Background: The state of oligomerization of surfactant associated protein-A (SP-A) monomers differs between individuals. This likely affects SP-A's functional properties and could thereby influence clinical status in patients with lung diseases. In this study we focus on SP-A structure in cystic fibrosis (CF) compared to both healthy subjects and disease controls. Methods: SP-A composition and function were assessed in both bronchoalveolar lavage (BAL) fluid and serum of 46 CF patients with mild disease, 25 patients with chronic bronchitis and 22 healthy subjects by gel chromatography and a functional agglutination assay. Relation of SP-A agglutination ability to disease severity of the subjects was explored. Results: SP-A was present in seven major oligomeric forms with the majority of SP-A being structurally organized as complex oligomeric forms. More complex oligomeric forms were associated with better SP-A function with regard to its agglutination ability. These forms were more frequently observed in BAL than in serum, but there were no differences between disease groups. In CF patients, more complex forms of SP-A were associated with better lung function. Conclusions: Organizational structure of SP-A affects its functional activity and is linked to disease severity in CF. © 2012 Griese et al.
Griese, M., Heinrich, S., Ratjen, F., Kabesch, M., Paul, K., Ballmann, M., … Kappler, M. (2012). Surfactant Protein A in Cystic Fibrosis: Supratrimeric Structure and Pulmonary Outcome. PLoS ONE, 7(12). https://doi.org/10.1371/journal.pone.0051050