibits the clearance of potentially toxic A-PS particles by blocking uptake into macrophages. Informa Healthcare 2015-11-17 2015-02-13 /pmc/articles/PMC4486002/ /pubmed/25676620 http://dx.doi.org/10.3109/17435390.2014.992487 Text en © 2015 The Author(s). Published by Taylor & Francis. http://creativecommons.org/Licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/Licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article McKenzie, Zofi Kendall, Michaela Mackay, Rose-Marie Whitwell, Harry Elgy, Christine Ding, Ping Mahajan, Sumeet Morgan, Cliff Griffiths, Mark Clark, Howard Madsen, Jens Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title | Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title_full | Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title_fullStr | Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title_full_unstemmed | Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title_short | Surfactant protein A (SP-A) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
title_sort | surfactant protein a (sp-a) inhibits agglomeration and macrophage uptake of toxic amine modified nanoparticles |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486002/ https://www.ncbi.nlm.nih.gov/pubmed/25676620 http://dx.doi.org/10.3109/17435390.2014.992487 |
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