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...
Autores principales: | , |
---|---|
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 |
_version_ | 1782193110329065472 |
---|---|
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. |
format | Text |
id | pubmed-2995781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT heinrichstefaniem assessmentofsurfactantproteinaspadependentagglutination AT griesematthias assessmentofsurfactantproteinaspadependentagglutination |