Fluidizing effects of C‐reactive protein on lung surfactant membranes: protective role of surfactant protein A

2010 ◽  
Vol 24 (10) ◽  
pp. 3662-3673 ◽  
Author(s):  
Alejandra Saenz ◽  
Almudena López‐Sánchez ◽  
Jonás Mojica‐Lázaro ◽  
Leticia Martínez‐Caro ◽  
Nicolas Nin ◽  
...  
Keyword(s):  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Protective Role ◽  
Surfactant Protein A ◽  
C Reactive Protein ◽  
Reactive Protein

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

2004 ◽  
Vol 287 (6) ◽  
pp. L1145-L1153 ◽  
Author(s):  
Kaushik Nag ◽  
Karina Rodriguez-Capote ◽  
Amiya Kumar Panda ◽  
Laura Frederick ◽  
Stephen A. Hearn ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Amorphous Material ◽  
Protein A ◽  
Surfactant Protein ◽  
Water Soluble ◽  
Surfactant Protein A ◽  
Surface Films ◽  
Inhibitory Effects ◽  
C Reactive Protein ◽  
Reactive Protein

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 (γ) 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 γ 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.

Increase of C-Reactive Protein and Decrease of Surfactant Protein A in Surfactant after Lung Transplantation

1998 ◽  
Vol 157 (1) ◽  
pp. 43-49 ◽  
Author(s):  
CRISTINA CASALS ◽  
ANDRÉS VARELA ◽  
MIGUEL L. F. RUANO ◽  
FERNANDO VALIÑO ◽  
JESÚS PÉREZ-GIL ◽  
...  
Keyword(s):  
Lung Transplantation ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
C Reactive Protein ◽  
Reactive Protein

scholarly journals Cutting Edge: The Immunostimulatory Activity of the Lung Surfactant Protein-A Involves Toll-Like Receptor 4

2002 ◽  
Vol 168 (12) ◽  
pp. 5989-5992 ◽  
Author(s):  
Loïc Guillot ◽  
Viviane Balloy ◽  
Francis X. McCormack ◽  
Douglas T. Golenbock ◽  
Michel Chignard ◽  
...  
Keyword(s):  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Cutting Edge ◽  
Surfactant Protein A ◽  
Toll Like Receptor ◽  
Immunostimulatory Activity ◽  
Toll Like Receptor 4 ◽  
Lung Surfactant Protein

Surfactant protein A prevents silica-mediated toxicity to rat alveolar macrophages

2000 ◽  
Vol 278 (4) ◽  
pp. L713-L718 ◽  
Author(s):  
Robert W. Spech ◽  
Paul Wisniowski ◽  
Diane L. Kachel ◽  
Jo Rae Wright ◽  
William J. Martin
Keyword(s):  
Cell Injury ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Occupational Lung Disease ◽  
Direct Injury ◽  
Surfactant Apoprotein ◽  
Surfactant Apoprotein A ◽  
Cytotoxic Index

Silicosis is a serious occupational lung disease associated with irreversible pulmonary fibrosis. The interaction between inhaled crystalline silica and the alveolar macrophage (AM) is thought to be a key event in the development of silicosis and fibrosis. Silica can cause direct injury to AMs and can induce AMs to release various inflammatory mediators. Acute silicosis is also characterized by a marked elevation in surfactant apoprotein A (SP-A); however, the role of SP-A in silicosis is unknown. We investigated whether SP-A directly affects the response of AMs to silica. In this study, the degree of silica toxicity to cultured rat AMs as assessed by a 51Cr cytotoxicity assay was shown to be dependent on the time of exposure and the concentration and size of the silica particles. Silica directly injured rat AMs as evidenced by a cytotoxic index of 32.9 ± 2.5, whereas the addition of rat SP-A (5 μg/ml) significantly reduced the cytotoxic index to 16.6 ± 1.2 ( P < 0.001). This effect was reversed when SP-A was incubated with either polyclonal rabbit anti-rat SP-A antibody ord-mannose. These data indicate that SP-A mitigates the effect of silica on AM viability, and this effect may involve the carbohydrate recognition domain of SP-A. The elevation of SP-A in acute silicosis may serve as a normal host response to prevent lung cell injury after exposure to silica.

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