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This Article Full Text Full Text (PDF) All Versions of this Article: 287/6/L1145    most recent 00408.2003v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Web of Science (8) Citing Articles via Google Scholar Google Scholar Articles by Nag, K. Articles by Possmayer, F. Search for Related Content PubMed PubMed Citation Articles by Nag, K. Articles by Possmayer, F.

Disparate effects of two phosphatidylcholine binding proteins, C-reactive protein and surfactant protein A, on pulmonary surfactant structure and function

¹Departments of Obstetrics and Gynecology, ²Canadian Institutes of Health Research Group in Fetal and Neonatal Health and Development, and ³Department of Chemistry, University of Western Ontario, London N6A 5A5; ⁶Department of Pathology, St. Joseph's Health Centre, London, Ontario N6A 4V2; ⁷Department of Physiology and Biophysics, University of Calgary, Calgary, Alberta T2N 4N1, Canada; ⁴Departamento de Bioquímica, Instituto Superior de Ciencias Médicas de la Havana-Instituto de Ciencias Básicas y Preclínicas Victoria de Girón, Havana, Cuba; and ⁵Department of Chemistry, Behala College, Calcutta 700 060, West Bengal, India

Submitted 25 November 2003 ; accepted in final form 16 July 2004

C-reactive protein (CRP) and surfactant protein A (SP-A) are phosphatidylcholine (PC) binding proteins that function in the innate host defense system. We examined the effects of CRP and SP-A on the surface activity of bovine lipid extract surfactant (BLES), a clinically applied modified natural surfactant. CRP inhibited BLES adsorption to form a surface-active film and the film's ability to lower surface tension () to low values near 0 mN/m during surface area reduction. The inhibitory effects of CRP were reversed by phosphorylcholine, a water-soluble CRP ligand. SP-A enhanced BLES adsorption and its ability to lower to low values. Small amounts of SP-A blocked the inhibitory effects of CRP. Electron microscopy showed CRP has little effect on the lipid structure of BLES. SP-A altered BLES multilamellar vesicular structure by generating large, loose bilayer structures that were separated by a fuzzy amorphous material, likely SP-A. These studies indicate that although SP-A and CRP both bind PC, there is a difference in the manner in which they interact with surface films.

acute respiratory distress syndrome; captive bubble tensiometer; electron microscopy; surface tension; surfactant biophysical impairment