Surfactant Protein A Inhibits Lipopolysaccharide-Induced Immune Cell Activation by Preventing the Interaction of Lipopolysaccharide with Lipopolysaccharide-Binding Protein

2002 ◽  
Vol 27 (3) ◽  
pp. 353-360 ◽  
Author(s):  
Cordula Stamme ◽  
Mareike Müller ◽  
Lutz Hamann ◽  
Thomas Gutsmann ◽  
Ulrich Seydel
Keyword(s):  
Cell Activation ◽  
Immune Cell ◽  
Binding Protein ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Lipopolysaccharide Binding Protein ◽  
Immune Cell Activation ◽  
Lipopolysaccharide Binding

scholarly journals Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein

2005 ◽  
Vol 391 (1) ◽  
pp. 115-124 ◽  
Author(s):  
Ignacio García-Verdugo ◽  
Fernando Sánchez-Barbero ◽  
Katrin Soldau ◽  
Peter S. Tobias ◽  
Cristina Casals
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Fluorescence Analysis ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Coli Strain ◽  
Surfactant Protein A ◽  
Human Macrophage ◽  
Independent Manner ◽  
Lps Binding

SP-A (surfactant protein A) is a lipid-binding collectin primarily involved in innate lung immunity. SP-A interacts with the bacterial rough LPS (lipopolysaccharide) Re-LPS (Re595 mutant of LPS from Salmonella minnesota), but not with smooth LPS. In the present study, we first examined the characteristics of the interaction of human SP-A with Re-LPS. Fluorescence intensity and anisotropy measurements of FITC-labelled Re-LPS in the presence and absence of SP-A indicated that SP-A bound to Re-LPS in solution in a Ca2+-independent manner, with a dissociation constant of 2.8×10−8 M. In the presence of calcium, a high-mobility complex of SP-A and [3H]Rb-LPS (Rb mutant of LPS from Escherichia coli strain LCD 25) micelles was formed, as detected by sucrose density gradients. Re-LPS aggregation induced by SP-A was further characterized by light scattering. On the other hand, human SP-A inhibited TNF-α (tumour necrosis factor-α) secretion by human macrophage-like U937 cells stimulated with either Re-LPS or smooth LPS. We further examined the effects of human SP-A on the binding of Re-LPS to LBP (LPS-binding protein) and CD14. SP-A decreased the binding of Re-LPS to CD14, but not to LBP, as detected by cross-linking experiments with 125I-ASD-Re-LPS [125I-labelled sulphosuccinimidyl-2-(p-azidosalicylamido)-1,3-dithiopropionate derivative of Re-LPS] and fluorescence analysis with FITC-Re-LPS. When SP-A, LBP and CD14 were incubated together, SP-A reduced the ability of LBP to transfer 125I-ASD-Re-LPS to CD14. These SP-A effects were not due to the ability of SP-A to aggregate Re-LPS in the presence of calcium, since they were observed in both the absence and the presence of calcium. These studies suggest that SP-A could contribute to modulate Re-LPS responses by altering the competence of the LBP–CD14 receptor complex.

Introduction of Mannose Binding Protein-Type Phosphatidylinositol Recognition into Pulmonary Surfactant Protein A†

Biochemistry ◽  
1999 ◽  
Vol 38 (22) ◽  
pp. 7321-7331 ◽  
Author(s):  
Hirofumi Chiba ◽  
Hitomi Sano ◽  
Masaki Saitoh ◽  
Hitoshi Sohma ◽  
Dennis R. Voelker ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Binding Protein ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Mannose Binding Protein ◽  
Mannose Binding ◽  
Pulmonary Surfactant Protein

scholarly journals Lipopolysaccharide-Binding Protein: A New Biomarker for Infectious Endocarditis?

2009 ◽  
Vol 55 (2) ◽  
pp. 295-304 ◽  
Author(s):  
Tanja Vollmer ◽  
Cornelia Piper ◽  
Knut Kleesiek ◽  
Jens Dreier
Keyword(s):  
Binding Protein ◽  
Molecular Genetic ◽  
Protein A ◽  
Response To Therapy ◽  
Infectious Endocarditis ◽  
Therapeutic Monitoring ◽  
Lipopolysaccharide Binding Protein ◽  
Reactive Protein ◽  
Wbc Count ◽  
Lipopolysaccharide Binding

Abstract Background: Infectious endocarditis (IE) is a bacterial infection of the endocardium. Diagnosis is based on results obtained from echocardiography, blood cultures, and molecular genetic screening for bacteria and on data for inflammatory markers such as the leukocyte (WBC) count and the C-reactive protein (CRP) concentration. The aim of the present study was to evaluate lipopolysaccharide-binding protein (LBP) as a supportive biomarker for the diagnosis and therapeutic monitoring of IE. Methods: We measured LBP and CRP concentrations and WBC counts in 57 IE patients at hospital admission, 40 patients with noninfectious heart valve diseases (HVDs), and 55 healthy blood donors. The progression of these 3 markers and the influence of cardiac surgery on them were evaluated in 29 IE patients and 21 control patients. Results: Serum LBP concentrations were significantly higher in IE patients [mean (SD), 33.41 (32.10) mg/L] compared with HVD patients [6.67 (1.82) mg/L, P < 0.0001] and healthy control individuals [5.61 (1.20) mg/L]. The progression in the LBP concentration during therapy of IE patients correlated with the changes in the CRP concentration. The 2 markers were equally influenced by antibiotic treatment and surgical intervention. Conclusions: Serial LBP measurement may provide an effective and useful tool for evaluating the response to therapy in IE patients. We found a strong correlation between LBP and CRP concentrations; LBP has a tendency to increase earlier in cases of reinfection.

Identification and characterization of p63 (CKAP4/ERGIC-63/CLIMP-63), a surfactant protein A binding protein, on type II pneumocytes

2006 ◽  
Vol 291 (3) ◽  
pp. L436-L446 ◽  
Author(s):  
Nisha Gupta ◽  
Yefim Manevich ◽  
Altaf S. Kazi ◽  
Jian-Qin Tao ◽  
Aron B. Fisher ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Type Ii Cells ◽  
Receptor Complex ◽  
Type Ii ◽  
Surface Binding ◽  
Intact Mouse ◽  
The Cross

Surfactant protein A (SP-A) binds to alveolar type II cells through a specific high-affinity cell membrane receptor, although the molecular nature of this receptor is unclear. In the present study, we have identified and characterized an SP-A cell surface binding protein by utilizing two chemical cross-linkers: profound sulfo-SBED protein-protein interaction reagent and dithiobis(succinimidylpropionate) (DSP). Sulfo-SBED-biotinylated SP-A was cross-linked to the plasma membranes isolated from rat type II cells, and the biotin label was transferred from SP-A to its receptor by reduction. The biotinylated SP-A-binding protein was identified on blots by using streptavidin-labeled horseradish peroxidase. By using DSP, we cross-linked SP-A to intact mouse type II cells and immunoprecipitated the SP-A-receptor complex using anti-SP-A antibody. Both of the cross-linking approaches showed a major band of 63 kDa under reduced conditions that was identified as the rat homolog of the human type II transmembrane protein p63 (CKAP4/ERGIC-63/CLIMP-63) by matrix-assisted laser desorption ionization and nanoelectrospray tandem mass spectrometry of tryptic fragments. Thereafter, we confirmed the presence of p63 protein in the cross-linked SP-A-receptor complex by immunoprobing with p63 antibody. Coimmunoprecipitation experiments and functional assays confirmed specific interaction between SP-A and p63. Antibody to p63 could block SP-A-mediated inhibition of ATP-stimulated phospholipid secretion. Both intracellular and membrane localized pools of p63 were detected on type II cells by immunofluorescence and immunobloting. p63 colocalized with SP-A in early endosomes. Thus p63 closely interacts with SP-A and may play a role in the trafficking or the biological function of the surfactant protein.

Old and new findings on lipopolysaccharide-binding protein: a soluble pattern-recognition molecule

2011 ◽  
Vol 39 (4) ◽  
pp. 989-993 ◽  
Author(s):  
Ralf R. Schumann
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Lipopolysaccharide Binding Protein ◽  
New Findings ◽  
Substantial Progress ◽  
Large Protein Family ◽  
Functional Consequences ◽  
Health And Disease ◽  
Lipopolysaccharide Binding ◽  
Key Questions

LBP [LPS (lipopolysaccharide)-binding protein] was discovered approximately 25 years ago. Since then, substantial progress has been made towards our understanding of its function in health and disease. Furthermore, the discovery of a large protein family sharing functional and structural attributes has helped in our knowledge. Still, key questions are unresolved, and here an overview on the old and new findings on LBP is given. LBP is an acute-phase protein of the liver, but is also synthesized in other cells of the organism. While LBP is named after the ability to bind to LPS of Gram-negative bacteria, it also can recognize other bacterial compounds, such as lipopeptides. It has been shown that LBP is needed to combat infections; however, the main mechanism of action is still not clear. New findings on natural genetic variations of LBP leading to functional consequences may help in further elucidating the mechanism of LBP and its role in innate immunity and disease.

Effects of surfactant protein A and surfactant lipids on lymphocyte proliferation in vitro

1994 ◽  
Vol 267 (4) ◽  
pp. L357-L364 ◽  
Author(s):  
S. G. Kremlev ◽  
T. M. Umstead ◽  
D. S. Phelps
Keyword(s):  
Lymphocyte Proliferation ◽  
Cell Function ◽  
Immune Cell ◽  
Pulmonary Inflammation ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Inhibitory Influence ◽  
Surfactant Replacement Therapy

We studied the effects of dipalmitoyl L-alpha-phosphatidylcholine (DPPC), Survanta, surfactant protein A (SP-A), and mixtures of these substances on mitogen-induced lymphocyte proliferation using concanavalin A as a mitogen. A concentration-dependent suppression of proliferation was observed with 50-250 micrograms/ml of DPPC or Survanta. However, when SP-A was added to cultures, proliferation was stimulated. The inhibitory effects of DPPC and Survanta were altered in mixtures that contained SP-A. When added to 50 micrograms/ml of Survanta, SP-A reversed the inhibitory influence of Survanta and caused increased proliferation. These findings suggest that surfactant phospholipids cause a suppression of mitogen-induced lymphocyte proliferation, which is reversed somewhat by addition of SP-A. We hypothesize that immune cell function in the lung varies with changes in the relative amounts of surfactant components. Changes in surfactant composition may occur during pulmonary inflammation or infection or with surfactant replacement therapy and may influence immune and inflammatory processes in the lung.

Is lipopolysaccharide-binding protein a useful marker for systemic infection on the ICU?

2001 ◽  
Vol 18 (Supplement 21) ◽  
pp. 119-120
Author(s):  
A. Nierhaus ◽  
B. Montag ◽  
D. Frings ◽  
N. Suerhoff ◽  
J. Schulte am Esch
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Systemic Infection ◽  
Lipopolysaccharide Binding Protein ◽  
Lipopolysaccharide Binding

Surfactant protein A differentially regulates peripheral and inflammatory neutrophil chemotaxis

2003 ◽  
Vol 284 (1) ◽  
pp. L140-L147 ◽  
Author(s):  
Trista L. Schagat ◽  
Jessica A. Wofford ◽  
Kelly E. Greene ◽  
Jo Rae Wright
Keyword(s):  
Actin Polymerization ◽  
Immune Cell ◽  
Protein A ◽  
Neutrophil Migration ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Boyden Chamber ◽  
Neutrophil Chemotaxis ◽  
Complement Protein ◽  
Homologous Proteins

Surfactant protein A (SP-A), a pulmonary lectin, plays an important role in regulating innate immune cell function. Besides accelerating pathogen clearance by pulmonary phagocytes, SP-A also stimulates alveolar macrophage chemotaxis and directed actin polymerization. We hypothesized that SP-A would also stimulate neutrophil chemotaxis. With the use of a Boyden chamber assay, we found that SP-A (0.5–25 μg/ml) did not stimulate chemotaxis of rat peripheral neutrophils or inflammatory bronchoalveolar lavage (BAL) neutrophils isolated from LPS-treated lungs. However, SP-A affected neutrophil chemotaxis toward the bacterial peptide formyl-met-leu-phe (fMLP). Surprisingly, the effect was different for the two neutrophil populations: SP-A reduced peripheral neutrophil chemotaxis toward fMLP (49 ± 5% fMLP alone) and enhanced inflammatory BAL neutrophil chemotaxis (277 ± 48% fMLP alone). This differential effect was not seen for the homologous proteins mannose binding lectin and complement protein 1q but was recapitulated by type IV collagen. SP-A bound both neutrophil populations comparably and did not alter formyl peptide binding. These data support a role for SP-A in regulating neutrophil migration in pulmonary tissue.

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