scholarly journals Enhanced clearance of surfactant protein D during LPS-induced acute inflammation in rat lung

2001 ◽  
Vol 281 (1) ◽  
pp. L268-L277 ◽  
Author(s):  
Joel F. Herbein ◽  
Jo Rae Wright

Pulmonary surfactant participates in the regulation of alveolar compliance and lung host defense. Surfactant homeostasis is regulated through a combination of synthesis, secretion, clearance, recycling, and degradation of surfactant components. The extracellular pool size of surfactant protein (SP) D fluctuates significantly during acute inflammation. We hypothesized that changes in SP-D levels are due, in part, to altered clearance of SP-D. Clearance pathways in rats were assessed with fluorescently labeled SP-D that was instilled into control lungs or lungs that had been treated with lipopolysaccharide (LPS) 16 h earlier. SP-D clearance from lavage into lung tissue was time dependent from 5 min to 1 h and 1.7-fold greater in LPS-treated lungs than in control lungs. Analysis of cells isolated by enzymatic digestion of lung tissue revealed differences in the SP-D-positive cell population between groups. LPS-treated lungs had 28.1-fold more SP-D-positive tissue-associated neutrophils and 193.6-fold greater SP-D association with those neutrophils compared with control lungs. These data suggest that clearance of SP-D into lung tissue is increased during inflammation and that tissue-associated neutrophils significantly contribute to this process.

1994 ◽  
Vol 269 (25) ◽  
pp. 17311-17319 ◽  
Author(s):  
E. Crouch ◽  
A. Persson ◽  
D. Chang ◽  
J. Heuser

2013 ◽  
Vol 5 (3) ◽  
pp. 197-208 ◽  
Author(s):  
Marine L.B. Hillaire ◽  
Henk P. Haagsman ◽  
Albert D.M.E. Osterhaus ◽  
Guus F. Rimmelzwaan ◽  
Martin van Eijk

1998 ◽  
Vol 275 (1) ◽  
pp. L1-L13 ◽  
Author(s):  
Robert J. Mason ◽  
Kelly Greene ◽  
Dennis R. Voelker

Surfactant protein (SP) A and SP-D are collagenous glycoproteins with multiple functions in the lung. Both of these proteins are calcium-dependent lectins and are structurally similar to mannose-binding protein and bovine conglutinin. Both form polyvalent multimeric structures for interactions with pathogens, cells, or other molecules. SP-A is an integral part of the surfactant system, binds phospholipids avidly, and is found in lamellar bodies and tubular myelin. Initially, most research interest focused on its role in surfactant homeostasis. Recently, more attention has been placed on the role of SP-A as a host defense molecule and its interactions with pathogens and phagocytic cells. SP-D is much less involved with the surfactant system. SP-D appears to be primarily a host defense molecule that binds surfactant phospholipids poorly and is not found in lamellar inclusion bodies or tubular myelin. Both SP-A and SP-D bind a wide spectrum of pathogens including viruses, bacteria, fungi, and pneumocystis. In addition, both molecules have been measured in the systemic circulation by immunologic methods and may be useful biomarkers of disease. The current challenges are characterization of the three-dimensional crystal structure of SP-A and SP-D, molecular cloning of their receptors, and determination of their precise physiological functions in vivo.


2000 ◽  
Vol 182 (3) ◽  
pp. 917-922 ◽  
Author(s):  
Bianca A. W. M. van Rozendaal ◽  
Annemiek B. van Spriel ◽  
Jan G. J. van de Winkel ◽  
Henk P. Haagsman

2003 ◽  
Vol 278 (28) ◽  
pp. 25678-25687 ◽  
Author(s):  
Jeya Nadesalingam ◽  
Andrés López Bernal ◽  
Alister W. Dodds ◽  
Antony C. Willis ◽  
David J. Mahoney ◽  
...  

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