Assessment of Surfactant Protein A (SP-A) dependent agglutination

BACKGROUND: Monomers of the collectin surfactant associated protein-A (SP-A) are arranged in trimers and higher oligomers. The state of oligomerization differs between individuals and likely affects SP-A's functional properties. SP-A can form aggregates together with other SP-A molecules. Here...

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Autores principales: Heinrich, Stefanie M, Griese, Matthias
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2995781/
https://www.ncbi.nlm.nih.gov/pubmed/21092225
http://dx.doi.org/10.1186/1471-2466-10-59
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author Heinrich, Stefanie M
Griese, Matthias
author_facet Heinrich, Stefanie M
Griese, Matthias
author_sort Heinrich, Stefanie M
collection PubMed
description BACKGROUND: Monomers of the collectin surfactant associated protein-A (SP-A) are arranged in trimers and higher oligomers. The state of oligomerization differs between individuals and likely affects SP-A's functional properties. SP-A can form aggregates together with other SP-A molecules. Here we report and assess a test system for the aggregate forming properties of SP-A in serum and broncho-alveolar lavage samples. METHODS: Anti-SP-A antibodies fixed to latex beads bound SP-A at its N-terminal end and allowed the interaction with other SP-A molecules in a given sample by their C-terminal carbohydrate recognition domain (CRD) to agglutinate the beads to aggregates, which were quantified by light microscopy. RESULTS: SP-A aggregation was dependent on its concentration, the presence of calcium, and was dose-dependently inhibited by mannose. Unaffected by the presence of SP-D no aggregation was observed in absence of SP-A. The more complex the oligomeric structure of SP-A present in a particular sample, the better was its capability to induce aggregation at a given total concentration of SP-A. SP-A in serum agglutinated independently of the pulmonary disease; in contrast SP-A in lung lavage fluid was clearly inferior in patients with chronic bronchitis and particularly with cystic fibrosis compared to controls. CONCLUSIONS: The functional status of SP-A with respect to its aggregating properties in serum and lavage samples can be easily assessed. SP-A in lung lavage fluid in patients with severe neutrophilic bronchitis was inferior.
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spelling pubmed-29957812010-12-02 Assessment of Surfactant Protein A (SP-A) dependent agglutination Heinrich, Stefanie M Griese, Matthias BMC Pulm Med Research Article BACKGROUND: Monomers of the collectin surfactant associated protein-A (SP-A) are arranged in trimers and higher oligomers. The state of oligomerization differs between individuals and likely affects SP-A's functional properties. SP-A can form aggregates together with other SP-A molecules. Here we report and assess a test system for the aggregate forming properties of SP-A in serum and broncho-alveolar lavage samples. METHODS: Anti-SP-A antibodies fixed to latex beads bound SP-A at its N-terminal end and allowed the interaction with other SP-A molecules in a given sample by their C-terminal carbohydrate recognition domain (CRD) to agglutinate the beads to aggregates, which were quantified by light microscopy. RESULTS: SP-A aggregation was dependent on its concentration, the presence of calcium, and was dose-dependently inhibited by mannose. Unaffected by the presence of SP-D no aggregation was observed in absence of SP-A. The more complex the oligomeric structure of SP-A present in a particular sample, the better was its capability to induce aggregation at a given total concentration of SP-A. SP-A in serum agglutinated independently of the pulmonary disease; in contrast SP-A in lung lavage fluid was clearly inferior in patients with chronic bronchitis and particularly with cystic fibrosis compared to controls. CONCLUSIONS: The functional status of SP-A with respect to its aggregating properties in serum and lavage samples can be easily assessed. SP-A in lung lavage fluid in patients with severe neutrophilic bronchitis was inferior. BioMed Central 2010-11-22 /pmc/articles/PMC2995781/ /pubmed/21092225 http://dx.doi.org/10.1186/1471-2466-10-59 Text en Copyright ©2010 Heinrich and Griese; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Heinrich, Stefanie M
Griese, Matthias
Assessment of Surfactant Protein A (SP-A) dependent agglutination
title Assessment of Surfactant Protein A (SP-A) dependent agglutination
title_full Assessment of Surfactant Protein A (SP-A) dependent agglutination
title_fullStr Assessment of Surfactant Protein A (SP-A) dependent agglutination
title_full_unstemmed Assessment of Surfactant Protein A (SP-A) dependent agglutination
title_short Assessment of Surfactant Protein A (SP-A) dependent agglutination
title_sort assessment of surfactant protein a (sp-a) dependent agglutination
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2995781/
https://www.ncbi.nlm.nih.gov/pubmed/21092225
http://dx.doi.org/10.1186/1471-2466-10-59
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