scholarly journals Human Surfactant Protein – A Gene Locus for Genetic Studies in the Finnish Population

2000 ◽  
Vol 16 (3-4) ◽  
pp. 119-124 ◽  
Author(s):  
Mika Rämet ◽  
Ritva Haataja ◽  
Riitta Marttila ◽  
Anu-Maaria Häamäaläainen ◽  
Mikael Knip ◽  
...  
Keyword(s):  
Gene Locus ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Pulmonary Diseases ◽  
Surfactant Protein A ◽  
Single Amino Acid ◽  
Finnish Population ◽  
Genetic Studies ◽  
New Alleles

Lung surfactant lowers the surface tension but surfactant proteins also have other functions. Surfactant protein A (SP-A) has a well-defined role in innate immunity. The gene locus for human SP-A genes is in chromosome 10q21 through q24 and consists of two highly homologous functional SP-A genes (SP-A1 and SP-A2) and a pseudogene. Several alleles that differ by a single amino acid have been identified for both SP-A genes. The SP-A gene locus has been shown to be sufficiently polymorphic for genetic studies in the American population. In this study, we analysed the SP-A allele frequencies in a Finnish population (n= 790) and found them to differ from the frequencies observed in US. Furthermore, we describe several new alleles for both SP-A genes. The heterozygosity indices and polymorphism information content values ranged between 0.50–0.62 indicating that SP-A gene locus is polymorphic enough for studies associating the locus with pulmonary diseases.

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 gene locus associated with recurrent otitis media

2001 ◽  
Vol 138 (2) ◽  
pp. 266-268 ◽  
Author(s):  
Mika Rämet ◽  
Johan Löfgren ◽  
Olli-Pekka Alho ◽  
Mikko Hallman
Keyword(s):  
Otitis Media ◽  
Gene Locus ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Recurrent Otitis Media

Expression and Localization of Lung Surfactant Protein A in Human Tissues

2003 ◽  
Vol 29 (5) ◽  
pp. 591-597 ◽  
Author(s):  
Jens Madsen ◽  
Ida Tornøe ◽  
Ole Nielsen ◽  
Claus Koch ◽  
Wolfram Steinhilber ◽  
...  
Keyword(s):  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Human Tissues ◽  
Lung Surfactant Protein

Endocytic pathway for surfactant protein A in human macrophages: binding, clathrin-mediated uptake, and trafficking through the endolysosomal pathway

2006 ◽  
Vol 290 (2) ◽  
pp. L334-L342 ◽  
Author(s):  
Joy E. Crowther ◽  
Larry S. Schlesinger
Keyword(s):  
Specific Binding ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Endocytic Pathway ◽  
Surfactant Protein A ◽  
Coated Pits ◽  
Protein Protein Interaction ◽  
Intracellular Compartments ◽  
Over Time

In the noninflamed lung, surfactant protein A (SP-A) acts as an anti-inflammatory molecule through its effects on macrophage (MΦ) function, modulating cytokine and reactive oxygen and nitrogen intermediate production. The receptors responsible for these effects of SP-A on human MΦ are not clear, although SP-A binding to several proteins has been described. In this study, we demonstrate high-affinity specific binding of SP-A to primary human MΦ. SP-A binding was inhibited by EGTA, indicating calcium dependence. However, mannan did not inhibit SP-A binding, suggesting that binding is mediated by a direct protein-protein interaction that does not involve carbohydrate recognition. Our laboratory has previously shown that SP-A is rapidly endocytosed by human MΦ into discrete vesicles. Although previous work indicates that SP-A is ultimately degraded by murine MΦ over time, the trafficking pathway of SP-A through MΦ after uptake has not been reported and is of potential biological importance. We examined trafficking of SP-A in human MΦ by electron and confocal microscopy and show for the first time that SP-A is endocytosed by primary human MΦ through clathrin-coated pits and colocalizes sequentially over time with the early endosome marker EEA1, late endosome marker lamp-1, and lysosome marker cathepsin D. We conclude that SP-A binds to receptor(s) on human MΦ, is endocytosed by a receptor-mediated, clathrin-dependent process, and trafficks through the endolysosomal pathway. These studies provide further insight into the interactions of SP-A with the MΦ cell surface and intracellular compartments that play important roles in SP-A modulation of lung MΦ biology.

scholarly journals Elucidation of Lipid Binding Sites on Lung Surfactant Protein A Using X-ray Crystallography, Mutagenesis, and Molecular Dynamics Simulations

Biochemistry ◽  
2016 ◽  
Vol 55 (26) ◽  
pp. 3692-3701 ◽  
Author(s):  
Boon Chong Goh ◽  
Huixing Wu ◽  
Michael J. Rynkiewicz ◽  
Klaus Schulten ◽  
Barbara A. Seaton ◽  
...  
Keyword(s):  
Binding Sites ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Surfactant Protein A ◽  
X Ray ◽  
X Ray Crystallography ◽  
Lung Surfactant Protein ◽  
Dynamics Simulations
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